|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
13-566 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 1161.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 13 TAKIWLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMM 92
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 93 PNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGA 172
Cdd:PRK07059 81 PNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLGFKGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 173 IVNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWL 252
Cdd:PRK07059 161 IVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 253 NTAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSE 332
Cdd:PRK07059 241 QPAFEKKPRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 FRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRT 412
Cdd:PRK07059 321 FDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGND 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 413 LPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATH 492
Cdd:PRK07059 401 LPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASH 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 493 PGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK07059 481 PGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
15-565 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 824.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 15 KIWLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQS-LGLAKGDRVAVMMP 93
Cdd:PRK08974 3 KVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 94 NILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLG-AKGA 172
Cdd:PRK08974 83 NLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLStAKGT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 173 IVNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElWL 252
Cdd:PRK08974 163 LVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAK-AA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 253 NTAFLRKPRPESLTfmcALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSE 332
Cdd:PRK08974 242 YGPLLHPGKELVVT---ALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 FRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRT 412
Cdd:PRK08974 319 FQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 413 LPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATH 492
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLH 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271215 493 PGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK08974 478 PKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
17-565 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 726.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 17 WLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSL-GLAKGDRVAVMMPNI 95
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 96 LQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGA-KGAIV 174
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPlKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 175 NLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQ----MEL 250
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcralMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 251 WLNTAflrkprpeSLTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNN 330
Cdd:PRK05677 246 NLNEG--------CEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 331 SEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFtGTIGIPLPSTEVEIRDEDG 410
Cdd:PRK05677 318 EAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 411 RTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAA 490
Cdd:PRK05677 397 NELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 491 THPGILECAAIGVADPHSGEAVKLFVVRK-DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK05677 477 ALPGVLQCAAIGVPDEKSGEAIKVFVVVKpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
12-565 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 721.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 12 STAKIWLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWL-QSLGLAKGDRVAV 90
Cdd:PRK08751 2 SQARPWLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlGELQLKKGDRVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 91 MMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLG-A 169
Cdd:PRK08751 82 MMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGfP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 170 KGAIVNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQME 249
Cdd:PRK08751 162 KAALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 250 LWLNTAFLRKPRPEslTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN 329
Cdd:PRK08751 242 QWLAGTGKLEEGCE--VVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 330 NSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDED 409
Cdd:PRK08751 320 TPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 410 GRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVA 489
Cdd:PRK08751 400 GTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVI 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 490 ATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK08751 480 AMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
14-565 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 661.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 14 AKIWLGSYPPGVPAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQS-LGLAKGDRVAVMM 92
Cdd:PRK12492 3 PDFWNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 93 PNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDML-GAKG 171
Cdd:PRK12492 83 PNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLpAAKG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 172 AIVNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElw 251
Cdd:PRK12492 163 WLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVR-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 252 lntAFLRKPRPESLTFM--------CALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTL 323
Cdd:PRK12492 241 ---ACLSQLGPDGQPLMkegqevmiAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 324 FNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEV 403
Cdd:PRK12492 318 FVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 404 EIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPN 483
Cdd:PRK12492 398 KVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 484 EIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKD 563
Cdd:PRK12492 478 EIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRE 557
|
..
gi 499271215 564 LR 565
Cdd:PRK12492 558 LR 559
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
37-565 |
0e+00 |
|
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: 644.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 37 IGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVN 116
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 117 PLYTPRELEHQLVDAGAKAIFVLEnfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlSF 196
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAV------------------------------------------------------SF 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 197 KTVLAKGATLGFkRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrkPRPESLTFMCALPLYHI 276
Cdd:cd05936 107 TDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLED-----LLEGDDVVLAALPLFHV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 277 FALTVNSLMGLATGGNNILIPNPRDIpAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVA 356
Cdd:cd05936 181 FGLTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 357 ERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRP 436
Cdd:cd05936 260 ERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRP 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 437 EETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV 516
Cdd:cd05936 340 EETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFV 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 499271215 517 VRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05936 419 VLKEgASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
37-565 |
0e+00 |
|
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: 536.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 37 IGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVN 116
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 117 PLYTPRELEHQLVDAGAKAIFVlenfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsf 196
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 197 ktvlakgatlgfkrpnvapgdvAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaflrkPRPESlTFMCALPLYHI 276
Cdd:COG0318 103 ----------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG------LTPGD-VVLVALPLFHV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 277 FALTVNSLMGLATGGNNILIPNpRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVA 356
Cdd:COG0318 154 FGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 357 ERWLELTGCPIHEGYGLSETSPVATANRLDT-DDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQR 435
Cdd:COG0318 233 ERFEERFGVRIVEGYGLTETSPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWND 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 436 PEETARAIsPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLF 515
Cdd:COG0318 313 PEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAF 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499271215 516 VVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:COG0318 392 VVLRPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALR 442
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
7-565 |
1.98e-156 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 459.47 E-value: 1.98e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 7 QQAGSSTA-KIWLGSYPPGVPAEIgPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKG 85
Cdd:PRK05605 4 SQEMSAFAdKPWLQSYAPWTPHDL-DYGDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 86 DRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGD 165
Cdd:PRK05605 83 DRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 166 -MLGAKGAIVNLVVRRVKKLVPAWSI--PGHLSFKTVLAK---GATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHA 239
Cdd:PRK05605 163 aMPLLQRLALRLPIPALRKARAALTGpaPGTVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 240 NLLSNMAQMELWLNTafLRKpRPEslTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPrDIPAFVKELGRYRTNIFPG 319
Cdd:PRK05605 243 NLFANAAQGKAWVPG--LGD-GPE--RVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 320 LNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLP 399
Cdd:PRK05605 317 VPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 400 STEVEIRDED--GRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSG 477
Cdd:PRK05605 397 DTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIRIVDRIKELIITGG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 478 FNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNV 556
Cdd:PRK05605 476 FNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQL 555
|
....*....
gi 499271215 557 GKILRKDLR 565
Cdd:PRK05605 556 GKVRRREVR 564
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
35-566 |
1.34e-142 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 422.01 E-value: 1.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTE-VKHVVVASMGDmlgakgaivnlvvrrvkklvPAWSIPGH 193
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPaLEHVVICETEE--------------------DDPHTEKM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 LSFKTVLAKGATlGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelWLNTAFLRkprpESLTFMCALPL 273
Cdd:PRK07656 145 KTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAAD---WAEYLGLT----EGDRYLAANPF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 YHIFALTVNSLMGLATGGnnILIPNPRDIPAFVKEL-GRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVq 352
Cdd:PRK07656 217 FHVFGYKAGVNAPLMRGA--TILPLPVFDPDEVFRLiETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASM- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 353 rPVA--ERWLELTGCP-IHEGYGLSETSPVATANRLDTD--DFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQ 427
Cdd:PRK07656 294 -PVAllERFESELGVDiVLTGYGLSEASGVTTFNRLDDDrkTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 428 VMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPH 507
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 508 SGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK07656 453 LGEVGKAYVVLKPgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
15-564 |
1.93e-134 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 402.87 E-value: 1.93e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 15 KIWLGSYPPGVPAEIGPLTyRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPN 94
Cdd:PRK06710 5 KPWLKSYPEEIPSTISYDI-QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 95 ILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLG-AKGAI 173
Cdd:PRK06710 84 CPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPfPKNLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 174 VNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLN 253
Cdd:PRK06710 164 YPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 254 TAflrkpRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIPNpRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEF 333
Cdd:PRK06710 244 NC-----KEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPK-FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 RKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRD-EDGRT 412
Cdd:PRK06710 318 KEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 413 LPVGEIGEICIRGPQVMAGYWQRPEETArAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATH 492
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271215 493 PGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
31-565 |
6.65e-132 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 394.94 E-value: 6.65e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 31 PLTyrsIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGF 110
Cdd:PRK06187 5 PLT---IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 111 TVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTE-VKHVVVASMGDMLGAkgaivnlvvrrvkklvpaws 189
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPL-------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 190 IPGHLSFKTVLAKGATLgFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaFLRKPRpesltFMC 269
Cdd:PRK06187 142 APEVGEYEELLAAASDT-FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK--LSRDDV-----YLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 270 ALPLYHIFALTVnSLMGLATGGNNILipnPRDIPA--FVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGG 347
Cdd:PRK06187 214 IVPMFHVHAWGL-PYLALMAGAKQVI---PRRFDPenLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 GMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDD-----FTGTIGIPLPSTEVEIRDEDGRTLPV--GEIGE 420
Cdd:PRK06187 290 GAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQLpgqwtKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 421 ICIRGPQVMAGYWQRPEETARAIsPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:PRK06187 370 IIVRGPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 501 IGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK06187 449 IGVPDEKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
41-561 |
2.81e-130 |
|
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: 387.74 E-value: 2.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 41 FDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYT 120
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 121 PRELEHQLVDAGAKAIFvlenfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvl 200
Cdd:cd17631 81 PPEVAYILADSGAKVLF--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 201 akgatlgfkrpnvapGDVAFLQYTGGTTGVSKGATLTHANLLSNMaqmelwLNTAFLRKPRPESLtFMCALPLYHIFALT 280
Cdd:cd17631 98 ---------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA------VNALAALDLGPDDV-LLVVAPLFHIGGLG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 281 VNSLMGLATGGNNILIPNPrDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWL 360
Cdd:cd17631 156 VFTLPTLLRGGTVVILRKF-DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 ElTGCPIHEGYGLSETSPVATANRL-DTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:cd17631 235 A-RGVKFVQGYGMTETSPGVTFLSPeDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK 519
Cdd:cd17631 314 AAAFR-DGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPR 392
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499271215 520 DPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:cd17631 393 PGAeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
41-476 |
6.05e-126 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 375.88 E-value: 6.05e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 41 FDHAVAQYSWRPAFTCM-GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLY 119
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 120 TPRELEHQLVDAGAKAIFVLENF--AHTVEQVLARTEVKHVVVASMGDMLGAKGAIVNLVVRRVKKLVPAWsipghlsfk 197
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALklEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPP--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 198 tvlakgatlgfkrpnVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAFlrkPRPESLTFMCALPLYHIF 277
Cdd:pfam00501 152 ---------------PDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGF---GLGPDDRVLSTLPLFHDF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 278 ALTVNSLMGLATGGNNILIP--NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPV 355
Cdd:pfam00501 214 GLSLGLLGPLLAGATVVLPPgfPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWLELTGCPIHEGYGLSETSPVATANRLDTDDFT--GTIGIPLPSTEVEIRDED-GRTLPVGEIGEICIRGPQVMAGY 432
Cdd:pfam00501 294 ARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRslGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGY 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 499271215 433 WQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS 476
Cdd:pfam00501 374 LNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
58-560 |
1.88e-124 |
|
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: 374.63 E-value: 1.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLEnfaHTVEQVLARTEvkhvvvasmgdmlgAKGAIVNLVVRRVKklVPAWSIPGHLSFKTVLAKGATLgFKRPNVAPGD 217
Cdd:cd05911 88 TDP---DGLEKVKEAAK--------------ELGPKDKIIVLDDK--PDGVLSIEDLLSPTLGEEDEDL-PPPLKDGKDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAFLRKPRpesltFMCALPLYHIFALtvNSLMGLATGGNNILIP 297
Cdd:cd05911 148 TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSNDV-----ILGFLPLYHIYGL--FTTLASLLNGATVIIM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYR---TNIFPglnTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL-TGCPIHEGYGL 373
Cdd:cd05911 221 PKFDSELFLDLIEKYKitfLYLVP---PIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 374 SETSPVATANrLDTDDFTGTIGIPLPSTEVEIRDEDGRT-LPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTG 452
Cdd:cd05911 298 TETGGILTVN-PDGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 453 DVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRH 531
Cdd:cd05911 377 DIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTEKEVKDY 456
|
490 500 510
....*....|....*....|....*....|
gi 499271215 532 CAASLTNYKRPRY-VEFRTELPKSNVGKIL 560
Cdd:cd05911 457 VAKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
32-560 |
4.57e-120 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 365.44 E-value: 4.57e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 32 LTYRSIGEFFDHAVA--QYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQS-LGLAKGDRVAVMMPNILQNPVIVYGILRA 108
Cdd:PRK08314 5 LTLPETSLFHNLEVSarRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 109 GFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGAIVNLVVRRVKKLVPAW 188
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAVPAWLRAEPPLQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 189 SIPGHLSFKTVLAKGATLGfkrP-NVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESlTF 267
Cdd:PRK08314 165 APGGVVAWKEALAAGLAPP---PhTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST------PES-VV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 268 MCALPLYHIFALtVNSLMGLATGGNNILIpNPR-DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFG 346
Cdd:PRK08314 235 LAVLPLFHVTGM-VHSMNAPIYAGATVVL-MPRwDREAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 347 GGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDfTGTIGIPLPSTEVEIRD-EDGRTLPVGEIGEICIRG 425
Cdd:PRK08314 313 GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPK-LQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 426 PQVMAGYWQRPEETARA-ISPDG--FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIG 502
Cdd:PRK08314 392 PQVFKGYWNRPEATAEAfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271215 503 VADPHSGEAVKLFVVRKDP---NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:PRK08314 472 TPDPRRGETVKAVVVLRPEargKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
217-560 |
1.47e-118 |
|
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: 353.90 E-value: 1.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLntaflrkPRPESLTFMCALPLYHIFALTVNsLMGLATGGNNILI 296
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG-------GLTEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PnPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSET 376
Cdd:cd04433 73 P-KFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTET 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 377 SPVATANRLDTDDF-TGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETArAISPDGFFRTGDVG 455
Cdd:cd04433 152 GGTVATGPPDDDARkPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 456 FMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDP-NLTEEEVKRHCAA 534
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGaDLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 499271215 535 SLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
44-564 |
2.36e-111 |
|
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: 341.52 E-value: 2.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 44 AVAQYSWRPAF----TcmGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLY 119
Cdd:cd05904 14 FASAHPSRPALidaaT--GRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 120 TPRELEHQLVDAGAKAIFvlenfahTVEQVLARTEVKHVVVASMGdmlgakgaivnlvvrrvkklvpawSIPGHLSFKTV 199
Cdd:cd05904 92 TPAEIAKQVKDSGAKLAF-------TTAELAEKLASLALPVVLLD------------------------SAEFDSLSFSD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 200 LAKGATLGFK-RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwLNTAFLRKPRPESlTFMCALPLYHIFA 278
Cdd:cd05904 141 LLFEADEAEPpVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQ----FVAGEGSNSDSED-VFLCVLPMFHIYG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 279 LTVnSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAER 358
Cdd:cd05904 216 LSS-FALGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 359 WLE-LTGCPIHEGYGLSETSPVATANRLDTDDFT--GTIGIPLPSTEVEIRD-EDGRTLPVGEIGEICIRGPQVMAGYWQ 434
Cdd:cd05904 295 FRAkFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkyGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 435 RPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKL 514
Cdd:cd05904 375 NPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMA 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499271215 515 FVVRK-DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05904 455 FVVRKpGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
17-564 |
1.01e-106 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 331.62 E-value: 1.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 17 WLGSYPPGVPAE-IGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNI 95
Cdd:PRK06178 14 QQAAWPAGIPREpEYPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 96 LQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGAIVn 175
Cdd:PRK06178 94 PQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 176 lvvrrVKKLV--PAWSIPGHLSFKTVLAkGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlN 253
Cdd:PRK06178 173 -----LPDSLraPRLAAAGAIDLLPALR-ACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAA------A 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 254 TAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIpNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEF 333
Cdd:PRK06178 241 AYAVAVVGGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLL-ARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 RKLDFSSLILTfgggMAVQ------RPVAERWLELTGCPIHEG-YGLSETSPVATANR-LDTDDFTGT-----IGIPLPS 400
Cdd:PRK06178 320 AEYDLSSLRQV----RVVSfvkklnPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAgFQDDDFDLLsqpvfVGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 401 TEVEIRDED-GRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFN 479
Cdd:PRK06178 396 TEFKICDFEtGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 480 VFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRyVEFRTELPKSNVGK 558
Cdd:PRK06178 475 VFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGK 553
|
....*.
gi 499271215 559 ILRKDL 564
Cdd:PRK06178 554 VRKQDL 559
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
61-564 |
1.97e-100 |
|
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: 310.95 E-value: 1.97e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAifvle 140
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfahtveqvlartevkhVVVASMGDmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapgDVAF 220
Cdd:cd05935 77 -----------------AVVGSELD---------------------------------------------------DLAL 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprpESLTFMCALPLYHIfALTVNSLMGLATGGNNILIPNPR 300
Cdd:cd05935 89 IPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLT-------PSDVILACLPLFHV-TGFVGSLNTAVYVGGTYVLMARW 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 301 DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVA 380
Cdd:cd05935 161 DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQT 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 381 TANRLDTDDFTgTIGIPLPSTEVEIRD-EDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDG---FFRTGDVGF 456
Cdd:cd05935 241 HTNPPLRPKLQ-CLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGY 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 457 MNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDP---NLTEEEVKRHCA 533
Cdd:cd05935 320 MDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWAR 399
|
490 500 510
....*....|....*....|....*....|.
gi 499271215 534 ASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05935 400 EQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
59-565 |
1.20e-97 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 307.81 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFV 138
Cdd:COG0365 38 RTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 139 ---------LENFAHTVEQVLARTE-VKHVVVasmgdmlgakgaivnlvvrrVKKLVPAWSIPGHLSFKTVLAKGATLgF 208
Cdd:COG0365 118 adgglrggkVIDLKEKVDEALEELPsLEHVIV--------------------VGRTGADVPMEGDLDWDELLAAASAE-F 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 209 KRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMA-QMELWLNtaflrkPRPESlTFMCALPLYHIFALTvNSLMG- 286
Cdd:COG0365 177 EPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLD------LKPGD-VFWCTADIGWATGHS-YIVYGp 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGGNNIL---IPNPRDIPAFVKELGRYRTNIF---PglnTLFNALMNNSEF--RKLDFSSLILTFGGGMAVQRPVAER 358
Cdd:COG0365 249 LLNGATVVLyegRPDFPDPGRLWELIEKYGVTVFftaP---TAIRALMKAGDEplKKYDLSSLRLLGSAGEPLNPEVWEW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 359 WLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQ--VMAGYWQRP 436
Cdd:COG0365 326 WYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 437 EETARAI--SPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKL 514
Cdd:COG0365 406 ERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKA 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 515 FVVRKDP-NLTEE---EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:COG0365 486 FVVLKPGvEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLR 540
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
31-559 |
4.41e-97 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 306.35 E-value: 4.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 31 PLTYRSIGEFFDHAVAQYSWRPA--FTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRA 108
Cdd:PRK08315 12 PLLEQTIGQLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 109 GFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENF-----AHTVEQVlaRTEVKHvvvASMGDMLGAKGAIVNLVVRrvkk 183
Cdd:PRK08315 92 GAILVTINPAYRLSELEYALNQSGCKALIAADGFkdsdyVAMLYEL--APELAT---CEPGQLQSARLPELRRVIF---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 184 lVPAWSIPGHLSFKTVLAKG-----ATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSN-----MAQmelwln 253
Cdd:PRK08315 163 -LGDEKHPGMLNFDELLALGravddAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNgyfigEAM------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 254 tAFLRKPRpesltfMC-ALPLYHIFALtVNSLMGLATGGNNILIPNPRDIPAFV-----KElgryRTNIFPGLNTLFNAL 327
Cdd:PRK08315 236 -KLTEEDR------LCiPVPLYHCFGM-VLGNLACVTHGATMVYPGEGFDPLATlaaveEE----RCTALYGVPTMFIAE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 328 MNNSEFRKLDFSSLiltFGGGMA-------VQRPVAERW--LELTGCpihegYGLSETSPVATANRLDtDDF---TGTIG 395
Cdd:PRK08315 304 LDHPDFARFDLSSL---RTGIMAgspcpieVMKRVIDKMhmSEVTIA-----YGMTETSPVSTQTRTD-DPLekrVTTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 396 IPLPSTEVEIRDED-GRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMIL 474
Cdd:PRK08315 375 RALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMII 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 475 VSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPK 553
Cdd:PRK08315 455 RGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPM 534
|
....*.
gi 499271215 554 SNVGKI 559
Cdd:PRK08315 535 TVTGKI 540
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
36-565 |
1.18e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 298.77 E-value: 1.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 36 SIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNV 115
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 116 NPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGaivnlvvrrvkklvpawsipGHLS 195
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPG--------------------GWLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 196 FKTVLAKGATLGFkRPNVAPGDVAFLQYTGGTTGVSKGATLTH----ANLLSNMAQMELWLNTAFLRkprpesltfmcAL 271
Cdd:PRK08316 152 FADWAEAGSVAEP-DVELADDDLAQILYTSGTESLPKGAMLTHraliAEYVSCIVAGDMSADDIPLH-----------AL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 272 PLYHIFALTVNSLMGLATGGNNILIPNPrDIPAFVKELGRYR-TNIF--PglnTLFNALMNNSEFRKLDFSSLILTFGGG 348
Cdd:PRK08316 220 PLYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERiTSFFapP---TVWISLLRHPDFDTRDLSSLRKGYYGA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 349 MAVQRPVAERWLE-LTGCPIHEGYGLSETSPVATANRL-DTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGP 426
Cdd:PRK08316 296 SIMPVEVLKELRErLPGLRFYNCYGQTEIAPLATVLGPeEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSP 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 427 QVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADP 506
Cdd:PRK08316 376 QLMLGYWDDPEKTAEAFR-GGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 507 HSGEAVKLFVVRKDPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK08316 455 KWIEAVTAVVVPKAGAtVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELR 514
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
58-565 |
8.08e-92 |
|
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: 290.37 E-value: 8.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENfahtveqvlarTEVKHVVVASMGDMlgakgAIVNLVVR--RVKKLVPAWSIPGHLSFKTVLAKgatlgfkRPNVAP 215
Cdd:cd05926 92 TPKG-----------ELGPASRAASKLGL-----AILELALDvgVLIRAPSAESLSNLLADKKNAKS-------EGVPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 216 GDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlNTAflrkpRPESLTF----MCALPLYHIFALTVNSLMGLATGG 291
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASAT------NIT-----NTYKLTPddrtLVVMPLFHVHGLVASLLSTLAAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 292 NnILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNN------SEFRKLDF---SSLILTfgggmavqrPVAERWLEL 362
Cdd:cd05926 218 S-VVLPPRFSASTFWPDVRDYNATWYTAVPTIHQILLNRpepnpeSPPPKLRFirsCSASLP---------PAVLEALEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 T-GCPIHEGYGLSETSPVATANRLDTD-DFTGTIGIPLpSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETA 440
Cdd:cd05926 288 TfGAPVLEAYGMTEAAHQMTSNPLPPGpRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 441 RAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RK 519
Cdd:cd05926 367 EAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlRE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499271215 520 DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05926 447 GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVA 492
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
20-565 |
1.54e-89 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 286.67 E-value: 1.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 20 SYPPGVPAEigPLTYRSIGEFFDHAVAQYSWRPA--FTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQ 97
Cdd:PRK12583 5 SYYQGGGDK--PLLTQTIGDAFDATVARFPDREAlvVRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 98 NPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFahtveqvlaRTEVKHVVVASM--GDMLGAKGAIVN 175
Cdd:PRK12583 83 WLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAF---------KTSDYHAMLQELlpGLAEGQPGALAC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 176 L---VVRRVKKLVPAwSIPGHLSFKTVLAKGATLGFKRPNVA-----PGDVAFLQYTGGTTGVSKGATLTHANLLSN--M 245
Cdd:PRK12583 154 ErlpELRGVVSLAPA-PPPGFLAWHELQARGETVSREALAERqasldRDDPINIQYTSGTTGFPKGATLSHHNILNNgyF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 246 AQMELWLNtaflrkprpESLTFMCALPLYHIFAlTVNSLMGLATGGNNILIPNPR-DIPAFVKELGRYRTNIFPGLNTLF 324
Cdd:PRK12583 233 VAESLGLT---------EHDRLCVPVPLYHCFG-MVLANLGCMTVGACLVYPNEAfDPLATLQAVEEERCTALYGVPTMF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 325 NALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCP-IHEGYGLSETSPVA--TANRLDTDDFTGTIGIPLPST 401
Cdd:PRK12583 303 IAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 402 EVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVF 481
Cdd:PRK12583 383 EVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 482 PNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:PRK12583 463 PREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQ 542
|
....*
gi 499271215 561 RKDLR 565
Cdd:PRK12583 543 KFRMR 547
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
33-502 |
1.49e-87 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 282.76 E-value: 1.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 33 TYRSIGEFFDHAVAQYSWRPAFTCMG----KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRA 108
Cdd:COG1022 9 PADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 109 GFTVVnvnPLY---TPRELEHQLVDAGAKAIFVlENFAH--TVEQVLART-EVKHVVVASMGDMLGAKGAIvnlvvrrvk 182
Cdd:COG1022 89 GAVTV---PIYptsSAEEVAYILNDSGAKVLFV-EDQEQldKLLEVRDELpSLRHIVVLDPRGLRDDPRLL--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 183 klvpawsipghlSFKTVLAKGATLGFK------RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwLNTAF 256
Cdd:COG1022 156 ------------SLDELLALGREVADPaelearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA----LLERL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 257 LRKPRPESLTFmcaLPLYHIFALTVnSLMGLATGGNNILIPNPRDIPAFVKELG------------RYRTNIF------P 318
Cdd:COG1022 220 PLGPGDRTLSF---LPLAHVFERTV-SYYALAAGATVAFAESPDTLAEDLREVKptfmlavprvweKVYAGIQakaeeaG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 319 GL-NTLFNALMNNSE----------------------FRKLDFSSLILTFG--------GGMAVQRPVAeRWLELTGCPI 367
Cdd:COG1022 296 GLkRKLFRWALAVGRryararlagkspslllrlkhalADKLVFSKLREALGgrlrfavsGGAALGPELA-RFFRALGIPV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYGLSETSPVATANRLDTDDFtGTIGIPLPSTEVEIrdedgrtlpvGEIGEICIRGPQVMAGYWQRPEETARAISPDG 447
Cdd:COG1022 375 LEGYGLTETSPVITVNRPGDNRI-GTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 448 FFRTGDVGFMNAEGLTKIVDRKKDMI-LVSGFNVFPNEIEEVAATHPGILECAAIG 502
Cdd:COG1022 444 WLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
62-565 |
2.91e-87 |
|
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: 276.48 E-value: 2.91e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVlen 141
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 fahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapgDVAFL 221
Cdd:cd05934 82 ---------------------------------------------------------------------------DPASI 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 222 QYTGGTTGVSKGATLTHANLLSnmaqmelWLNTAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIP--NP 299
Cdd:cd05934 87 LYTSGTTGPPKGVVITHANLTF-------AGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPrfSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 300 RdipAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRpvAERWLELTGCPIHEGYGLSETSpV 379
Cdd:cd05934 160 S---RFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPEL--HEEFEERFGVRLLEGYGMTETI-V 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 380 ATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR---GPQVMAGYWQRPEETARAIsPDGFFRTGDVGF 456
Cdd:cd05934 234 GVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 457 MNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAAS 535
Cdd:cd05934 313 RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlRPGETLDPEELFAFCEGQ 392
|
490 500 510
....*....|....*....|....*....|
gi 499271215 536 LTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05934 393 LAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
61-564 |
3.81e-86 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 275.97 E-value: 3.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQ-SLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVL 139
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 ENFAHTVEQVLARTEVKHVV-VASMGDMLGAKgaivnlvvrrvkklvpawsipghlsfktvlakgaTLGFKRPNvapGDV 218
Cdd:PRK06839 108 KTFQNMALSMQKVSYVQRVIsITSLKEIEDRK----------------------------------IDNFVEKN---ESA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQ-YTGGTTGVSKGATLTHANLLSNMaqmelwLNTAFLRKPRPESLTFMCaLPLYHIFALTVNSLMGLATGGNnILIP 297
Cdd:PRK06839 151 SFIIcYTSGTTGKPKGAVLTQENMFWNA------LNNTFAIDLTMHDRSIVL-LPLFHIGGIGLFAFPTLFAGGV-IIVP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLElTGCPIHEGYGLSETS 377
Cdd:PRK06839 223 RKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTETS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 378 PvaTANRLDTDDF---TGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDV 454
Cdd:PRK06839 302 P--TVFMLSEEDArrkVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 455 GFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCA 533
Cdd:PRK06839 379 ARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSsSVLIEKDVIEHCR 458
|
490 500 510
....*....|....*....|....*....|.
gi 499271215 534 ASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK06839 459 LFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
34-565 |
5.22e-86 |
|
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: 275.79 E-value: 5.22e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 34 YRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVV 113
Cdd:cd05959 3 YNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 114 NVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGdmlgakgaivnlvvrrvkklvPAWSIPGH 193
Cdd:cd05959 83 PVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSG---------------------GAGPEAGA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 LSFKTVLAKGATlGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANL---LSNMAQMELWLNtaflrkprpESLTFMCA 270
Cdd:cd05959 142 LLLAELVAAEAE-QLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIywtAELYARNVLGIR---------EDDVCFSA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 271 LPLYHIFALTVNSLMGLATGGNNILIPNpRDIPAFV-KELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGM 349
Cdd:cd05959 212 AKLFFAYGLGNSLTFPLSVGATTVLMPE-RPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 350 AVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFtGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVM 429
Cdd:cd05959 291 ALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRY-GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSG 509
Cdd:cd05959 370 TMYWNNRDKTRDTFQ-GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 510 EAVKLFVVRK----DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05959 449 TKPKAFVVLRpgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
51-565 |
7.33e-86 |
|
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: 273.40 E-value: 7.33e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKI-GAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLV 129
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLaNRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 130 DAGAKaifvlenfahtveqvlartevkhvvvasmgdmlgakgaivnLVVRRvkklvpawsipghlsfktvlakgatlgfk 209
Cdd:cd05941 82 DSEPS-----------------------------------------LVLDP----------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 rpnvapgdvAFLQYTGGTTGVSKGATLTHANLLSNM-AQMELWLNTaflrkprpESLTFMCALPLYHIFALTVNSLMGLA 288
Cdd:cd05941 92 ---------ALILYTSGTTGRPKGVVLTHANLAANVrALVDAWRWT--------EDDVLLHVLPLHHVHGLVNALLCPLF 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPNPRDIPAFVKELgRYRTNIFPGLNTLFNALMNNSEF--------RKLDFSSLILTFGGGMAVQRPVAERWL 360
Cdd:cd05941 155 AGASVEFLPKFDPKEVAISRL-MPSITVFMGVPTIYTRLLQYYEAhftdpqfaRAAAAERLRLMVSGSAALPVPTLEEWE 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 ELTGCPIHEGYGLSETSpVATANRLDTDDFTGTIGIPLPSTEVEIRDED-GRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:cd05941 234 AITGHTLLERYGMTEIG-MALSNPLDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEAT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS-GFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVR 518
Cdd:cd05941 313 KEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVL 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499271215 519 KD--PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05941 393 RAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELR 441
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-565 |
1.26e-85 |
|
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: 269.53 E-value: 1.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 215 PGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM-ELWLNTAFLRkprpesltFMCALPLYHIFALtVNSLMGLATGGNN 293
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIgERLGLTEQDR--------LCIPVPLFHCFGS-VLGVLACLTHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 294 ILIPNPR-DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCP-IHEGY 371
Cdd:cd05917 72 MVFPSPSfDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 372 GLSETSPVATANRLDtDDF---TGTIGIPLPSTEVEIRDEDGRTLP-VGEIGEICIRGPQVMAGYWQRPEETARAISPDG 447
Cdd:cd05917 152 GMTETSPVSTQTRTD-DSIekrVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 448 FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEE 526
Cdd:cd05917 231 WLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEgAELTEE 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 499271215 527 EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05917 311 DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
58-565 |
1.66e-83 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 269.05 E-value: 1.66e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAkAIF 137
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEP-ALV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VL--ENFAhTVEQVLARTEVKHVVVasmgdmLGAKGAivnlvvrrvkklvpawsipGHLsfkTVLAKGATLGFKRPNVAP 215
Cdd:PRK07514 105 VCdpANFA-WLSKIAAAAGAPHVET------LDADGT-------------------GSL---LEAAAAAPDDFETVPRGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 216 GDVAFLQYTGGTTGVSKGATLTHANLLSNmAQM--ELWlntAFlrkpRPESLtFMCALPLYHIFALTVNSLMGLATGGNN 293
Cdd:PRK07514 156 DDLAAILYTSGTTGRSKGAMLSHGNLLSN-ALTlvDYW---RF----TPDDV-LIHALPIFHTHGLFVATNVALLAGASM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 294 ILIP--NPRDIPAFVKelgryRTNIFPGLNTLFNALMNNSEFRKLDFSSLILtFGGGMAvqrPV-AE---RWLELTGCPI 367
Cdd:PRK07514 227 IFLPkfDPDAVLALMP-----RATVMMGVPTFYTRLLQEPRLTREAAAHMRL-FISGSA---PLlAEthrEFQERTGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYGLSETSpVATANRLDTDDFTGTIGIPLPSTEVEIRD-EDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPD 446
Cdd:PRK07514 298 LERYGMTETN-MNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK-DPNLTE 525
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKpGAALDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499271215 526 EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07514 457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLR 496
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
35-565 |
3.79e-83 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 271.83 E-value: 3.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKA--------LTFSDLN---THSAKIgawLQSLGLAKGDRVAVMMPNILQNPVIVY 103
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSFLLDAdpldrpetWTYAELLadvTRTANL---LHSLGVGPGDVVAFLLPNLPETHFALW 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 104 GILRAGftVVN-VNPLYTPRELEHQLVDAGAKAIFVLENF-----AHTVEQVLAR-TEVKHVV-VASMGDMLGAKGAIVN 175
Cdd:PRK07529 102 GGEAAG--IANpINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAAlPELRTVVeVDLARYLPGPKRLAVP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 176 LVVRRVKKLVpawsipghLSFKTVLAKG-ATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMaqmelWLNT 254
Cdd:PRK07529 180 LIRRKAHARI--------LDFDAELARQpGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANA-----WLGA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 255 AFLrKPRPESlTFMCALPLYHIFALTVNSLMGLATGGNnILIPNP---RDiPAFVKEL----GRYRTNIFPGLNTLFNAL 327
Cdd:PRK07529 247 LLL-GLGPGD-TVFCGLPLFHVNALLVTGLAPLARGAH-VVLATPqgyRG-PGVIANFwkivERYRINFLSGVPTVYAAL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 328 MN---NSEfrklDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVE 404
Cdd:PRK07529 323 LQvpvDGH----DISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 405 I--RDEDGRTL---PVGEIGEICIRGPQVMAGYwQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFN 479
Cdd:PRK07529 399 VviLDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHN 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 480 VFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-VRKDPNLTEEEVKRHCAASLTnyKR---PRYVEFRTELPKSN 555
Cdd:PRK07529 478 IDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIA--ERaavPKHVRILDALPKTA 555
|
570
....*....|
gi 499271215 556 VGKILRKDLR 565
Cdd:PRK07529 556 VGKIFKPALR 565
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
35-565 |
8.59e-83 |
|
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: 268.17 E-value: 8.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGftVVN 114
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYTPR--ELEHQLVDAGAKAIFVLEN---FAH--TVEQVLARTE-VKHVVVAsmGDmlgakgaivnlvvrrvkklvp 186
Cdd:COG1021 103 VFALPAHRraEISHFAEQSEAVAYIIPDRhrgFDYraLARELQAEVPsLRHVLVV--GD--------------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 187 awsiPG-HLSFKTVLAKGATLgfKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM-ELW-LNtaflrkprPE 263
Cdd:COG1021 160 ----AGeFTSLDALLAAPADL--SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASaEICgLD--------AD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 264 SlTFMCALPLYHIFALTVNSLMG-LATGGNNILIPNPRDIPAFvkEL-GRYRTNIFPGLNTLFNALMNNSEFRKLDFSSL 341
Cdd:COG1021 226 T-VYLAALPAAHNFPLSSPGVLGvLYAGGTVVLAPDPSPDTAF--PLiERERVTVTALVPPLALLWLDAAERSRYDLSSL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 342 ILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATanRLDTDDFT--GTIGIPL-PSTEVEIRDEDGRTLPVGEI 418
Cdd:COG1021 303 RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYT--RLDDPEEVilTTQGRPIsPDDEVRIVDEDGNPVPPGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 419 GEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEC 498
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 499 AAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAAS-LTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:COG1021 461 AVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALR 528
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
45-565 |
5.14e-82 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 266.08 E-value: 5.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 45 VAQYSWRPaftCM-----GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLY 119
Cdd:PLN02246 33 LSEFSDRP---CLidgatGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 120 TPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDmlgakgaivnlvvrrvkklvpawsipGHLSFkTV 199
Cdd:PLN02246 110 TPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPE--------------------------GCLHF-SE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 200 LAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM------ELWLNtaflrkprpESLTFMCALPL 273
Cdd:PLN02246 163 LTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQvdgenpNLYFH---------SDDVILCVLPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 YHIFALtvNSLM--GLATGGNnILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGG---- 347
Cdd:PLN02246 234 FHIYSL--NSVLlcGLRVGAA-ILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGaapl 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 GMAVQRPVAERwleLTGCPIHEGYGLSETSPV-----ATAnRLDTDDFTGTIGIPLPSTEVEIRD-EDGRTLPVGEIGEI 421
Cdd:PLN02246 311 GKELEDAFRAK---LPNAVLGQGYGMTEAGPVlamclAFA-KEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 422 CIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAI 501
Cdd:PLN02246 387 CIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 502 GVADPHSGEAVKLFVVR-KDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PLN02246 467 PMKDEVAGEVPVAFVVRsNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
36-566 |
5.50e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 260.69 E-value: 5.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 36 SIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNV 115
Cdd:PRK06188 13 TYGHLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 116 NPLYTPRELEHQLVDAGAKAIFVLEN-FAHTVEQVLAR-TEVKHVVvaSMGDMLGAKGaivnlvvrrvkklvpawsipgh 193
Cdd:PRK06188 93 HPLGSLDDHAYVLEDAGISTLIVDPApFVERALALLARvPSLKHVL--TLGPVPDGVD---------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 lsfktVLAKGATLGFK--RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSnMAQMEL----WlntaflrkprPESLTF 267
Cdd:PRK06188 149 -----LLAAAAKFGPAplVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIAT-MAQIQLaeweW----------PADPRF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 268 MCALPLYHIFALTVnsLMGLATGGNNILIPNpRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGG 347
Cdd:PRK06188 213 LMCTPLSHAGGAFF--LPTLLRGGTVIVLAK-FDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 GMAVQrPV--AERwLELTGCPIHEGYGLSET-SPVATANRLDTDDFT----GTIGIPLPSTEVEIRDEDGRTLPVGEIGE 420
Cdd:PRK06188 290 ASPMS-PVrlAEA-IERFGPIFAQYYGQTEApMVITYLRKRDHDPDDpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 421 ICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:PRK06188 368 ICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 501 IGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK06188 447 IGVPDEKWGEAVTAVVVlRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
51-565 |
7.97e-79 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 255.08 E-value: 7.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKaifvlenfahtveqvlartevkhVVVASmGDmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd05919 81 CEAR-----------------------LVVTS-AD--------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvapgDVAFLQYTGGTTGVSKGATLTHANLLsnmaqmelWLNTAFLRKP---RPESLTFmCALPLYHIFALTvNSLM-G 286
Cdd:cd05919 92 ------DIAYLLYSSGTTGPPKGVMHAHRDPL--------LFADAMAREAlglTPGDRVF-SSAKMFFGYGLG-NSLWfP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCP 366
Cdd:cd05919 156 LAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGP 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVATANRLDtDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETaRAISPD 446
Cdd:cd05919 236 ILDGIGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDP----N 522
Cdd:cd05919 314 GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPaapqE 393
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499271215 523 LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05919 394 SLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
61-566 |
1.45e-77 |
|
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: 251.49 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapgDVAF 220
Cdd:cd05972 81 E---------------------------------------------------------------------------DPAL 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrkpRPESLTFMCALPLYHIFALTvnSLMG-LATGGNNILIPNP 299
Cdd:cd05972 86 IYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL------RPDDIHWNIADPGWAKGAWS--SFFGpWLLGATVFVYEGP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 300 R-DIPAFVKELGRYRTNIFPGLNTLFNALMNnSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSp 378
Cdd:cd05972 158 RfDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 379 VATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR--GPQVMAGYWQRPEETARAISpDGFFRTGDVGF 456
Cdd:cd05972 236 LTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAY 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 457 MNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD----PNLTEEEVKRHC 532
Cdd:cd05972 315 RDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepSEELAEELQGHV 394
|
490 500 510
....*....|....*....|....*....|....
gi 499271215 533 AASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:cd05972 395 KKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-565 |
1.47e-76 |
|
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: 251.40 E-value: 1.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLEN 141
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAHTVEQVLAR-TEVKHVVVASMGDMLGAKGaivnlvvrrvkklvpawsIPGHLSFKTVLAKGATLgFKRPNVAPGDVAF 220
Cdd:cd12119 107 FLPLLEAIAPRlPTVEHVVVMTDDAAMPEPA------------------GVGVLAYEELLAAESPE-YDWPDFDENTAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTH-ANLLSNMA-QMELWLNTAflrkprpESLTFMCALPLYHifaltVNS----LMGLATGGNNI 294
Cdd:cd12119 168 ICYTSGTTGNPKGVVYSHrSLVLHAMAaLLTDGLGLS-------ESDVVLPVVPMFH-----VNAwglpYAAAMVGAKLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 LiPNPRDIPAFVKEL-GRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELtGCPIHEGYGL 373
Cdd:cd12119 236 L-PGPYLDPASLAELiEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 374 SETSPVATANRLDTD----------DFTGTIGIPLPSTEVEIRDEDGRTLPV--GEIGEICIRGPQVMAGYWQRPEETAr 441
Cdd:cd12119 314 TETSPLGTVARPPSEhsnlsedeqlALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESE- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 442 AISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD- 520
Cdd:cd12119 393 ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEg 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499271215 521 PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd12119 473 ATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
40-565 |
5.12e-72 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 239.56 E-value: 5.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 40 FFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLY 119
Cdd:PRK07470 12 FLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 120 TPRELEHQLVDAGAKAIFVLENFAHTVEQVLA-RTEVKHVVVasmgdmLGAKgaivnlvvrrvkklvpawsiPGHLSFKT 198
Cdd:PRK07470 92 TPDEVAYLAEASGARAMICHADFPEHAAAVRAaSPDLTHVVA------IGGA--------------------RAGLDYEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 VLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHAnllsnmaQMELWLNT--AFLRKPRPESLTFMCALPLYHi 276
Cdd:PRK07470 146 LVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG-------QMAFVITNhlADLMPGTTEQDASLVVAPLSH- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 277 fALTVNSLMGLATGGNNILIPNPR-DIPAFVKELGRYR-TNIFPgLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRP 354
Cdd:PRK07470 218 -GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRvTNLFT-VPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 355 VAERWLELTGCPIHEGYGLSETS---PVATANRLDTDDFT----GTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQ 427
Cdd:PRK07470 296 DQKRALAKLGKVLVQYFGLGEVTgniTVLPPALHDAEDGPdariGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 428 VMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPH 507
Cdd:PRK07470 376 VFAGYYNNPEANAKAFR-DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPV 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 508 SGE-AVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07470 455 WGEvGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
35-564 |
3.14e-70 |
|
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: 233.76 E-value: 3.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARtEVKHvvvasmgdmlgakgaivnlvvrrvkklvpawSIPghl 194
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDRHAGFDHRALAR-ELAE-------------------------------SIP--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 195 sfktvlakgatlgfkrpnvapgDVAFLQYTGGTTGVSKGATLTHANLLSNM-AQMEL-WLNtaflrkprpESLTFMCALP 272
Cdd:cd05920 140 ----------------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVrASAEVcGLD---------QDTVYLAVLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 273 LYHIFALTVNSLMG-LATGGNNILIPNPRDIPAF--VKELGRYRTNIFPGLNTLFnalMNNSEFRKLDFSSLILTFGGGM 349
Cdd:cd05920 189 AAHNFPLACPGVLGtLLAGGRVVLAPDPSPDAAFplIEREGVTVTALVPALVSLW---LDAAASRRADLSSLRLLQVGGA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 350 AVQRPVAERWLELTGCPIHEGYGLSETspVATANRLD--TDDFTGTIGIPL-PSTEVEIRDEDGRTLPVGEIGEICIRGP 426
Cdd:cd05920 266 RLSPALARRVPPVLGCTLQQVFGMAEG--LLNYTRLDdpDEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 427 QVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADP 506
Cdd:cd05920 344 YTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDE 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 507 HSGEAVKLFVVRKDPNLTEEEVKRHC-AASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05920 424 LLGERSCAFVVLRDPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
29-565 |
3.63e-68 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 229.18 E-value: 3.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 29 IGPLTYRSIgefFDHAVAQYSWRPAF---TCMGKA--LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVY 103
Cdd:PRK08008 4 VGGQHLRQM---WDDLADVYGHKTALifeSSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 104 GILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVL--ARTEVKHVVVASMGDmlgakgaivnlvvrrv 181
Cdd:PRK08008 81 GLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQqeDATPLRHICLTRVAL---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 182 kklvPAwsIPGHLSFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLsnMAQMELWLNTAFLRKPR 261
Cdd:PRK08008 145 ----PA--DDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR--FAGYYSAWQCALRDDDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 262 peSLTFMcalPLYHI-FALTVnsLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALM--------NNSE 332
Cdd:PRK08008 217 --YLTVM---PAFHIdCQCTA--AMAAFSAGATFVLLEKYSARAFWGQVCKYRATITECIPMMIRTLMvqppsandRQHC 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 FRKLDFSsliltfgggMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRT 412
Cdd:PRK08008 290 LREVMFY---------LNLSDQEKDAFEERFGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 413 LPVGEIGEICIRG---PQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVA 489
Cdd:PRK08008 361 LPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENII 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 490 ATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK08008 441 ATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
58-565 |
1.22e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 227.00 E-value: 1.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIf 137
Cdd:PRK09088 20 GRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 vlenfahtveqvlartevkhvvvasMGDMLGAKGAivnlvvrrvkklvpawSIPGHLSFKTVLAKGATLGFkRPNVAPGD 217
Cdd:PRK09088 99 -------------------------LGDDAVAAGR----------------TDVEDLAAFIASADALEPAD-TPSIPPER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMaqmelwLNTAFLRKPRPESlTFMCALPLYHIFALTVNSLMGLATGGNnILIP 297
Cdd:PRK09088 137 VSLILFTSGTSGQPKGVMLSERNLQQTA------HNFGVLGRVDAHS-SFLCDAPMFHIIGLITSVRPVLAVGGS-ILVS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNI--FPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLElTGCPIHEGYGLSE 375
Cdd:PRK09088 209 NGFEPKRTLGRLGDPALGIthYFCVPQMAQAFRAQPGFDAAALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 376 TSPV----ATANRLDTDdfTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRT 451
Cdd:PRK09088 288 AGTVfgmsVDCDVIRAK--AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 452 GDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTE-EEVKR 530
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDlERIRS 445
|
490 500 510
....*....|....*....|....*....|....*
gi 499271215 531 HCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
61-566 |
8.71e-67 |
|
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: 222.61 E-value: 8.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKaifvLE 140
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----LD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapgDVAF 220
Cdd:cd05912 78 ----------------------------------------------------------------------------DIAT 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHAN-LLSNMAQMelwLNTAFLRKPRpesltFMCALPLYHIFALTVnsLMGLATGGNNILIPNP 299
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNhWWSAIGSA---LNLGLTEDDN-----WLCALPLFHISGLSI--LMRSVIYGMTVYLVDK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 300 RDIPAFVKELGRYRTNIFPGLNTLFNALMN------NSEFRKldfsslILtFGGGMAVQrPVAERWLELtGCPIHEGYGL 373
Cdd:cd05912 152 FDAEQVLHLINSGKVTIISVVPTMLQRLLEilgegyPNNLRC------IL-LGGGPAPK-PLLEQCKEK-GIPVYQSYGM 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 374 SET-SPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGrtlPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTG 452
Cdd:cd05912 223 TETcSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 453 DVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPnLTEEEVKRHC 532
Cdd:cd05912 299 DIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYC 377
|
490 500 510
....*....|....*....|....*....|....
gi 499271215 533 AASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:cd05912 378 SEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
60-565 |
1.20e-66 |
|
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: 223.03 E-value: 1.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 60 ALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVL 139
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 ENFAHTveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkRPNVAPGDVA 219
Cdd:cd05903 81 ERFRQF----------------------------------------------------------------DPAAMPDAVA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 220 FLQYTGGTTGVSKGATLTHANLLSNM-AQMELWlntaflrkPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNIL--I 296
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIrQYAERL--------GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdI 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PNPRDIPAFVKElgrYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSET 376
Cdd:cd05903 169 WDPDKALALMRE---HGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEC 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 377 SPVATANRLDTDD-FTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAiSPDGFFRTGDVG 455
Cdd:cd05903 246 PGAVTSITPAPEDrRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 456 FMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDP-NLTEEEVKRHC-A 533
Cdd:cd05903 325 RLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVAYLdR 404
|
490 500 510
....*....|....*....|....*....|..
gi 499271215 534 ASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05903 405 QGVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
22-565 |
3.52e-66 |
|
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: 224.33 E-value: 3.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 22 PPGVPAEIGplTYRSIGEFFDHAVAQYSWRPAFT--CMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNP 99
Cdd:cd17642 6 GPFYPLEDG--TAGEQLHKAMKRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 100 VIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLAR-TEVKHVVVASMGDMLGAKGAIVNLVV 178
Cdd:cd17642 84 LPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKlKIIKTIIILDSKEDYKGYQCLYTFIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 179 RRVKKLVPAWSipghlsFKTVlakgatlGFKRPNvapgDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlNTAFLR 258
Cdd:cd17642 164 QNLPPGFNEYD------FKPP-------SFDRDE----QVALIMNSSGSTGLPKGVQLTHKNIVARFSHAR---DPIFGN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 259 KPRPESlTFMCALPLYHIFALTvnSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDF 338
Cdd:cd17642 224 QIIPDT-AILTVIPFHHGFGMF--TTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 SSLILTFGGGMAVQRPVAERWLELTGCP-IHEGYGLSE-TSPVATANrlDTDDFTGTIGIPLPSTEVEIRDED-GRTLPV 415
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTEtTSAILITP--EGDDKPGAVGKVVPFFYAKVVDLDtGKTLGP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 416 GEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGI 495
Cdd:cd17642 379 NERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKI 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271215 496 LECAAIGVADPHSGEAVKLFVVRK-DPNLTEEEVKRHCAASLTNYKRPR-YVEFRTELPKSNVGKILRKDLR 565
Cdd:cd17642 459 FDAGVAGIPDEDAGELPAAVVVLEaGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
51-565 |
4.44e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 223.22 E-value: 4.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:PRK06145 18 RAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAIFVLENFAhtveqvlartevkhVVVAsmgdmLGAKGAIVNLVVRrvkklvpawsipghlSFKTVLAKGATLGFKR 210
Cdd:PRK06145 98 AGAKLLLVDEEFD--------------AIVA-----LETPKIVIDAAAQ---------------ADSRRLAQGGLEIPPQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwlNTAFLRKPRPESLtfMCALPLYHIFALTVNSLMGLATG 290
Cdd:PRK06145 144 AAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSID-----HVIALGLTASERL--LVVGPLYHVGAFDLPGIAVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNnILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL-TGCPIHE 369
Cdd:PRK06145 217 GT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 370 GYGLSETSPVATANRLDTD-DFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGF 448
Cdd:PRK06145 296 AYGLTETCSGDTLMEAGREiEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDW 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 449 FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEE 527
Cdd:PRK06145 375 FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlNPGATLTLEA 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 499271215 528 VKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK06145 455 LDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
58-565 |
4.50e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 223.42 E-value: 4.50e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENFAHTVEQVLARTeVKHVVVASMGDMLGAKGaiVNLVVRRVKklvpawsiPGHLSFKTVLAKGATlgfKRPNVAPGD 217
Cdd:PRK12406 89 AHADLLHGLASALPAG-VTVLSVPTPPEIAAAYR--ISPALLTPP--------AGAIDWEGWLAQQEP---YDGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLqYTGGTTGVSKG-----ATLTHAnllsnmAQMELWLNTAFLRKPRPESLtfmCALPLYHIfALTVNSLMGLATGGN 292
Cdd:PRK12406 155 QSMI-YTSGTTGHPKGvrraaPTPEQA------AAAEQMRALIYGLKPGIRAL---LTGPLYHS-APNAYGLRAGRLGGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 293 NILIPNpRDIPAFVKELGRYR-TNIF--PglnTLFNALMNNSEF--RKLDFSSLILTFGGGMAVQRPVAERWLELTGCPI 367
Cdd:PRK12406 224 LVLQPR-FDPEELLQLIERHRiTHMHmvP---TMFIRLLKLPEEvrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPqVMAG--YWQRPEETArAISP 445
Cdd:PRK12406 300 YEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIA-GNPDftYHNKPEKRA-EIDR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 446 DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLfVVRKDP--NL 523
Cdd:PRK12406 378 GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMA-VVEPQPgaTL 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499271215 524 TEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK12406 457 DEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
58-565 |
7.46e-66 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 222.47 E-value: 7.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENFAHTVEQVLARTEvKHVVVASMGDmlgakGAIvnlvvrrvkklvpawsiPGHLSFKTVLA-KGATLGfkrPNVAPG 216
Cdd:PRK08276 89 VSAALADTAAELAAELP-AGVPLLLVVA-----GPV-----------------PGFRSYEEALAaQPDTPI---ADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVafLQYTGGTTGVSKG--ATLTH----ANLLSNMAQMELWLNTAflrkprPESLTFMCAlPLYHIfALTVNSLMGLATG 290
Cdd:PRK08276 143 AD--MLYSSGTTGRPKGikRPLPGldpdEAPGMMLALLGFGMYGG------PDSVYLSPA-PLYHT-APLRFGMSALALG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNNILIPNpRDIPAFVKELGRYR---TNIFPglnTLFNALMNNSEFR--KLDFSSLILTFGGGMAVQRPVAERWLELTGC 365
Cdd:PRK08276 213 GTVVVMEK-FDAEEALALIERYRvthSQLVP---TMFVRMLKLPEEVraRYDVSSLRVAIHAAAPCPVEVKRAMIDWWGP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 366 PIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPStEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISP 445
Cdd:PRK08276 289 IIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 446 DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-----VRKD 520
Cdd:PRK08276 368 HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadgADAG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 499271215 521 PNLtEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK08276 448 DAL-AAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
217-561 |
1.55e-65 |
|
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: 216.60 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelWLNTAFLRkprpESLTFMCALPLYHIFALTVNSLMGLATGGNniLI 296
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAA---WADCADLT----EDDRYLIINPFFHTFGYKAGIVACLLTGAT--VV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PNPR-DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWL-ELTGCPIHEGYGLS 374
Cdd:cd17638 72 PVAVfDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRsELGFETVLTAYGLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 375 ETSpVATANRLDtDDFT---GTIGIPLPSTEVEIRDEdgrtlpvgeiGEICIRGPQVMAGYWQRPEETARAISPDGFFRT 451
Cdd:cd17638 152 EAG-VATMCRPG-DDAEtvaTTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 452 GDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDP-NLTEEEVKR 530
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIA 299
|
330 340 350
....*....|....*....|....*....|.
gi 499271215 531 HCAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:cd17638 300 WCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
16-565 |
1.82e-65 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 222.93 E-value: 1.82e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 16 IWLGSYPP-GVPAEIgpltyrSIGEFFDHAVAQYSWRPAFT--CMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMM 92
Cdd:PLN02330 14 IFRSRYPSvPVPDKL------TLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 93 PNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIfvlenfahtVEQVLARTEVKHVVVASMgdMLGAKga 172
Cdd:PLN02330 88 PNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLI---------VTNDTNYGKVKGLGLPVI--VLGEE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 173 ivnlvvrrvkklvpawSIPGHLSFKTVLAKGATLGFKRPN--VAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmel 250
Cdd:PLN02330 155 ----------------KIEGAVNWKELLEAADRAGDTSDNeeILQTDLCALPFSSGTTGISKGVMLTHRNLVANLC---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 251 wlntAFLRKPRPE---SLTFMCALPLYHIFALTVNSLMGLATGGNnILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNAL 327
Cdd:PLN02330 215 ----SSLFSVGPEmigQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 328 MNNSEFRKLDFSSLILTfgGGMAVQRPVAERWL-----ELTGCPIHEGYGLSETSPVaTANRLDTDDFTG-----TIGIP 397
Cdd:PLN02330 290 VKNPIVEEFDLSKLKLQ--AIMTAAAPLAPELLtafeaKFPGVQVQEAYGLTEHSCI-TLTHGDPEKGHGiakknSVGFI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 398 LPSTEVEIRDED-GRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS 476
Cdd:PLN02330 367 LPNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 477 GFNVFPNEIEEVAATHPGILECAAIGVADPHSGE-AVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSN 555
Cdd:PLN02330 447 GFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEiPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSL 526
|
570
....*....|
gi 499271215 556 VGKILRKDLR 565
Cdd:PLN02330 527 SGKIMRRLLK 536
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
51-565 |
9.03e-65 |
|
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: 218.12 E-value: 9.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIG-AWLQSLGLAKGDRVAVMMPNilqNPVIV---YGILRAGFTVVNVNPLYTPRELEh 126
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIAnVLVGELGIVPGNRVLLRGSN---SPELVacwFGIQKAGAIAVATMPLLRPKELA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 127 qlvdagakaifvlenfahtveQVLARTEVKHVVVAsmgdmlgakgaivnlvvrrvkklvpawsipGHLSfktvlakgatl 206
Cdd:cd05958 77 ---------------------YILDKARITVALCA------------------------------HALT----------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 207 gfkrpnvAPGDVAFLQYTGGTTGVSKGATLTHANLLsnmAQMELWlNTAFLRkPRPESLTFMCAlPLYHIFALTVNSLMG 286
Cdd:cd05958 95 -------ASDDICILAFTSGTTGAPKATMHFHRDPL---ASADRY-AVNVLR-LREDDRFVGSP-PLAFTFGLGGVLLFP 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGGNNILIPNpRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCP 366
Cdd:cd05958 162 FGVGASGVLLEE-ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVATANRLDtDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPqvmAGYWQRPEETARAISPD 446
Cdd:cd05958 241 IIDGIGSTEMFHIFISARPG-DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK-----DP 521
Cdd:cd05958 317 GWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGP 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 499271215 522 NLTeEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05958 397 VLA-RELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
28-564 |
1.70e-64 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 220.39 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 28 EIGPLTYRSIGEFFDHAVAQYSWRPAFT-CMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGIL 106
Cdd:PRK06087 16 QQGYWGDASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 107 RAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHT--VEQVLA-RTEVKHvvvasMGDMLGakgaivnlvvrrVKK 183
Cdd:PRK06087 96 KVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTrpVDLILPlQNQLPQ-----LQQIVG------------VDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 184 LVPAWSipgHLSFKTVLAKGATLGFKrPNVAPGDVAFLQYTGGTTGVSKGATLTHANLL----SNMAQMEL-WLNTaflr 258
Cdd:PRK06087 159 LAPATS---SLSLSQIIADYEPLTTA-ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILaserAYCARLNLtWQDV---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 259 kprpesltFMCALPLYHI--FALTVNSLMGLatGGNNIL--IPNPRdipAFVKELGRYRTNIFPGLNTLFNALMNNSEFR 334
Cdd:PRK06087 231 --------FMMPAPLGHAtgFLHGVTAPFLI--GARSVLldIFTPD---ACLALLEQQRCTCMLGATPFIYDLLNLLEKQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 335 KLDFSSLILTFGGGMAVQRPVAERWLElTGCPIHEGYGLSETSPVATANRLD-TDDFTGTIGIPLPSTEVEIRDEDGRTL 413
Cdd:PRK06087 298 PADLSALRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 414 PVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHP 493
Cdd:PRK06087 377 PPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHP 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 494 GILECAAIGVADPHSGEAVKLFVVRKDP--NLTEEEVKRH-CAASLTNYKRPRYVEFRTELPKSNVGKI----LRKDL 564
Cdd:PRK06087 457 KIHDACVVAMPDERLGERSCAYVVLKAPhhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIqkflLRKDI 534
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
51-565 |
1.43e-63 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 215.98 E-value: 1.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:PRK03640 18 RTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAIFVLENFAHTVeqvlarTEVKHVVVASMGDmlgakgaivnlVVRRVKKLVPAWsipgHLSFktvlakgatlgfkr 210
Cdd:PRK03640 98 AEVKCLITDDDFEAKL------IPGISVKFAELMN-----------GPKEEAEIQEEF----DLDE-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvapgdVAFLQYTGGTTGVSKGATLTHAN-LLSNMA-QMELWLNtaflrkprpESLTFMCALPLYHIFALTVnsLMGLA 288
Cdd:PRK03640 143 -------VATIMYTSGTTGKPKGVIQTYGNhWWSAVGsALNLGLT---------EDDCWLAAVPIFHISGLSI--LMRSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN-------NSEFRkldfsSLILtfGGGmavqrPVAERWLE 361
Cdd:PRK03640 205 IYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLLErlgegtyPSSFR-----CMLL--GGG-----PAPKPLLE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 362 ---LTGCPIHEGYGLSET-SPVATANRLDTDDFTGTIGIPLPSTEVEIRDeDGRTLPVGEIGEICIRGPQVMAGYWQRPE 437
Cdd:PRK03640 273 qckEKGIPVYQSYGMTETaSQIVTLSPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNRED 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:PRK03640 352 ATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499271215 518 rKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK03640 431 -KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELK 477
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
61-507 |
1.89e-63 |
|
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: 214.77 E-value: 1.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLY---TPRELEHQLVDAGAKAIF 137
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VlenfahtveqvlartevkhvvvasmGDmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvaPGD 217
Cdd:cd05907 83 V-------------------------ED-------------------------------------------------PDD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlnTAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNNILIP 297
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILSNAL-------ALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAfvkELGRYRTNIFPGLNTLFNALMNN------SEFRKLDFSSLIL-----TFGGGMAVQRPVAERWLELtGCP 366
Cdd:cd05907 162 SAETLLD---DLSEVRPTVFLAVPRVWEKVYAAikvkavPGLKRKLFDLAVGgrlrfAASGGAPLPAELLHFFRAL-GIP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVATANRLDTDDFtGTIGIPLPSTEVEIRDEdgrtlpvgeiGEICIRGPQVMAGYWQRPEETARAISPD 446
Cdd:cd05907 238 VYEGYGLTETSAVVTLNPPGDNRI-GTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDAD 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVS-GFNVFPNEIEEVAATHPGILECAAIGVADPH 507
Cdd:cd05907 307 GWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIGDGRPF 368
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
51-566 |
2.31e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 215.24 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAwlqslGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:PRK07787 16 ADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAifvlenfahtveqvlartevkhVVVASMGDMLGAKGAIVNLVVRrvkklvpAWSIPghlsfktvlakgatlgfkr 210
Cdd:PRK07787 91 SGAQA----------------------WLGPAPDDPAGLPHVPVRLHAR-------SWHRY------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNM-AQMELWLNTAflrkprpeSLTFMCALPLYHIFALTVNSLMGLAT 289
Cdd:PRK07787 123 PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLdALAEAWQWTA--------DDVLVHGLPLFHVHGLVLGVLGPLRI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNniLIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLdFSSLILTFGGGMAVQRPVAERWLELTGCPIHE 369
Cdd:PRK07787 195 GNR--FVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 370 GYGLSETSpVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPV-GE-IGEICIRGPQVMAGYWQRPEETARAISPDG 447
Cdd:PRK07787 272 RYGMTETL-ITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHdGEtVGELQVRGPTLFDGYLNRPDATAAAFTADG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 448 FFRTGDVGFMNAEGLTKIVDRKK-DMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPnLTEE 526
Cdd:PRK07787 351 WFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD-VAAD 429
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499271215 527 EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK07787 430 ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
58-561 |
2.45e-63 |
|
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: 215.00 E-value: 2.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapGD 217
Cdd:cd05914 85 VSDE--------------------------------------------------------------------------DD 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLRKPRPESLTFmcaLPLYHIFALTVNSLMGLATGGNNIL-- 295
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYRNIVSNVD----GVKEVVLLGKGDKILSI---LPLHHIYPLTFTLLLPLLNGAHVVFld 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 296 -IPNPR-DIPAFVKE------------LGRYRTNIFPGLNT-----LFNALMNNSEFRKLDFSSLILTFGG-------GM 349
Cdd:cd05914 164 kIPSAKiIALAFAQVtptlgvpvplviEKIFKMDIIPKLTLkkfkfKLAKKINNRKIRKLAFKKVHEAFGGnikefviGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 350 AVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTiGIPLPSTEVEIRDEDgrtlPVGEIGEICIRGPQVM 429
Cdd:cd05914 244 AKINPDVEEFLRTIGFPYTIGYGMTETAPIISYSPPNRIRLGSA-GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILV-SGFNVFPNEIEEVAATHPGILEC---------A 499
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESlvvvqekklV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271215 500 AIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHcAASLTNYKRPRYV-EFRTELPKSNVGKILR 561
Cdd:cd05914 399 ALAYIDPDFLDVKALKQRNIIDAIKWEVRDKV-NQKVPNYKKISKVkIVKEEFEKTPKGKIKR 460
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
67-565 |
1.23e-62 |
|
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: 213.07 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 67 NTHSAKIGAWlQSLGLAKGDRVAVMMPNILQNPVIVYGILRAG----FTVVNVNPLYTPRELEHQLVDAGAKAIFVlenf 142
Cdd:cd05922 1 LGVSAAASAL-LEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 143 ahtveqvlartevkhvvVASMGDmlgakgaivnlvvrRVKKLVPAWSIPGhLSFKTVLAKGATLGFKRPNVAPGDVAFLQ 222
Cdd:cd05922 76 -----------------DAGAAD--------------RLRDALPASPDPG-TVLDADGIRAARASAPAHEVSHEDLALLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 223 YTGGTTGVSKGATLTHANLLSNMAQMELWL-NTAFLRkprpesltFMCALPLYHIFALTVnSLMGLATGGNNILIPNPRD 301
Cdd:cd05922 124 YTSGSTGSPKLVRLSHQNLLANARSIAEYLgITADDR--------ALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 302 IPAFVKELGRYRTNIFPGLNTLFnALMNNSEFRKLDFSSL-ILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVA 380
Cdd:cd05922 195 DDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLrYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRM 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 381 T---ANRLDTDdfTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFM 457
Cdd:cd05922 274 TylpPERILEK--PGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 458 NAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPhSGEAVKLFVVRKDpNLTEEEVKRHCAASLT 537
Cdd:cd05922 352 DEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPD-KIDPKDVLRSLAERLP 429
|
490 500
....*....|....*....|....*...
gi 499271215 538 NYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
43-565 |
1.00e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 212.72 E-value: 1.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 43 HAVAQYSwRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPR 122
Cdd:PRK07786 26 HALMQPD-APALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 123 ELEHQLVDAGAKAIF---VLENFAHTVEQVLARTEVKHVVVASMGDmlgakgaivnlvvrrvkklvpawsipGHLSFKTV 199
Cdd:PRK07786 105 EIAFLVSDCGAHVVVteaALAPVATAVRDIVPLLSTVVVAGGSSDD--------------------------SVLGYEDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 200 LAKGAtlgfkrPNVAPGDV-----AFLQYTGGTTGVSKGATLTHANLlSNMAQMELWLNTAFlrkpRPESLTFmCALPLY 274
Cdd:PRK07786 159 LAEAG------PAHAPVDIpndspALIMYTSGTTGRPKGAVLTHANL-TGQAMTCLRTNGAD----INSDVGF-VGVPLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 275 HIFALTvNSLMGLATGGNNILIP-NPRDIPAFVKELGRYR-TNIFPgLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQ 352
Cdd:PRK07786 227 HIAGIG-SMLPGLLLGAPTVIYPlGAFDPGQLLDVLEAEKvTGIFL-VPAQWQAVCAEQQARPRDLALRVLSWGAAPASD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 353 RPVAERWLELTGCPIHEGYGLSETSPVATAnrLDTDDFT---GTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVM 429
Cdd:PRK07786 305 TLLRQMAATFPEAQILAAFGQTEMSPVTCM--LLGEDAIrklGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSG 509
Cdd:PRK07786 383 SGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWG 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 510 EA-VKLFVVRKDPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07786 462 EVpVAVAAVRNDDAaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
51-564 |
4.39e-61 |
|
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: 208.15 E-value: 4.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYtPRE-LEHQLV 129
Cdd:cd05930 3 AVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 130 DAGAKAIFVlenfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfk 209
Cdd:cd05930 82 DSGAKLVLT----------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 rpnvAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFlrkPRPESLTFMCALPLyhIFALTVNSLMG-LA 288
Cdd:cd05930 91 ----DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL----WMQEAY---PLTPGDRVLQFTSF--SFDVSVWEIFGaLL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPN--PRDIPAFVKELGRYR---TNIFPglnTLFNALMNNSEFRklDFSSLILTFGGGMAVQRPVAERWLEL- 362
Cdd:cd05930 158 AGATLVVLPEevRKDPEALADLLAEEGitvLHLTP---SLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELl 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHEGYGLSETSPVATANRLDTDDFTG---TIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:cd05930 233 PGARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISPDGFF------RTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVK 513
Cdd:cd05930 313 AERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 514 LFVV-RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05930 393 AYVVpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
58-559 |
6.20e-61 |
|
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: 209.11 E-value: 6.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSlGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENFahtVEQVlarTEVKHVVVASMGDML----------GAKGAIVNLVVrrvkKLVPAWSIpghlsfktvlakgatLG 207
Cdd:cd05909 84 TSKQF---IEKL---KLHHLFDVEYDARIVyledlrakisKADKCKAFLAG----KFPPKWLL---------------RI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 208 FKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwLNTAFlrKPRPESlTFMCALPLYHIFALTVNSLMGL 287
Cdd:cd05909 139 FGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQ----ITAIF--DPNPED-VVFGALPFFHSFGLTGCLWLPL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 288 ATGGNNILIPNP---RDIPAFVKElgrYRTNIFPGLNTLFNALMNNSEfrKLDFSSLILTFGGGMAVQRPVAERWLELTG 364
Cdd:cd05909 212 LSGIKVVFHPNPldyKKIPELIYD---KKATILLGTPTFLRGYARAAH--PEDFSSLRLVVAGAEKLKDTLRQEFQEKFG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 365 CPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRT-LPVGEIGEICIRGPQVMAGYWQRPEETARAI 443
Cdd:cd05909 287 IRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 444 SpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATH-PGILECAAIGVADPHSGEAVKLFVVRKDPn 522
Cdd:cd05909 367 G-DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDT- 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 499271215 523 lTEEEVKRHC-AASLTNYKRPRYVEFRTELPKSNVGKI 559
Cdd:cd05909 445 -DPSSLNDILkNAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
58-565 |
1.08e-60 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 210.47 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWL-QSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAI 136
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 137 FV-LENfahtVEQvlartevkhvvvasmgdmLGAKGaivnlvvrrvkklVPAWSIPGHLSFKTVLAKGAT----LGFK-- 209
Cdd:PLN02574 144 FTsPEN----VEK------------------LSPLG-------------VPVIGVPENYDFDSKRIEFPKfyelIKEDfd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 ---RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLsnmAQMELWLN-TAFLRKPRPESLTFMCALPLYHIFALTVnSLM 285
Cdd:PLN02574 189 fvpKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI---AMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSL-FVV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 286 GLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSE-FRKLDFSSLILTFGGGMAVQRPVAERWLE-LT 363
Cdd:PLN02574 265 GLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQtLP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 GCPIHEGYGLSETSPVATANrLDTDDFT--GTIGIPLPSTEVEIRD-EDGRTLPVGEIGEICIRGPQVMAGYWQRPEETA 440
Cdd:PLN02574 345 HVDFIQGYGMTESTAVGTRG-FNTEKLSkySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQ 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 441 RAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD 520
Cdd:PLN02574 424 STIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQ 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499271215 521 PN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PLN02574 504 GStLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-561 |
4.70e-60 |
|
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: 202.11 E-value: 4.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 223 YTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprpESLTFMCALPLYHIFALTvnslMGLAT---GGNNILIPNp 299
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLT-------EADVYLNMLPLFHIAGLN----LALATfhaGGANVVMEK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 300 RDIPAFVKELGRYRTNIF----PGLNTLFNALMNNSefrkLDFSSLILTFGggmaVQRP-VAERWLELTGCPIHEGYGLS 374
Cdd:cd17637 75 FDPAEALELIEEEKVTLMgsfpPILSNLLDAAEKSG----VDLSSLRHVLG----LDAPeTIQRFEETTGATFWSLYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 375 ETSPVATANRldTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDV 454
Cdd:cd17637 147 ETSGLVTLSP--YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 455 GFMNAEGLTKIVDRK--KDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRH 531
Cdd:cd17637 224 GRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPgATLTADELIEF 303
|
330 340 350
....*....|....*....|....*....|
gi 499271215 532 CAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:cd17637 304 VGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
59-565 |
1.11e-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: 199.20 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFv 138
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 139 lenfahtveqvlarTEvkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvAPGDV 218
Cdd:cd05971 84 --------------TD-----------------------------------------------------------GSDDP 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkPRPESLTFMCA------------LPLYHiFALTVnslmg 286
Cdd:cd05971 91 ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLF----PRDGDLYWTPAdwawigglldvlLPSLY-FGVPV----- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGgnniliPNPRDIPAFVKELGRYR-TNIF--PGLNTLFNAlmnNSEFRKLDFSSLILTFGGGmavqRPVAERWL--- 360
Cdd:cd05971 161 LAHR------MTKFDPKAALDLMSRYGvTTAFlpPTALKMMRQ---QGEQLKHAQVKLRAIATGG----ESLGEELLgwa 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 -ELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQ--VMAGYWQRPE 437
Cdd:cd05971 228 rEQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDgFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:cd05971 308 ATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 518 RKDPNLTEEEVKR----HCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05971 387 LNPGETPSDALAReiqeLVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
60-534 |
1.65e-57 |
|
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: 201.31 E-value: 1.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 60 ALTFSDLNTHSAKIGAWLQSLGLAkGDRVAVMMPnilQNPVIV---YGILRAGFTVVnvnPLYTPRELEHqlvdagakai 136
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVGKP-GDRVLLLAP---PGLDFVaafLGCLYAGAIAV---PLPPPTPGRH---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 137 fvlenfAHTVEQVLARTEVKHVVVASmgdmlGAKGAivnlvVRRVKKLVPAWSIPGHLSFKTVLAKGATLgFKRPNVAPG 216
Cdd:cd05931 87 ------AERLAAILADAGPRVVLTTA-----AALAA-----VRAFAASRPAAGTPRLLVVDLLPDTSAAD-WPPPSPDPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMelwlNTAFlrKPRPESlTFMCALPLYHIFALTVNSLMGLATGGNNILI 296
Cdd:cd05931 150 DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQI----RRAY--GLDPGD-VVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PnPRdipAFV-------KELGRYRTNIFPGLNtlFnAL------MNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELT 363
Cdd:cd05931 223 S-PA---AFLrrplrwlRLISRYRATISAAPN--F-AYdlcvrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 G---------CPiheGYGLSE------TSPVAT---ANRLDTDDFTGTI----------------GIPLPSTEVEIRDED 409
Cdd:cd05931 296 ApfgfrpeafRP---SYGLAEatlfvsGGPPGTgpvVLRVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 410 GRT-LPVGEIGEICIRGPQVMAGYWQRPEETAR------AISPDGFFRTGDVGFMnAEGLTKIVDRKKDMILVSGFNVFP 482
Cdd:cd05931 373 TGReLPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYP 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 483 NEIE-EVAATHPGILE--CAAIGVADPHSGEAVklFVVRKDPNLTEEEVKRHCAA 534
Cdd:cd05931 452 QDIEaTAEEAHPALRPgcVAAFSVPDDGEERLV--VVAEVERGADPADLAAIAAA 504
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
61-564 |
3.08e-57 |
|
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: 199.27 E-value: 3.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEhqlvdagakaifvle 140
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELA--------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfahtveQVLARTEVKHVVVAsmgDMLGAKGAIVNLVVR--RVKKLVpawsipghlsfKTVLAKGATLGFKRPNVAPGDV 218
Cdd:cd05923 94 -------ELIERGEMTAAVIA---VDAQVMDAIFQSGVRvlALSDLV-----------GLGEPESAGPLIEDPPREPEQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlNTAFLRKPRPESLtfMCALPLYHIFALTVNSLMGLATGGNNILIP- 297
Cdd:cd05923 153 AFVFYTSGTTGLPKGAVIPQRAAESRVLFMS---TQAGLRHGRHNVV--LGLMPLYHVIGFFAVLVAALALDGTYVVVEe 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 -NPRDIPAFVKELGRyrTNIFpGLNTLFNALMNNSEFRKLDFSSL-ILTFGGGmAVQRPVAERWLELTGCPIHEGYGLSE 375
Cdd:cd05923 228 fDPADALKLIEQERV--TSLF-ATPTHLDALAAAAEFAGLKLSSLrHVTFAGA-TMPDAVLERVNQHLPGEKVNIYGTTE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 376 TspvatANRL-DTDDFTGTIGIPLPSTEVEIRDEDGRT---LPVGEIGEICIR--GPQVMAGYWQRPEETARAISpDGFF 449
Cdd:cd05923 304 A-----MNSLyMRDARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKLQ-DGWY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 450 RTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVK 529
Cdd:cd05923 378 RTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELD 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 499271215 530 RHCAAS-LTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05923 458 QFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
34-566 |
3.45e-57 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 200.54 E-value: 3.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 34 YRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNilqNPVIVYGILRAGFT-- 111
Cdd:PRK07788 48 YGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARN---HRGFVLALYAAGKVga 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 112 -VVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASmGDMLGAKGAIV----NLVVRRVKKLVP 186
Cdd:PRK07788 125 rIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGN-PDDDEPSGSTDetldDLIAGSSTAPLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 187 AWSIPGHLsfkTVLakgatlgfkrpnvapgdvaflqyTGGTTGVSKGATLTHANLLSNMAQMelwlntaFLRKPRPESLT 266
Cdd:PRK07788 204 KPPKPGGI---VIL-----------------------TSGTTGTPKGAPRPEPSPLAPLAGL-------LSRVPFRAGET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 267 FMCALPLYHIFALtvnSLMGLATG-GNNILIPNPRDIPAFVKELGRYRTN------IFpgLNTLFNALMNNSEfrKLDFS 339
Cdd:PRK07788 251 TLLPAPMFHATGW---AHLTLAMAlGSTVVLRRRFDPEATLEDIAKHKATalvvvpVM--LSRILDLGPEVLA--KYDTS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 340 SLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIG 419
Cdd:PRK07788 324 SLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 420 EICIRGPQVMAGYWQ-RPEETAraispDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEC 498
Cdd:PRK07788 404 RIFVGNGFPFEGYTDgRDKQII-----DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 499 AAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK07788 479 AVIGVDDEEFGQRLRAFVVKAPgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
215-565 |
2.82e-56 |
|
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: 193.08 E-value: 2.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 215 PGDVAFLQYTGGTTGVSKGATLTHANLLSNmAQMelwLNTAFLRKPRPeslTFMCALPLYHIFALTVNSLMGLATGGNnI 294
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN-AWM---LALNSLFDPDD---VLLCGLPLFHVNGSVVTLLTPLASGAH-V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 LIPNP---RDiPAFVKEL----GRYRTNIFPGLNTLFNALMNNSEFRklDFSSLILTFGGGMAVQRPVAERWLELTGCPI 367
Cdd:cd05944 73 VLAGPagyRN-PGLFDNFwklvERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDG-----RTLPVGEIGEICIRGPQVMAGYWQRpEETARA 442
Cdd:cd05944 150 VEGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICVAGPGVFGGYLYT-EGNKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 443 ISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-VRKDP 521
Cdd:cd05944 229 FVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 499271215 522 NLTEEEVKRHCAASLTNYKR-PRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05944 309 VVEEEELLAWARDHVPERAAvPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
59-565 |
4.26e-56 |
|
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: 197.33 E-value: 4.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIfv 138
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMI-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 139 lenfahtveqvlartevkhVVVASMGDMLGAKGAIVNLVVRRVKKLVPAWSIPGHLSFKTVLAKGATLgFKRP--NVAPG 216
Cdd:cd05970 124 -------------------VAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPD-FERPtaNSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 --DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrkpRPESLtfmcalplyHifaLTV----------NSL 284
Cdd:cd05970 184 geDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNV------REGGL---------H---LTVadtgwgkavwGKI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 MGLATGGNNILIPN-PRDIP-AFVKELGRYRTNIFPGLNTLFNALMNnSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL 362
Cdd:cd05970 246 YGQWIAGAAVFVYDyDKFDPkALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHEGYGLSETSpVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQ-----VMAGYWQRPE 437
Cdd:cd05970 325 TGIKLMEGFGQTETT-LTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:cd05970 404 KTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 518 -RKDPNLTEE---EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05970 483 lAKGYEPSEElkkELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
59-502 |
8.27e-56 |
|
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: 194.89 E-value: 8.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGftVVNVnplytPR-------ELEHQLVDA 131
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALG--AVDV-----VRgsdssveELLYILNHS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 132 GAKAIFVlENfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrp 211
Cdd:cd17640 77 ESVALVV-EN---------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 nvAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLntaflrkPRPESLTFMCALPLYHIFALTVNSLmgLATGG 291
Cdd:cd17640 86 --DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIV-------PPQPGDRFLSILPIWHSYERSAEYF--IFACG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 292 NNILIPNprdIPAFVKELGRYRTNIFPGLNTLFNALMNN--------SEFRKLDFSSLIL--------TFGGGMAvqrPV 355
Cdd:cd17640 155 CSQAYTS---IRTLKDDLKRVKPHYIVSVPRLWESLYSGiqkqvsksSPIKQFLFLFFLSggifkfgiSGGGALP---PH 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWLELTGCPIHEGYGLSETSPVATANRLDTDdFTGTIGIPLPSTEVEIRDEDGRT-LPVGEIGEICIRGPQVMAGYWQ 434
Cdd:cd17640 229 VDTFFEAIGIEVLNGYGLTETSPVVSARRLKCN-VRGSVGRPLPGTEIKIVDPEGNVvLPPGEKGIVWVRGPQVMKGYYK 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 435 RPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS-GFNVFPNEIEEVAATHPGILECAAIG 502
Cdd:cd17640 308 NPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
51-564 |
8.72e-56 |
|
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: 194.39 E-value: 8.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd05945 7 RPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAIFVlenfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd05945 87 AKPALLIA------------------------------------------------------------------------ 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLRKPRPEsltFMCALPLYhiFALTVNSLM-GLAT 289
Cdd:cd05945 95 ---DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTN----WMLSDFPLGPGDV---FLNQAPFS--FDLSVMDLYpALAS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNniLIPNPRDIPAFVKELGRY----RTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELT-G 364
Cdd:cd05945 163 GAT--LVPVPRDATADPKQLFRFlaehGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpD 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 365 CPIHEGYGLSETSPVATANRLDTDDFTG----TIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETA 440
Cdd:cd05945 241 ARIYNTYGPTEATVAVTYIEVTPEVLDGydrlPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 441 RAISPD---GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:cd05945 321 AAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVV 400
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499271215 518 RKD----PNLTeeEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd05945 401 PKPgaeaGLTK--AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
51-566 |
2.64e-55 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 194.52 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTcM---GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQ 127
Cdd:PRK13391 13 KPAVI-MastGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 128 LVDAGAKAIFVLENFAHTVEQVLART-EVKHVVVAsmgDMLGAKGAIVNLvvRRVKKLVPAWSIPGHlsfktvlakgaTL 206
Cdd:PRK13391 92 VDDSGARALITSAAKLDVARALLKQCpGVRHRLVL---DGDGELEGFVGY--AEAVAGLPATPIADE-----------SL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 207 GfkrpnvapgdvAFLQYTGGTTGVSKG--ATLTHANLLSNMAQMELWLNtafLRKPRPESlTFMCALPLYHIFALTVNSL 284
Cdd:PRK13391 156 G-----------TDMLYSSGTTGRPKGikRPLPEQPPDTPLPLTAFLQR---LWGFRSDM-VYLSPAPLYHSAPQRAVML 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 mGLATGGNNILIPNpRDIPAFVKELGRYR---TNIFPglnTLFNALMN-NSEFR-KLDFSSLILTFGGGMAVQRPVAERW 359
Cdd:PRK13391 221 -VIRLGGTVIVMEH-FDAEQYLALIEEYGvthTQLVP---TMFSRMLKlPEEVRdKYDLSSLEVAIHAAAPCPPQVKEQM 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 360 LELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPStEVEIRDEDGRTLPVGEIGEICIRGPQvMAGYWQRPEET 439
Cdd:PRK13391 296 IDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGR-PFEYLNDPAKT 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISPDGFFRT-GDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-- 516
Cdd:PRK13391 374 AEARHPDGTWSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVqp 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499271215 517 ---VRKDPNLTEEEVKrHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK13391 454 vdgVDPGPALAAELIA-FCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
35-566 |
2.96e-55 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 195.27 E-value: 2.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKA------LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRA 108
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 109 GfTVVN-VNPLYTPRELEHQLVDAGAKAIFV---LENFAHtvEQVLAR-----TEVKHVVVasmgdmLGAKGAIvnlvvr 179
Cdd:PRK13295 104 G-AVLNpLMPIFRERELSFMLKHAESKVLVVpktFRGFDH--AAMARRlrpelPALRHVVV------VGGDGAD------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 180 rvkklvpawsipghlSFKTVLAK---------GATLGFKRPNvaPGDVAFLQYTGGTTGVSKGATLTHANLLSNMA---- 246
Cdd:PRK13295 169 ---------------SFEALLITpaweqepdaPAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVpyae 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 247 QMELwlntaflrkpRPESLTFMcALPLYHIFALTVNSLMGLATGGNNILipnpRDI--PAFVKELGRYRTNIFPGLNTLF 324
Cdd:PRK13295 232 RLGL----------GADDVILM-ASPMAHQTGFMYGLMMPVMLGATAVL----QDIwdPARAAELIRTEGVTFTMASTPF 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 325 NA-LMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVaTANRLDTDD--FTGTIGIPLPST 401
Cdd:PRK13295 297 LTdLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAV-TLTKLDDPDerASTTDGCPLPGV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 402 EVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETAraISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVF 481
Cdd:PRK13295 376 EVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIP 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 482 PNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHC-AASLTNYKRPRYVEFRTELPKSNVGKI 559
Cdd:PRK13295 454 VVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVpRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKI 533
|
570
....*....|.
gi 499271215 560 ----LRKDLRG 566
Cdd:PRK13295 534 qkfrLREMLRG 544
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
31-565 |
5.49e-55 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 194.59 E-value: 5.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 31 PLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGF 110
Cdd:PRK06155 17 PPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 111 TVVNVNPLYTPRELEHQLVDAGAKAIFV----LENFAHTVEQVLARTEVKhvvvasmgdMLGAkgaivnlvvrrvkklVP 186
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVeaalLAALEAADPGDLPLPAVW---------LLDA---------------PA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 187 AWSIPGHLSFKTVLAKGATLgfKRPNVAPGDVAFLQYTGGTTGVSKGATLTHAnllsnmaQMELW-LNTAFLRKPRPESL 265
Cdd:PRK06155 153 SVSVPAGWSTAPLPPLDAPA--PAAAVQPGDTAAILYTSGTTGPSKGVCCPHA-------QFYWWgRNSAEDLEIGADDV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 266 TFMCaLPLYHIFALtvNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTF 345
Cdd:PRK06155 224 LYTT-LPLFHTNAL--NAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVAL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 346 GGGMAVQrpVAERWLELTGCPIHEGYGLSET-SPVATANRldtDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:PRK06155 301 GPGVPAA--LHAAFRERFGVDLLDGYGSTETnFVIAVTHG---SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQ---VMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAI 501
Cdd:PRK06155 376 ADEpfaFATGYFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 502 GVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK06155 455 PVPSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
36-558 |
2.53e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 192.41 E-value: 2.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 36 SIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNV 115
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 116 NPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTE-VKHVVVasMGDMLGAKGAivnlvvrrvkklvpawsiPGHL 194
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPkLRTLVV--VEDGSGNDLL------------------PGAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 195 SFKTVLAKGATlgfKRPNVAP-GDVAFLQYTGGTTGVSKGATLTHANLLsnMAQMElwlNTAFLRKPRPESL-------- 265
Cdd:PRK07798 144 DYEDALAAGSP---ERDFGERsPDDLYLLYTGGTTGMPKGVMWRQEDIF--RVLLG---GRDFATGEPIEDEeelakraa 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 266 -----TFMCALPLYHIFALTvNSLMGLATGGNNILIPNPR-DIPAFVKELGRYRTNIF---------PglntLFNALMNN 330
Cdd:PRK07798 216 agpgmRRFPAPPLMHGAGQW-AAFAALFSGQTVVLLPDVRfDADEVWRTIEREKVNVItivgdamarP----LLDALEAR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 331 SEFrklDFSSLILTFGGGMAVQRPVAERWLELTgcP---IHEGYGLSET----SPVATANRLDTDDFTGTIGiplPSTEV 403
Cdd:PRK07798 291 GPY---DLSSLFAIASGGALFSPSVKEALLELL--PnvvLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIG---PRTVV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 404 eiRDEDGRTLPVG--EIGEICIRGPqVMAGYWQRPEETARAispdgfFRT---------GDVGFMNAEGLTKIVDRKKDM 472
Cdd:PRK07798 363 --LDEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPEKTAET------FPTidgvryaipGDRARVEADGTITLLGRGSVC 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 473 ILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-VRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTEL 551
Cdd:PRK07798 434 INTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVqLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEV 513
|
....*..
gi 499271215 552 PKSNVGK 558
Cdd:PRK07798 514 QRSPAGK 520
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
61-565 |
2.72e-54 |
|
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: 190.02 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYT---PRELEHQLVDAGAKAIF 137
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 vlenfahTVEQVLARTEvkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvaPGD 217
Cdd:cd05969 78 -------TTEELYERTD------------------------------------------------------------PED 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNmaqmelWLNTAFLRKPRPESLTFMCALP------LYHIFALTVNslmglatGG 291
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFY------YFTGKYVLDLHPDDIYWCTADPgwvtgtVYGIWAPWLN-------GV 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 292 NNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEF--RKLDFSSLILTFGGGMAVQrPVAERW-LELTGCPIH 368
Cdd:cd05969 158 TNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIH 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 369 EGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRG--PQVMAGYWQRPEETARAIsPD 446
Cdd:cd05969 237 DTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-ID 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNLTE 525
Cdd:cd05969 316 GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlKEGFEPSD 395
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499271215 526 E---EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05969 396 ElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
62-565 |
1.18e-53 |
|
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: 190.75 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWL-QSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:cd05928 43 SFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQVLARTEvkhvvvasmgdmlgakgaivNLvvrRVKKLVPAWSIPGHLSFKTVLAKGATlgfKRPNVAPG--DV 218
Cdd:cd05928 123 ELAPEVDSVASECP--------------------SL---KTKLLVSEKSRDGWLNFKELLNEAST---EHHCVETGsqEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLsnmaqMELWLNTAFLRKPRPeSLTFMCALPLYHIFAlTVNSLMGLATGGNNILIPN 298
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHSHSSLG-----LGLKVNGRYWLDLTA-SDIMWNTSDTGWIKS-AWSSLFEPWIQGACVFVHH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 299 -PR-DIPAFVKELGRYRTNIFPGLNTLFNALMNNsEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSET 376
Cdd:cd05928 250 lPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTET 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 377 SPVAtANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR-GPQ----VMAGYWQRPEETARAISPDgFFRT 451
Cdd:cd05928 329 GLIC-ANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD-FYLT 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 452 GDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV------RKDPNLTE 525
Cdd:cd05928 407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflSHDPEQLT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499271215 526 EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05928 487 KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
51-565 |
2.67e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 189.95 E-value: 2.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCM---GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQ 127
Cdd:PRK06164 23 RPDAVALideDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 128 LVDAGAKAIFVLENFaHTVEQVLARTEVKHVVVasmgdmLGAKGAIVnlvVRRVkklvpAWSIPGHLSFKTV----LAKG 203
Cdd:PRK06164 103 LGRGRARWLVVWPGF-KGIDFAAILAAVPPDAL------PPLRAIAV---VDDA-----ADATPAPAPGARVqlfaLPDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 204 ATLGFKRPNVAPGDVAFLQYT-GGTTGVSK------GATLTHANLLSNMAQMElwlntaflrkprPESLTfMCALPLYHI 276
Cdd:PRK06164 168 APPAAAGERAADPDAGALLFTtSGTTSGPKlvlhrqATLLRHARAIARAYGYD------------PGAVL-LAALPFCGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 277 FALtvNSLMGLATGGNNILIPNPRDIPAFVKELGRYR-TNIFpGLNTLFnALMNNSEFRKLDFSSL----ILTFGGGMav 351
Cdd:PRK06164 235 FGF--STLLGALAGGAPLVCEPVFDAARTARALRRHRvTHTF-GNDEML-RRILDTAGERADFPSArlfgFASFAPAL-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 352 qRPVAErWLELTGCPIHEGYGLSETSPVATANRLDtDDFTGTI---GIPL-PSTEVEIRD-EDGRTLPVGEIGEICIRGP 426
Cdd:PRK06164 309 -GELAA-LARARGVPLTGLYGSSEVQALVALQPAT-DPVSVRIeggGRPAsPEARVRARDpQDGALLPDGESGEIEIRAP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 427 QVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVAdp 506
Cdd:PRK06164 386 SLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-- 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 507 HSGEAVKL-FVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELP---KSNVGKILRKDLR 565
Cdd:PRK06164 464 RDGKTVPVaFVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLR 527
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
62-500 |
4.00e-53 |
|
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: 185.93 E-value: 4.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSL-GLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHtveqvlartevkhvvvasmgDMLGAKGAIVNLVVRRVKKLVPAWSIPGHlsfktvlakgatlgfkRPNVAPGDVAF 220
Cdd:TIGR01733 81 ALAS--------------------RLAGLVLPVILLDPLELAALDDAPAPPPP----------------DAPSGPDDLAY 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLRKPRPESLTFMCalplYHiFALTVNSLMGLATGGNNILIPNPR 300
Cdd:TIGR01733 125 VIYTSGSTGRPKGVVVTHRSLVNLLA----WLARRYGLDPDDRVLQFAS----LS-FDASVEEIFGALLAGATLVVPPED 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 301 DIPAFVKELGR----YRTNIFPGLNTLFNALMnnsEFRKLDFSSLILTFGGGMAVQRPVAERWLELTG-CPIHEGYGLSE 375
Cdd:TIGR01733 196 EERDDAALLAAliaeHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 376 TSPVATANRLDTDDFTGT----IGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF--- 448
Cdd:TIGR01733 273 TTVWSTATLVDPDDAPREspvpIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagg 352
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 449 -----FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:TIGR01733 353 dgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
38-564 |
5.01e-53 |
|
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: 187.87 E-value: 5.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 38 GEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNP 117
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 118 LYTPRELEHQLVDAGAKAifvlenfahtveqVLARTEVKHVvvasmgdmlGAKGAIVNLVVRRVKKLVPAwSIPGhlsfk 197
Cdd:cd17646 81 GYPADRLAYMLADAGPAV-------------VLTTADLAAR---------LPAGGDVALLGDEALAAPPA-TPPL----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 198 tvlakgatlgfkrPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMaqmeLWLNTAFLRKPRPESLtfmCALPLYhiF 277
Cdd:cd17646 133 -------------VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRL----LWMQDEYPLGPGDRVL---QKTPLS--F 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 278 ALTVNSLMG-LATGGNnILIPNP---RDIPAFVKELGRYR---TNIFPGLNTLFNALMNNSEFRkldfsSLILTFGGGMA 350
Cdd:cd17646 191 DVSVWELFWpLVAGAR-LVVARPgghRDPAYLAALIREHGvttCHFVPSMLRVFLAEPAAGSCA-----SLRRVFCSGEA 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 351 VQRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGT--IGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQV 428
Cdd:cd17646 265 LPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 429 MAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIG 502
Cdd:cd17646 345 ARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVA 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 503 VADPHSGEAVKLFVVRKD--PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17646 425 RAAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
39-564 |
1.07e-52 |
|
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: 187.02 E-value: 1.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPL 118
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVDAGAKAIFVLEnfahTVEQVLARTEVkhVVVASMGDMLGAKGAIvnlvvrrvkklvpawsipghlsfkt 198
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDR----SLAGRAGGLEV--AVVIDEALDAGPAGNP------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 vlakgatlgfkRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSnmaqmeLWLNTAFLRkPRPESlTFMCALPL----- 273
Cdd:cd12117 130 -----------AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR------LVKNTNYVT-LGPDD-RVLQTSPLafdas 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 -YHIFAltvnslmGLATGGNNILIP--NPRDIPAFVKELGRYRTNIFPGLNTLFNALmnnSEFRKLDFSSL--ILTfgGG 348
Cdd:cd12117 191 tFEIWG-------ALLNGARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQL---ADEDPECFAGLreLLT--GG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 349 MAVQRPVAERWLEltGCP---IHEGYGLSETSPVATANRLDTDDFTGT---IGIPLPSTEVEIRDEDGRTLPVGEIGEIC 422
Cdd:cd12117 259 EVVSPPHVRRVLA--ACPglrLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIANTRVYVLDEDGRPVPPGVPGELY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 423 IRGPQVMAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGIL 496
Cdd:cd12117 337 VGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 497 ECAAigVADPHSGEAVKL--FVVrKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd12117 417 EAVV--VVREDAGGDKRLvaYVV-AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-565 |
1.65e-52 |
|
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: 186.35 E-value: 1.65e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 31 PLTYRSigeFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNIlqnPVIV---YGILR 107
Cdd:cd12118 3 PLTPLS---FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNT---PAMYelhFGVPM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 108 AGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHtvEQVLARtevkhvvvasmGDmlgakgaivnlvvRRVKKLVPA 187
Cdd:cd12118 77 AGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFEY--EDLLAE-----------GD-------------PDFEWIPPA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 188 --WsipghlsfktvlakgatlgfkrpnvapgDVAFLQYTGGTTGVSKGATLTH----ANLLSNMAQMELWLNTAFLrkpr 261
Cdd:cd12118 131 deW----------------------------DPIALNYTSGTTGRPKGVVYHHrgayLNALANILEWEMKQHPVYL---- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 262 pesltfmCALPLYHI----FALTVNslmglATGGNNILIPNPrDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLD 337
Cdd:cd12118 179 -------WTLPMFHCngwcFPWTVA-----AVGGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARP 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 338 FSSLILTFGGGMAVQRPVAERWLELTGCPIHeGYGLSETSPVATA-------NRLDTDDFTGTI---GIPLPS-TEVEIR 406
Cdd:cd12118 246 LPHRVHVMTAGAPPPAAVLAKMEELGFDVTH-VYGLTETYGPATVcawkpewDELPTEERARLKarqGVRYVGlEEVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 407 DEDGrTLPV---GE-IGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFP 482
Cdd:cd12118 325 DPET-MKPVprdGKtIGEIVFRGNIVMKGYLKNPEATAEAFR-GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISS 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 483 NEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRtELPKSNVGKILR 561
Cdd:cd12118 403 VEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQK 481
|
....
gi 499271215 562 KDLR 565
Cdd:cd12118 482 FVLR 485
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
41-565 |
1.06e-51 |
|
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: 184.47 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 41 FDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYT 120
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 121 PRELEHQLVDAGAKAIFvlenfahTVEQVLARTEVKHVVVASMGDMLGAKGAIVNLVVRrvkklvpawsipghlsfktvl 200
Cdd:cd17651 81 AERLAFMLADAGPVLVL-------THPALAGELAVELVAVTLLDQPGAAAGADAEPDPA--------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 201 akgatlgfkrpnVAPGDVAFLQYTGGTTGVSKGATLTHANLLsNMAQmelWLNTAFLRKPRPESLTFmcALPLYHIFALT 280
Cdd:cd17651 133 ------------LDADDLAYVIYTSGSTGRPKGVVMPHRSLA-NLVA---WQARASSLGPGARTLQF--AGLGFDVSVQE 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 281 VNSlmGLATGGNNILIPNP--RDIPAFVKELGRYRTNI----FPGLNTLFNAlMNNSEFRKLDFSSLILtfGGGMAVQRP 354
Cdd:cd17651 195 IFS--TLCAGATLVLPPEEvrTDPPALAAWLDEQRISRvflpTVALRALAEH-GRPLGVRLAALRYLLT--GGEQLVLTE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 355 VAERWL-ELTGCPIHEGYGLSETSpVATANRLDTD----DFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVM 429
Cdd:cd17651 270 DLREFCaGLPGLRLHNHYGPTETH-VVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGV 503
Cdd:cd17651 349 RGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAR 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 504 ADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAASLTNYKRP-RYVEFRTeLPKSNVGKILRKDLR 565
Cdd:cd17651 429 EDRPGEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPsAFVLLDA-LPLTPNGKLDRRALP 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
223-553 |
1.65e-51 |
|
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: 179.42 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 223 YTGGTTGVSKGATLTHANLLSnMAqmelwLNTAFLRKPRPESlTFMCALPLYHIfaltvNSLMG-LAT---GGNNILIP- 297
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLA-QA-----LVLAVLQAIDEGT-VFLNSGPLFHI-----GTLMFtLATfhaGGTNVFVRr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 -NPRDIPAFVKELGRYRTNIFPglnTLFNALMNNSEFRKLDFSSL--ILTFGGGMAVQRPVAERWLELTGcpiheGYGLS 374
Cdd:cd17636 75 vDAEEVLELIEAERCTHAFLLP---PTIDQIVELNADGLYDLSSLrsSPAAPEWNDMATVDTSPWGRKPG-----GYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 375 ETSPVATANRLDTDDfTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAiSPDGFFRTGDV 454
Cdd:cd17636 147 EVMGLATFAALGGGA-IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARR-TRGGWHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 455 GFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCA 533
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVTEAELIEHCR 304
|
330 340
....*....|....*....|
gi 499271215 534 ASLTNYKRPRYVEFRTELPK 553
Cdd:cd17636 305 ARIASYKKPKSVEFADALPR 324
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
51-564 |
4.12e-51 |
|
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: 182.11 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYtPRE-LEHQLV 129
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 130 DAGAKAIfvlenfahtveqvLARTEVKHvvvasmgdmlgakgaivnlvvrRVKKLVPAWSIPGhlsfktvLAKGATLGFK 209
Cdd:cd12116 82 DAEPALV-------------LTDDALPD----------------------RLPAGLPVLLLAL-------AAAAAAPAAP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlntaflRKPRPESLTFMCAL--PLYHIFALTVnsLMGL 287
Cdd:cd12116 120 RTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR--------ERLGLGPGDRLLAVttYAFDISLLEL--LLPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 288 ATGGNniLIPNPRDIPAFVKELGRYRTNIFPglnTLFNA------LMNNSEFRKLD-FSSLIltfgGGMAVQRPVAERWL 360
Cdd:cd12116 190 LAGAR--VVIAPRETQRDPEALARLIEAHSI---TVMQAtpatwrMLLDAGWQGRAgLTALC----GGEALPPDLAARLL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 ELTGCpIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETA 440
Cdd:cd12116 261 SRVGS-LWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 441 RAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVK 513
Cdd:cd12116 340 ERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVA 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 514 lFVVRKDPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd12116 420 -YVVLKAGAaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
62-564 |
2.09e-50 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 179.57 E-value: 2.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLEN 141
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAhtveqvlartevKHVVVASMGDMLGAKGAivnlvvrrvkklvPAWSIPGHLSFKtvlakgatlgfkrpnvapgDVAFL 221
Cdd:TIGR01923 81 LE------------EKDFQADSLDRIEAAGR-------------YETSLSASFNMD-------------------QIATL 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 222 QYTGGTTGVSKGATLTHANLLSNMaqMELWLNTAFLRKPRpesltFMCALPLYHIFALTVnsLMGLATGGNNILIPNPRD 301
Cdd:TIGR01923 117 MFTSGTTGKPKAVPHTFRNHYASA--VGSKENLGFTEDDN-----WLLSLPLYHISGLSI--LFRWLIEGATLRIVDKFN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 302 ipAFVKELGRYRTNIFPGLNTLFNALMNNSEfRKLDFSSLILtfgGGMAVQRPVAERWLELtGCPIHEGYGLSETSPVAT 381
Cdd:TIGR01923 188 --QLLEMIANERVTHISLVPTQLNRLLDEGG-HNENLRKILL---GGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 382 ANRLDTDDFTGTIGIPLPSTEVEIRDEDgrtlpVGEIGEICIRGPQVMAGYWQrPEETARAISPDGFFRTGDVGFMNAEG 461
Cdd:TIGR01923 261 TATPEMLHARPDVGRPLAGREIKIKVDN-----KEGHGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDGEG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 462 LTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-RKDPNltEEEVKRHCAASLTNYK 540
Cdd:TIGR01923 335 FLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVsESDIS--QAKLIAYLTEKLAKYK 412
|
490 500
....*....|....*....|....
gi 499271215 541 RPRYVEFRTELPKSNVGKILRKDL 564
Cdd:TIGR01923 413 VPIAFEKLDELPYNASGKILRNQL 436
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
60-565 |
8.42e-50 |
|
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: 180.17 E-value: 8.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 60 ALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLvdagAKaifvL 139
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARL----RK----L 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 ENFAHTVEQ--VLARTEVkhvvvasmgdmlgakgaivnlvVRRVKKLVPAWSIPGhLSFKTVLAKGATLGFKR-PNVAPG 216
Cdd:cd05906 111 RHIWQLLGSpvVLTDAEL----------------------VAEFAGLETLSGLPG-IRVLSIEELLDTAADHDlPQSRPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSnmaqMELWLNTAFLRKPRPESLTFMcalPLYHIFALTVNSLMGLATGGNNILI 296
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILA----RSAGKIQHNGLTPQDVFLNWV---PLDHVGGLVELHLRAVYLGCQQVHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PNP---RDIPAFVKELGRYRTNIFPGLNTLFnALMNNS----EFRKLDFSSLILTFGGGMAVQRPVAERWLELT---GCP 366
Cdd:cd05906 241 PTEeilADPLRWLDLIDRYRVTITWAPNFAF-ALLNDLleeiEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLepyGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 ---IHEGYGLSETSPVATANRLD-TDDFTGT-----IGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPE 437
Cdd:cd05906 320 pdaIRPAFGMTETCSGVIYSRSFpTYDHSQAlefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDGFFRTGDVGFMNAEGLTkIVDRKKDMILVSGFNVFPNEIEEVAATHPGILE--CAAIGVADPHSG--EAVK 513
Cdd:cd05906 400 ANAEAFTEDGWFRTGDLGFLDNGNLT-ITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAEteELAI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 514 LFVVRKDPNL----TEEEVKRHCAASLTnyKRPRYV--EFRTELPKSNVGKILRKDLR 565
Cdd:cd05906 479 FFVPEYDLQDalseTLRAIRSVVSREVG--VSPAYLipLPKEEIPKTSLGKIQRSKLK 534
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
211-565 |
1.88e-49 |
|
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: 177.95 E-value: 1.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDvaFLQYTGGTTGVSKGATLTH-ANLLSNMAQMeLWlntAFLRKPRPESLTFMCAlPLYHIFALTVnSLMGLAT 289
Cdd:cd05929 122 EDEAAGW--KMLYSGGTTGRPKGIKRGLpGGPPDNDTLM-AA---ALGFGPGADSVYLSPA-PLYHAAPFRW-SMTALFM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNNILIPNpRDIPAFVKELGRYRTNIFPGLNTLFNALMN--NSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPI 367
Cdd:cd05929 194 GGTLVLMEK-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPII 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYGLSETSPVATANRLDTDDFTGTIGIPLPStEVEIRDEDGRTLPVGEIGEICIRGPQVMAgYWQRPEETARAISPDG 447
Cdd:cd05929 273 WEYYGGTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 448 FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-----VRKDPN 522
Cdd:cd05929 351 WSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapgADAGTA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499271215 523 LtEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05929 431 L-AEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
103-566 |
1.97e-49 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 184.36 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 103 YGILRAGFTVVNVNplYTprelehqlvdAGAKAIfvlenfAHTVEQvlarTEVKHVVVASMG-DMLGAKGAIVNLV---- 177
Cdd:PRK08633 683 LALLLAGKVPVNLN--YT----------ASEAAL------KSAIEQ----AQIKTVITSRKFlEKLKNKGFDLELPenvk 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 178 VRRVKKLVPAwsiPGHLSFKTVLAKGATL------GFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELW 251
Cdd:PRK08633 741 VIYLEDLKAK---ISKVDKLTALLAARLLparllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDV 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 252 LNTAflrkprpESLTFMCALPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNS 331
Cdd:PRK08633 818 FNLR-------NDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNK 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 332 EFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATAN---RLDTDDFT------GTIGIPLPSTE 402
Cdd:PRK08633 891 KLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNlpdVLAADFKRqtgskeGSVGMPLPGVA 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 403 VEIRD-EDGRTLPVGEIGEICIRGPQVMAGYWQRPEETA---RAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGF 478
Cdd:PRK08633 971 VRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGE 1050
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 479 NVFPNEIEEVAAT--HPGILECAAIGVADPHSGEavKLFVVRKDPNLTEEEVKRHCAAS-LTNYKRPRYVEFRTELPKSN 555
Cdd:PRK08633 1051 MVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLG 1128
|
490
....*....|.
gi 499271215 556 VGKIlrkDLRG 566
Cdd:PRK08633 1129 SGKL---DLKG 1136
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
61-566 |
3.36e-49 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 178.41 E-value: 3.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQVLArtevkhvvvasmgdmlGAKGAivnlvVRRVkklvpAWSIPGHLSfkTVLAKGATLGFKRPNVAP--GDV 218
Cdd:PRK13382 149 EFSATVDRALA----------------DCPQA-----TRIV-----AWTDEDHDL--TVEVLIAAHAGQRPEPTGrkGRV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLqyTGGTTGVSKGATltHANLLSNMAqmelwLNTAFLRKP-RPESLTFMCAlPLYHIFALtvnSLMGLATGGNNILIP 297
Cdd:PRK13382 201 ILL--TSGTTGTPKGAR--RSGPGGIGT-----LKAILDRTPwRAEEPTVIVA-PMFHAWGF---SQLVLAASLACTIVT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPR-DIPAFVKELGRYRTNIFPGLNTLFNALMNNSE--FRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLS 374
Cdd:PRK13382 268 RRRfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNAT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 375 ETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYwqRPEETARAIspDGFFRTGDV 454
Cdd:PRK13382 348 EAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH--DGFMASGDV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 455 GFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK-DPNLTEEEVKRHCA 533
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKpGASATPETLKQHVR 503
|
490 500 510
....*....|....*....|....*....|...
gi 499271215 534 ASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK13382 504 DNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
51-564 |
9.70e-48 |
|
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: 172.49 E-value: 9.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd17643 3 AVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAIfvlenfahtveqvlartevkhvvvasMGDmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd17643 83 SGPSLL--------------------------LTD--------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvaPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaFLRKPRpesltfmcaLPLYHIFAL--TVNSLMG-L 287
Cdd:cd17643 92 ----PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFG--FNEDDV---------WTLFHSYAFdfSVWEIWGaL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 288 ATGGNNILIPN-----PRDIPAFVKELGRYRTNIFPglnTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL 362
Cdd:cd17643 157 LHGGRLVVVPYevarsPEDFARLLRDEGVTVLNQTP---SAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHE---GYGLSETSPVATANRLDTDDFTG----TIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQR 435
Cdd:cd17643 234 FGLDRPQlvnMYGITETTVHVTFRPLDAADLPAaaasPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 436 PEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEcAAIGVADPHS 508
Cdd:cd17643 314 PELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRD-AAVIVREDEP 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 509 GEA--VKLFVVRKDPNLTEEEVKRHCAASLTNYKRP-RYVEFrTELPKSNVGKILRKDL 564
Cdd:cd17643 393 GDTrlVAYVVADDGAAADIAELRALLKELLPDYMVPaRYVPL-DALPLTVNGKLDRAAL 450
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
51-565 |
1.81e-47 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 173.64 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGftVVNVNPLYTPRELEhqlvd 130
Cdd:PRK10946 39 AIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSE----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 agakaifvLENFAHTVEQVLartevkhvVVASMGDMLGAKGAIVNLVVRRVKKL--VPAWSIPGHLSFKTVLAKGATlGF 208
Cdd:PRK10946 112 --------LNAYASQIEPAL--------LIADRQHALFSDDDFLNTLVAEHSSLrvVLLLNDDGEHSLDDAINHPAE-DF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 209 KRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLL-SNMAQMELWLNTAFLRkprpesltFMCALPLYHIFALTVNSLMG- 286
Cdd:PRK10946 175 TATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYySVRRSVEICGFTPQTR--------YLCALPAAHNYPMSSPGALGv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGGNNILIPNPRDIPAFvKELGRYRTNI---FPGLNTLFNALMNNSEFRKlDFSSLILTFGGGMAVQRPVAERWLELT 363
Cdd:PRK10946 247 FLAGGTVVLAPDPSATLCF-PLIEKHQVNVtalVPPAVSLWLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 GCPIHEGYGLSETspVATANRLDTDD---FTgTIGIPL-PSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:PRK10946 325 GCQLQQVFGMAEG--LVNYTRLDDSDeriFT-TQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK 519
Cdd:PRK10946 402 ASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 499271215 520 DPnLTEEEVKRHC-AASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK10946 482 EP-LKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
35-565 |
3.10e-47 |
|
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: 178.13 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYtPRE-LEHQLVDAGAKAIFVLENFAhtveQVLARTEVKHVVVasmgDMLGAKGAivnlvvrrvkklvPAWSIPgh 193
Cdd:COG1020 556 LDPAY-PAErLAYMLEDAGARLVLTQSALA----ARLPELGVPVLAL----DALALAAE-------------PATNPP-- 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 lsfktvlakgatlgfkrPNVAPGDVAFLQYTGGTTGVSKGATLTH---ANLLSNMAQ-MEL-----WLNTAflrkprpeS 264
Cdd:COG1020 612 -----------------VPVTPDDLAYVIYTSGSTGRPKGVMVEHralVNLLAWMQRrYGLgpgdrVLQFA--------S 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 265 LTF-MCALPLYhifaltvnslMGLATGGNNILIPN--PRDIPAFVKELGRYRTNIF---PglnTLFNALMnnsEFRKLDF 338
Cdd:COG1020 667 LSFdASVWEIF----------GALLSGATLVLAPPeaRRDPAALAELLARHRVTVLnltP---SLLRALL---DAAPEAL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 SSLILTFGGGMAVQRPVAERWLE-LTGCPIHEGYGLSETSPVATANRLDTDDFTG---TIGIPLPSTEVEIRDEDGRTLP 414
Cdd:COG1020 731 PSLRLVLVGGEALPPELVRRWRArLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVYVLDAHLQPVP 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 415 VGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEE 487
Cdd:COG1020 811 VGVPGELYIGGAGLARGYLNRPELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEA 890
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 488 VAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:COG1020 891 ALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLAL 968
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
217-565 |
5.95e-45 |
|
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: 161.73 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSNmAQMELwlntAFLRKPRPESltFMCALPLYHIFALTVnSLMGLATGGNNILI 296
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAS-AAGLH----SRLGFGGGDS--WLLSLPLYHVGGLAI-LVRSLLAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 PNPRDIPAFVKELGRYRTNIFPglNTLFNALMNNSEFRKLDfsSLILTFGGGMAVQRPVAERWLELtGCPIHEGYGLSET 376
Cdd:cd17630 73 ERNQALAEDLAPPGVTHVSLVP--TQLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 377 SPVATANRLDTDDfTGTIGIPLPSTEVEIRDEdgrtlpvgeiGEICIRGPQVMAGYWQRPEETARAisPDGFFRTGDVGF 456
Cdd:cd17630 148 ASQVATKRPDGFG-RGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQLVPEFN--EDGWFTTKDLGE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 457 MNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNlTEEEVKRHCAASL 536
Cdd:cd17630 215 LHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGPA-DPAELRAWLKDKL 293
|
330 340
....*....|....*....|....*....
gi 499271215 537 TNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd17630 294 ARFKLPKRIYPVPELPRTGGGKVDRRALR 322
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
42-565 |
7.52e-45 |
|
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: 167.67 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 42 DHAVAQYSWRPAFTCMG-----KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVN 116
Cdd:cd05968 68 DKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 117 PLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVlartEVKHVVVASMGDMLGAKGAIVnlvVRRVKKLVPAwsIPGHLSF 196
Cdd:cd05968 148 SGFGKEAAATRLQDAEAKALITADGFTRRGREV----NLKEEADKACAQCPTVEKVVV---VRHLGNDFTP--AKGRDLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 197 KTVLAKGATLGFKRpnVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwlNTAFLRKPRP-ESLTFMCAL---- 271
Cdd:cd05968 219 YDEEKETAGDGAER--TESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQ-----DMYFQFDLKPgDLLTWFTDLgwmm 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 272 -PLYHIFALTVNSLMGLATGGNNIliPNPRDIPAFVKelgRYRTNIFpGLN-TLFNALMNNSE--FRKLDFSSLILtFGG 347
Cdd:cd05968 292 gPWLIFGGLILGATMVLYDGAPDH--PKADRLWRMVE---DHEITHL-GLSpTLIRALKPRGDapVNAHDLSSLRV-LGS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 GMAVQRPVAERWL-ELTG---CPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPvGEIGEICI 423
Cdd:cd05968 365 TGEPWNPEPWNWLfETVGkgrNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 424 RGPQV-MA-GYWQRPEETARAI--SPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECA 499
Cdd:cd05968 444 LAPWPgMTrGFWRDEDRYLETYwsRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271215 500 AIGVADPHSGEAVKLFVVRKdPNLT-----EEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05968 524 AIGVPHPVKGEAIVCFVVLK-PGVTptealAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
61-488 |
7.67e-45 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 166.62 E-value: 7.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGL--AKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYtpreleHQLvdaGAKAI-F 137
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTV---PLY------DTL---GPEAIeY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENfahtveqvlarTEVKHVVVAsmgdmlgaKGaiVNLVvrrvkklvpawsipghlSFKTVLAKGAtlgFKRPNVAPG- 216
Cdd:cd05927 74 ILNH-----------AEISIVFCD--------AG--VKVY-----------------SLEEFEKLGK---KNKVPPPPPk 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 --DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaFLRKPRPEsLTFMCALPLYHIF-ALTVNSLM--GLATG- 290
Cdd:cd05927 113 peDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILE--ILNKINPT-DVYISYLPLAHIFeRVVEALFLyhGAKIGf 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 --GNNILIPN------PRDIPAFVKELGRYRTNIFPGLN-------TLFNALMNNSE-------------FRKLDFSSLI 342
Cdd:cd05927 190 ysGDIRLLLDdikalkPTVFPGVPRVLNRIYDKIFNKVQakgplkrKLFNFALNYKLaelrsgvvraspfWDKLVFNKIK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 343 LTFGG-------GMAVQRPVAERWLELT-GCPIHEGYGLSETSPVATANRLDtDDFTGTIGIPLPSTEVEIRD------- 407
Cdd:cd05927 270 QALGGnvrlmltGSAPLSPEVLEFLRVAlGCPVLEGYGQTECTAGATLTLPG-DTSVGHVGGPLPCAEVKLVDvpemnyd 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 408 ---EDGRtlpvgeiGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMI-LVSGFNVFPN 483
Cdd:cd05927 349 akdPNPR-------GEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPE 421
|
....*
gi 499271215 484 EIEEV 488
Cdd:cd05927 422 KIENI 426
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
61-565 |
9.05e-45 |
|
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: 164.23 E-value: 9.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYT---PRELEHQLVDAGAKAIf 137
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 vlenfahtveqvlartevkhvvvasmgdmlgakgaIVNLVVRrvkklvpawsipghlsfktvlAKGATlgfkrpnvapgD 217
Cdd:cd05973 77 -----------------------------------VTDAANR---------------------HKLDS-----------D 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrkpRPESLTFMCALP-----LYhiFALTVNSLMGLATggn 292
Cdd:cd05973 90 PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL------RPEDSFWNAADPgwaygLY--YAITGPLALGHPT--- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 293 nILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSefrkldfSSLILTFGGGMAVQRPVAE-------RWLELT-G 364
Cdd:cd05973 159 -ILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAG-------AEVPARPKGRLRRVSSAGEpltpeviRWFDAAlG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 365 CPIHEGYGLSETS-PVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICI---RGPQV-MAGYWQRPEET 439
Cdd:cd05973 231 VPIHDHYGQTELGmVLANHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPA 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 araisPDG-FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV- 517
Cdd:cd05973 311 -----IDGgYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVl 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 518 ----RKDPNLtEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05973 386 rgghEGTPAL-ADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
26-565 |
2.03e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 165.51 E-value: 2.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 26 PAEIGPLTYRSigeFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNIlqnPVIV--- 102
Cdd:PRK08162 12 AANYVPLTPLS---FLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNI---PAMVeah 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 103 YGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGAIVnlvvrrvk 182
Cdd:PRK08162 86 FGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDDPEYPGGRFI-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 183 klvpawsipGHLSFKTVLAKGatlgfkRPNVA---PGD----VAfLQYTGGTTGVSKGATLTHA----NLLSNMAQMELw 251
Cdd:PRK08162 158 ---------GALDYEAFLASG------DPDFAwtlPADewdaIA-LNYTSGTTGNPKGVVYHHRgaylNALSNILAWGM- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 252 lntaflrKPRPeslTFMCALPLYHI----FALTVNslmglATGGNNILIpnpRDI-PAFVKELGR-YRTNIFPGLNTLFN 325
Cdd:PRK08162 221 -------PKHP---VYLWTLPMFHCngwcFPWTVA-----ARAGTNVCL---RKVdPKLIFDLIReHGVTHYCGAPIVLS 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 326 ALMNNSEFRKLDFSSLILTFGGG----MAVQRPVAERWLELTgcpiHEgYGLSET-SPVATA------NRLDTDD---FT 391
Cdd:PRK08162 283 ALINAPAEWRAGIDHPVHAMVAGaappAAVIAKMEEIGFDLT----HV-YGLTETyGPATVCawqpewDALPLDEraqLK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 392 GTIGIPLPSTEvEIRDEDGRTL-PV---GE-IGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIV 466
Cdd:PRK08162 358 ARQGVRYPLQE-GVTVLDPDTMqPVpadGEtIGEIMFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLHPDGYIKIK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 467 DRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFV-VRKDPNLTEEEVKRHCAASLTNYKRPRYV 545
Cdd:PRK08162 436 DRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVeLKDGASATEEEIIAHCREHLAGFKVPKAV 515
|
570 580
....*....|....*....|
gi 499271215 546 EFrTELPKSNVGKILRKDLR 565
Cdd:PRK08162 516 VF-GELPKTSTGKIQKFVLR 534
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
51-565 |
9.61e-44 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 162.87 E-value: 9.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTC--MGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQL 128
Cdd:PRK13390 13 RPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 129 VDAGAKAIfvlenfahtveqvlartevkhVVVASMGDMLGAKGAIVNLvvrrvkKLVPAWSIPGHLSFKTVLAKGATLGF 208
Cdd:PRK13390 93 GDSGARVL---------------------VASAALDGLAAKVGADLPL------RLSFGGEIDGFGSFEAALAGAGPRLT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 209 KRPNVApgdvaFLQYTGGTTGVSKG---------------ATLTHANLLSNMAQMELWLNTAflrkprpesltfmcalPL 273
Cdd:PRK13390 146 EQPCGA-----VMLYSSGTTGFPKGiqpdlpgrdvdapgdPIVAIARAFYDISESDIYYSSA----------------PI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 YHIFALTVNSLMGlATGGNnILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN-NSEFR-KLDFSSLILTFGGGMAV 351
Cdd:PRK13390 205 YHAAPLRWCSMVH-ALGGT-VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKlDADVRtRYDVSSLRAVIHAAAPC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 352 QRPVAERWLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTeVEIRDEDGRTLPVGEIGEICIRGPQVMAG 431
Cdd:PRK13390 283 PVDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 432 YWQRPEETARAISPDGFFRT--GDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSG 509
Cdd:PRK13390 362 YLNDPEKTAAAQHPAHPFWTtvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271215 510 EAVKLFV-----VRKDPNLTEEEVKrHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK13390 442 EQVKAVIqlvegIRGSDELARELID-YTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
12-545 |
7.86e-42 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 158.88 E-value: 7.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 12 STAKIWLGSYPPGvpAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVM 91
Cdd:PRK08279 16 PDLPGILRGLKRT--ALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 92 MPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKG 171
Cdd:PRK08279 94 MENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 172 AIVNL--VVRRVKKLVPAWsipghlsfktvlakgatlgfkRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMe 249
Cdd:PRK08279 174 GYEDLaaAAAGAPTTNPAS---------------------RSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGF- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 250 lwlntAFLRKPRPESlTFMCALPLYHIFALTVNSLMGLATGGNNILipnpR---------------DIPAF--VKELGRY 312
Cdd:PRK08279 232 -----GGLLRLTPDD-VLYCCLPLYHNTGGTVAWSSVLAAGATLAL----RrkfsasrfwddvrryRATAFqyIGELCRY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 313 rtnifpglntlfnaLMNNSEfRKLDFS-SLILTFGGGMavqRP-VAERWLELTGCP-IHEGYGLSEtSPVATANrldTDD 389
Cdd:PRK08279 302 --------------LLNQPP-KPTDRDhRLRLMIGNGL---RPdIWDEFQQRFGIPrILEFYAASE-GNVGFIN---VFN 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 390 FTGTIGI-PLPS------------TEVEIRDEDGRTLPV--GEIGE----ICIRGPqvMAGYWQrPEETARAISPDGF-- 448
Cdd:PRK08279 360 FDGTVGRvPLWLahpyaivkydvdTGEPVRDADGRCIKVkpGEVGLligrITDRGP--FDGYTD-PEASEKKILRDVFkk 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 449 ----FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADP-HSGEA--VKLfVVRKDP 521
Cdd:PRK08279 437 gdawFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPgTDGRAgmAAI-VLADGA 515
|
570 580
....*....|....*....|....
gi 499271215 522 NLTEEEVKRHCAASLTNYKRPRYV 545
Cdd:PRK08279 516 EFDLAALAAHLYERLPAYAVPLFV 539
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
61-536 |
1.89e-41 |
|
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: 156.47 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFV-- 138
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 139 LENFAHTveqvlartevKHVVVASMGDMLgakgaivnlvvrrvkkLVPAWSIPGHLSFKTVLAKGATLGfKRPNVAPGDV 218
Cdd:cd05932 87 LDDWKAM----------APGVPEGLISIS----------------LPPPSAANCQYQWDDLIAQHPPLE-ERPTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLThanlLSNMAqmelWLNTAFLRKPRPESLTFMCA-LPLYHIFALTVNSLMGLATGgnnILIP 297
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLT----FGSFA----WAAQAGIEHIGTEENDRMLSyLPLAHVTERVFVEGGSLYGG---VLVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNIF---PGLNTLFN-ALMNNSEFRKLD-------FSSLI-------------LTFGGGMAVQR 353
Cdd:cd05932 209 FAESLDTFVEDVQRARPTLFfsvPRLWTKFQqGVQDKIPQQKLNlllkipvVNSLVkrkvlkglgldqcRLAGCGSAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 354 PVAERWLELTGCPIHEGYGLSETSPVATANRlDTDDFTGTIGIPLPSTEVEIRDEdgrtlpvgeiGEICIRGPQVMAGYW 433
Cdd:cd05932 289 PALLEWYRSLGLNILEAYGMTENFAYSHLNY-PGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 434 QRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS-GFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAV 512
Cdd:cd05932 358 KDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAPLALV 437
|
490 500
....*....|....*....|....*.
gi 499271215 513 KL--FVVRKDPNLTEEEVKRHCAASL 536
Cdd:cd05932 438 VLseEARLRADAFARAELEASLRAHL 463
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
51-564 |
8.28e-41 |
|
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: 153.97 E-value: 8.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKaiFVLenfahtVEQVLARTEVKHVVVASMGDMLGAKGAIVNLVVrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd12114 83 AGAR--LVL------TDGPDAQLDVAVFDVLILDLDALAAPAPPPPVD-------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMelwlNTAFLRKPRPESL---TFMCALPLYHIFALtvnslmgL 287
Cdd:cd12114 123 --VAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI----NRRFAVGPDDRVLalsSLSFDLSVYDIFGA-------L 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 288 ATGGNnILIPNP---RDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSL--ILTFGGGMAVQRPVAERWLeL 362
Cdd:cd12114 190 SAGAT-LVLPDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLrlVLLSGDWIPLDLPARLRAL-A 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHEGYGLSETSPVATANRLD-TDDFTGTI--GIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:cd12114 268 PDARLISLGGATEASIWSIYHPIDeVPPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELT 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARA--ISPDG--FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHsGEAVKLF 515
Cdd:cd12114 348 AARfvTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPG-GKRLAAF 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499271215 516 VV--RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd12114 427 VVpdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
39-564 |
3.29e-40 |
|
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: 151.70 E-value: 3.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPL 118
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVDAGAKaifvlenfahtveqvlartevkHVVVAsmgdmlgakgaivnlvvrrvkklvpawsipghlsfkt 198
Cdd:cd12115 83 YPPERLRFILEDAQAR----------------------LVLTD------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 vlakgatlgfkrpnvaPGDVAFLQYTGGTTGVSKGATLTHANLlSNMAQmelWLNTAFLRKPRPESL--TFMCalplyhi 276
Cdd:cd12115 104 ----------------PDDLAYVIYTSGSTGRPKGVAIEHRNA-AAFLQ---WAAAAFSAEELAGVLasTSIC------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 277 FALTVNSLMG-LATGGNNILIPNPRDIPAFVKELGRYRTNIFPglnTLFNALMnnsEFRKLDFSSLILTFGGGMAVQRPV 355
Cdd:cd12115 157 FDLSVFELFGpLATGGKVVLADNVLALPDLPAAAEVTLINTVP---SAAAELL---RHDALPASVRVVNLAGEPLPRDLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWLELTGCPIHEGYGLSETSPVATANRLDTDDF-TGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQ 434
Cdd:cd12115 231 QRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASgEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 435 RPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHS 508
Cdd:cd12115 311 RPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 509 GEAVKLFVVRKDPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd12115 391 ERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
61-565 |
3.84e-40 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 153.90 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGfTVVNvnPLYT---PRELEHQLVDAGAKAIF 137
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNG-AIVG--PLFEafmEEAVRDRLEDSEAKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 vlenfahTVEQVLAR------TEVKHVVVasmgdmlgakgaiVNLVVRrvkklvpawSIPGHLSFKTvLAKGATLGFKRP 211
Cdd:PRK04319 151 -------TTPALLERkpaddlPSLKHVLL-------------VGEDVE---------EGPGTLDFNA-LMEQASDEFDIE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 NVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtafLRkprpESLTFMC-ALP------LYHIFALTVNsl 284
Cdd:PRK04319 201 WTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVLD---LH----EDDVYWCtADPgwvtgtSYGIFAPWLN-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 mglatGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN-NSE-FRKLDFSSL--ILTFGGGMavqRPVAERW- 359
Cdd:PRK04319 272 -----GATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGaGDDlVKKYDLSSLrhILSVGEPL---NPEVVRWg 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 360 LELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRG--PQVMAGYWQRPE 437
Cdd:PRK04319 344 MKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:PRK04319 424 KYESYFA-GDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVA 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 518 RKDPNLTEEEVKR----HCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK04319 503 LRPGYEPSEELKEeirgFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
61-565 |
6.17e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 151.86 E-value: 6.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGlAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:PRK07638 27 LTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFahtveqvlartevkhvvvasMGDMLGAKGAIVNL--VVRRVKKLVPAWSI---PGHLSFktvlakgatlgfkrpnvap 215
Cdd:PRK07638 106 YK--------------------LNDLPDEEGRVIEIdeWKRMIEKYLPTYAPienVQNAPF------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 216 gdvaFLQYTGGTTGVSKgatlthanllsnmaqmelwlntAFLRKPRPESLTFMCALPLYHIFA----LTVNSLM------ 285
Cdd:PRK07638 147 ----YMGFTSGSTGKPK----------------------AFLRAQQSWLHSFDCNVHDFHMKRedsvLIAGTLVhslfly 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 286 ----GLATGGNNILIPNprDIPAFVKE-LGRYRTNIFPGLNTLFNALMNNSEFrkLDFSSLILTFG---GGMAVQRpVAE 357
Cdd:PRK07638 201 gaisTLYVGQTVHLMRK--FIPNQVLDkLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGakwEAEAKEK-IKN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 358 RWLELTgcpIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYwQRPE 437
Cdd:PRK07638 276 IFPYAK---LYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGY-IIGG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVv 517
Cdd:PRK07638 352 VLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII- 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499271215 518 rkDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07638 431 --KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
39-564 |
6.66e-40 |
|
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: 151.71 E-value: 6.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPL 118
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVDAGAKAIFV------LENFAHTVEQVLARTevkhvvvasmgdmlGAKGAIVNLvvrrvkklvpawsipg 192
Cdd:cd17655 81 YPEERIQYILEDSGADILLTqshlqpPIAFIGLIDLLDEDT--------------IYHEESENL---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 193 hlsfktvlakgatlgfkRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLlSNMAqmeLWLNTAFlrkPRPESLTFMCALP 272
Cdd:cd17655 131 -----------------EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGV-VNLV---EWANKVI---YQGEHLRVALFAS 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 273 LYhiFALTVNSL-MGLATGGNNILIPNPR--DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILtfgGGM 349
Cdd:cd17655 187 IS--FDASVTEIfASLLSGNTLYIVRKETvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHLIV---GGE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 350 AVQRPVAERWLEL--TGCPIHEGYGLSETSPVATANRLDTDDFTGT---IGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:cd17655 262 ALSTELAKKIIELfgTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQVMAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEC 498
Cdd:cd17655 342 GEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEA 421
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 499 AAIGVADpHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17655 422 VVIARKD-EQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
26-562 |
1.41e-39 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 151.58 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 26 PAEIGPltyrSIGEFFDHAVAQYSWRPA--FTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNilqNPVIVY 103
Cdd:PRK05852 11 ASDFGP----RIADLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGS---NAEFVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 104 GIL---RAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHtvEQVLARTEVKHVVVaSMGDMLGAKGAIVNLVVRR 180
Cdd:PRK05852 84 ALLaasRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPH--DRAEPTTRWWPLTV-NVGGDSGPSGGTLSVHLDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 181 VKKLVPAWSIPGHLsfktvlakgatlgfkRPnvapgDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwLNTAFLRKP 260
Cdd:PRK05852 161 ATEPTPATSTPEGL---------------RP-----DDAMIMFTGGTTGLPKMVPWTHANIASSVRA----IITGYRLSP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 261 RPESLTFMcalPLYHIFALTVNSLMGLATGGNnILIPNPRDIPA--FVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDF 338
Cdd:PRK05852 217 RDATVAVM---PLYHGHGLIAALLATLASGGA-VLLPARGRFSAhtFWDDIKAVGATWYTAVPTIHQILLERAATEPSGR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 SSLILTF--GGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANRLD----TDDFTGTIGIPLPSTEVEIR--DEDG 410
Cdd:PRK05852 293 KPAALRFirSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEgigqTENPVVSTGLVGRSTGAQIRivGSDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 411 RTLPVGEIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAA 490
Cdd:PRK05852 373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271215 491 THPGILECAAIGVADPHSGEAVKLFVVRKDP-NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRK 562
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYGEAVAAVIVPRESaPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
39-565 |
1.53e-39 |
|
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: 149.77 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTvvnvnpl 118
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPrelehqlVDAGAKAifvlenfahtveqvlartevkhvvvASMGDMLGAKGAivNLVVrrvkklvpawsipghlsfkt 198
Cdd:cd17653 74 YVP-------LDAKLPS-------------------------ARIQAILRTSGA--TLLL-------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 vlakgatlgfkrPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrKPRPESLTFMCalplyhiFA 278
Cdd:cd17653 100 ------------TTDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDV----GPGSRVAQVLS-------IA 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 279 LTVNSLMGLAT---GGNNILipnpRDIPAFVKELGRyRTNIFPGLNTLFNALmnnsefRKLDFSSLILTFGGGMAVQRPV 355
Cdd:cd17653 157 FDACIGEIFSTlcnGGTLVL----ADPSDPFAHVAR-TVDALMSTPSILSTL------SPQDFPNLKTIFLGGEAVPPSL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWLEltGCPIHEGYGLSETSPVATANRLDTDDFTgTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQR 435
Cdd:cd17653 226 LDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGN 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 436 PEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVadpHSG 509
Cdd:cd17653 303 PALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNG 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 510 EAVKlFVVRKDPNltEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd17653 380 RLVA-FVTPETVD--VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALR 432
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
50-560 |
3.27e-39 |
|
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: 151.58 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 50 WRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAG--FTVVNVNplYTPRELEHQ 127
Cdd:cd17634 74 YEGDDTSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGavHSVIFGG--FAPEAVAGR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 128 LVDAGAKAIFVLENFAHTVEQVlartEVKHVVvasmGDMLGAKGAIVN--LVVRRVKKLVpAWSIPGHLSFKTVLAKgAT 205
Cdd:cd17634 152 IIDSSSRLLITADGGVRAGRSV----PLKKNV----DDALNPNVTSVEhvIVLKRTGSDI-DWQEGRDLWWRDLIAK-AS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 206 LGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM----------ELWLNTAflrkprpeSLTFMCALPlYH 275
Cdd:cd17634 222 PEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTmkyvfdygpgDIYWCTA--------DVGWVTGHS-YL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 276 IFAltvnslmGLATGGNNIL---IPNPRDIPAFVKELGRYRTNIFPGLNTLFNALM--NNSEFRKLDFSSLILTFGGGMA 350
Cdd:cd17634 293 LYG-------PLACGATTLLyegVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMaaGDDAIEGTDRSSLRILGSVGEP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 351 VQrPVAERW----LELTGCPIHEGYGLSETSPVATANRLDTDDF-TGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRG 425
Cdd:cd17634 366 IN-PEAYEWywkkIGKEKCPVVDTWWQTETGGFMITPLPGAIELkAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 426 P---QVMAGYWQRPEETARAISP-DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAI 501
Cdd:cd17634 445 PwpgQTRTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVV 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499271215 502 GVADPHSGEAVKLFVVRK----DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:cd17634 525 GIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
212-473 |
8.12e-39 |
|
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: 148.90 E-value: 8.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 NVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaflRKPRPESlTFMCALPLYHIFALTVNSLMgLATGG 291
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVP----ELLGPDD-RYLAYLPLAHIFELAAENVC-LYRGG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 292 NnILIPNPR------------DIPAF-------VKE-LGRYRTNIFPGLN-------TLFNALMNNSEF----------- 333
Cdd:cd17639 158 T-IGYGSPRtltdkskrgckgDLTEFkptlmvgVPAiWDTIRKGVLAKLNpmgglkrTLFWTAYQSKLKalkegpgtpll 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 --------RKLDFSSLILTFGGGMAVQrPVAERWLELTGCPIHEGYGLSETspVATANRLDTDDF-TGTIGIPLPSTEVE 404
Cdd:cd17639 237 delvfkkvRAALGGRLRYMLSGGAPLS-ADTQEFLNIVLCPVIQGYGLTET--CAGGTVQDPGDLeTGRVGPPLPCCEIK 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271215 405 IRD-EDGRTLPVGEI--GEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMI 473
Cdd:cd17639 314 LVDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
61-565 |
3.66e-38 |
|
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: 148.62 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIfVLE 140
Cdd:cd05967 83 YTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLI-VTA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQV------------LARTEVKHVVVASMGDMLGAKGAivnlvvrrvkklvpawsiPGH-LSFKTVLAKGAtlg 207
Cdd:cd05967 162 SCGIEPGKVvpykplldkaleLSGHKPHHVLVLNRPQVPADLTK------------------PGRdLDWSELLAKAE--- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 208 fKRP--NVAPGDVAFLQYTGGTTGVSKGA---TLTHANLLS-------NMAQMELWLNTAFLRKPRPESltFMCALPLYH 275
Cdd:cd05967 221 -PVDcvPVAATDPLYILYTSGTTGKPKGVvrdNGGHAVALNwsmrniyGIKPGDVWWAASDVGWVVGHS--YIVYGPLLH 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 276 ifaltvnslmGLAT---GGNNILIPNPrdiPAFVKELGRYRTNIFPGLNTLFNAL----MNNSEFRKLDFSSLILTFGGG 348
Cdd:cd05967 298 ----------GATTvlyEGKPVGTPDP---GAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 349 MAVQRPVAErWLE-LTGCPIHEGYGLSETSPVATANRLDTDDF---TGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:cd05967 365 ERLDPPTLE-WAEnTLGVPVIDHWWQTETGWPITANPVGLEPLpikAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GP---QVMAGYWQRPE---ETARAISPdGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEC 498
Cdd:cd05967 444 LPlppGCLLTLWKNDErfkKLYLSKFP-GYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271215 499 AAIGVADPHSGE-AVKLFVVRKDPNLTEEEVKRHCAAS----LTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05967 523 AVVGVRDELKGQvPLGLVVLKEGVKITAEELEKELVALvreqIGPVAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
217-561 |
1.01e-37 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 142.40 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSN----MAQMELWLNTAFLRKPrpesltfmcaLPLYHIFALtVNSLMGLATGGN 292
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVpdilQKEGLNWVVGDVTYLP----------LPATHIGGL-WWILTCLIHGGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 293 NILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN-----NSEFRKLDFssliLTFGGGMAVQRPVAE-RWLELTGCP 366
Cdd:cd17635 71 CVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSelksaNATVPSLRL----IGYGGSRAIAADVRFiEATGLTNTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHegYGLSETSpvaTANRLDTDDFT---GTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAI 443
Cdd:cd17635 147 QV--YGLSETG---TALCLPTDDDSieiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 444 SpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVR---KD 520
Cdd:cd17635 222 I-DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLD 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499271215 521 PNLTeEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:cd17635 301 ENAI-RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
30-565 |
4.91e-37 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 144.51 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 30 GPLTYRSIgefFDHAVAQYSWRPAFT--CMGKAL--TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGI 105
Cdd:PRK06018 8 WPLLCHRI---IDHAARIHGNREVVTrsVEGPIVrtTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 106 LRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTE-VKHVVVasMGDmlgakgaivnlvvrrvKKL 184
Cdd:PRK06018 85 MGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLTFVPILEKIADKLPsVERYVV--LTD----------------AAH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 185 VPAWSIPGHLSFKTVLAkGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTH-ANLLSNMAQMElwlntaflrkprPE 263
Cdd:PRK06018 147 MPQTTLKNAVAYEEWIA-EADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHrSNVLHALMANN------------GD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 264 SL------TFMCALPLYHifaltVNSlMGLA----TGGNNILIPNPRDIPAFVKEL-GRYRTNIFPGLNTLFNALMNNSE 332
Cdd:PRK06018 214 ALgtsaadTMLPVVPLFH-----ANS-WGIAfsapSMGTKLVMPGAKLDGASVYELlDTEKVTFTAGVPTVWLMLLQYME 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 FRKLDFSSLILTFGGGMAVQRPVAERWLELtGCPIHEGYGLSETSPVATANRLDTD----------DFTGTIGIPLPSTE 402
Cdd:PRK06018 288 KEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMSPLGTLAALKPPfsklpgdarlDVLQKQGYPPFGVE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 403 VEIRDEDGRTLPVG--EIGEICIRGPQVMAGYWQrpeETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNV 480
Cdd:PRK06018 367 MKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWI 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 481 FPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK-DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKI 559
Cdd:PRK06018 444 SSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKpGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKI 523
|
....*.
gi 499271215 560 LRKDLR 565
Cdd:PRK06018 524 LKTALR 529
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
42-506 |
4.94e-37 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 145.63 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 42 DHAVAQYSWrpaftcmgkaLTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGIlrAGFTVVNVnPLYtp 121
Cdd:PLN02736 70 DGTVGEYKW----------MTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHAC--SAYSYVSV-PLY-- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 122 relehqlvDA-GAKAIFVLENFAhTVEQVLARTEVKHVVVASMGDMLGAKgAIVnlVVRRVKKLVPawSIPGH-----LS 195
Cdd:PLN02736 135 --------DTlGPDAVKFIVNHA-EVAAIFCVPQTLNTLLSCLSEIPSVR-LIV--VVGGADEPLP--SLPSGtgveiVT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 196 FKTVLAKGATlgFKRPNVAPG--DVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlNTAFLRKPRPeSLTFMCALPL 273
Cdd:PLN02736 201 YSKLLAQGRS--SPQPFRPPKpeDVATICYTSGTTGTPKGVVLTHGNLIANVA------GSSLSTKFYP-SDVHISYLPL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 YHIFAlTVNSLM----GLATG---GNN-------------ILIPNPR-------DIPAFVKELGRYRTNIFpglNTLFN- 325
Cdd:PLN02736 272 AHIYE-RVNQIVmlhyGVAVGfyqGDNlklmddlaalrptIFCSVPRlynriydGITNAVKESGGLKERLF---NAAYNa 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 326 ---ALMNNSE----FRKLDFSSLILTFGGGMAV----QRPVAERWLELT----GCPIHEGYGLSETSPVATANRLDtDDF 390
Cdd:PLN02736 348 kkqALENGKNpspmWDRLVFNKIKAKLGGRVRFmssgASPLSPDVMEFLricfGGRVLEGYGMTETSCVISGMDEG-DNL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 391 TGTIGIPLPSTEVEIRD-------EDGRTLPVGEIgeiCIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLT 463
Cdd:PLN02736 427 SGHVGSPNPACEVKLVDvpemnytSEDQPYPRGEI---CVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRL 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 464 KIVDRKKDMI-LVSGFNVFPNEIEEVAATHPGILEC-----------AAIGVADP 506
Cdd:PLN02736 504 KIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCfvygdslnsslVAVVVVDP 558
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
215-519 |
9.30e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 143.01 E-value: 9.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 215 PGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprpESLTFMCALPLYHIFALTVNSLMGLATGGNNI 294
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK-------TKDRILSWMPLTHDMGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 LIPNPRDI--PA-FVKELGRYRTNIFPGLN---TLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLE------L 362
Cdd:cd05908 178 LMPTRLFIrrPIlWLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskygL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHEGYGLSETSPVATANRLDTDDFTGTI---------------------------GIPLPSTEVEIRDEDGRTLPV 415
Cdd:cd05908 258 KRNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsecltfvevGKPIDETDIRICDEDNKILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 416 GEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTkIVDRKKDMILVSGFNVFPNEIEEVAATHPGI 495
Cdd:cd05908 338 GYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
330 340
....*....|....*....|....*..
gi 499271215 496 L--ECAAIGVADPHS-GEAVKLFVVRK 519
Cdd:cd05908 417 ElgRVVACGVNNSNTrNEEIFCFIEHR 443
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
367-561 |
1.31e-36 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 138.69 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVaTANRLDTDDFTGTIGIPLPSTEVEIRDEDGrtlpvGEIGEICIRGPQVMAGYWqrpeeTARAISPD 446
Cdd:cd17633 139 LIEFYGTSELSFI-TYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV-----RGGFSNPD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVkLFVVRKDpNLTEE 526
Cdd:cd17633 208 GWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYK 285
|
170 180 190
....*....|....*....|....*....|....*
gi 499271215 527 EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:cd17633 286 QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
45-524 |
5.43e-36 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 141.57 E-value: 5.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 45 VAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPREL 124
Cdd:PRK09274 26 AVPGGRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 125 EHQLVDAGAKAiFVLENFAHTVEQVLARTE--VKHVVVASmgdmlgakgaivnlvvrrvkklvPAWSIPGHlSFKTVLAK 202
Cdd:PRK09274 106 KQCLAEAQPDA-FIGIPKAHLARRLFGWGKpsVRRLVTVG-----------------------GRLLWGGT-TLATLLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 203 GATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLsnmAQMELWLNTAFLRKPRPESLTFmcalPLYHIFALtvn 282
Cdd:PRK09274 161 GAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFE---AQIEALREDYGIEPGEIDLPTF----PLFALFGP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 283 sLMGLATggnniLIP----------NPRDIpafVKELGRYR-TNIFpGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAV 351
Cdd:PRK09274 231 -ALGMTS-----VIPdmdptrpatvDPAKL---FAAIERYGvTNLF-GSPALLERLGRYGEANGIKLPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 352 QRPVAERWLEL--TGCPIHEGYGLSETSPVAT--------ANRLDTDDFTGT-IGIPLPSTEVEIRD---------EDGR 411
Cdd:PRK09274 301 PIAVIERFRAMlpPDAEILTPYGATEALPISSiesreilfATRAATDNGAGIcVGRPVDGVEVRIIAisdapipewDDAL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 412 TLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDG----FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEE 487
Cdd:PRK09274 381 RLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCER 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 499271215 488 VAATHPGILECAAIGVADPhsGEAVKLFVVRKDPNLT 524
Cdd:PRK09274 461 IFNTHPGVKRSALVGVGVP--GAQRPVLCVELEPGVA 495
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-564 |
2.91e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 142.22 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYtPRE-LEHQLVDAGAKaiFVLENfAHTVEQVLARTEVKHVVVASMGDMLGAKgaivnlvvrrvkklvpawsiPGH 193
Cdd:PRK12467 592 LDPEY-PQDrLAYMLDDSGVR--LLLTQ-SHLLAQLPVPAGLRSLCLDEPADLLCGY--------------------SGH 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 lsfktvlakgatlgFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESLTFMCALPL 273
Cdd:PRK12467 648 --------------NPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA------ADDSMLMVSTFA 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 YHIFaltVNSLMG-LATGGNNILIP--NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNnSEFRKLDFSSLILTFGGgMA 350
Cdd:PRK12467 708 FDLG---VTELFGaLASGATLHLLPpdCARDAEAFAALMADQGVTVLKIVPSHLQALLQ-ASRVALPRPQRALVCGG-EA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 351 VQRPVAERWLELT-GCPIHEGYGLSETSPVATANRL---DTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGP 426
Cdd:PRK12467 783 LQVDLLARVRALGpGARLINHYGPTETTVGVSTYELsdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 427 QVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECA 499
Cdd:PRK12467 863 GLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAV 942
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 500 AIGVADPHSGEAVKLFVVRKDPNLTE-----EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK12467 943 VLAQPGDAGLQLVAYLVPAAVADGAEhqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
62-565 |
5.43e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 138.69 E-value: 5.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLEN 141
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAHTVEQVLAR-TEVKHVVVASMGDMLgakgaivnlvvrrvkklvPAWSIPgHLSFKTVLAkGATLGFKRPNVAPGDVAF 220
Cdd:PRK07008 121 FLPLVDALAPQcPNVKGWVAMTDAAHL------------------PAGSTP-LLCYETLVG-AQDGDYDWPRFDENQASS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTH-ANLLSNMAqmelwlntAFLrkprPESL------TFMCALPLYHIFAltvnslMGL----AT 289
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHrSTVLHAYG--------AAL----PDAMglsardAVLPVVPMFHVNA------WGLpysaPL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNNILIPNPRDIPAFVKEL-GRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIH 368
Cdd:PRK07008 243 TGAKLVLPGPDLDGKSLYELiEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 369 EGYGLSETSPVATANRL------DTDDFTGTI----GIPLPSTEVEIRDEDGRTLPVG--EIGEICIRGPQVMAGYWQRP 436
Cdd:PRK07008 323 HAWGMTEMSPLGTLCKLkwkhsqLPLDEQRKLlekqGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVIDRYFRGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 437 EetaraiSP--DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKL 514
Cdd:PRK07008 403 A------SPlvDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLL 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 515 FVVRK-DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07008 477 VVVKRpGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
61-531 |
2.26e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 137.48 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQlvdagakaifvle 140
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHA------------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQVLARtevkhVVVASMGDMLGAKGAIVNLV-VRRVKKLVPAWSIPGhLSFKTVLAKGATLGFK--RPNVAPGD 217
Cdd:PRK12582 148 KLKHLFDLVKPR-----VVFAQSGAPFARALAALDLLdVTVVHVTGPGEGIAS-IAFADLAATPPTAAVAaaIAAITPDT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAQMELwlntAFLRKPRPESLTFMCALPLYHIFALTVNsLMGLATGGNNILIP 297
Cdd:PRK12582 222 VAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQ----LRPREPDPPPPVSLDWMPWNHTMGGNAN-FNGLLWGGGTLYID 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNIFP--------GLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL----TG- 364
Cdd:PRK12582 297 DGKPLPGMFEETIRNLREISPtvygnvpaGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQALavrtTGh 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 365 -CPIHEGYGLSETSPVATANRLDTDDfTGTIGIPLPSTEVEIrdedgrtLPVGEIGEICIRGPQVMAGYWQRPEETARAI 443
Cdd:PRK12582 377 rIPFYTGYGATETAPTTTGTHWDTER-VGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTAAAF 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 444 SPDGFFRTGDVG-FMN----AEGLtkIVDRK--KDMILVSG--FNVFPNEIEEVAATHPGILE----------CAAIGVA 504
Cdd:PRK12582 449 DEEGFYRLGDAArFVDpddpEKGL--IFDGRvaEDFKLSTGtwVSVGTLRPDAVAACSPVIHDavvagqdrafIGLLAWP 526
|
490 500
....*....|....*....|....*..
gi 499271215 505 DPHSGEAVKlfvvrKDPNLTEEEVKRH 531
Cdd:PRK12582 527 NPAACRQLA-----GDPDAAPEDVVKH 548
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
35-564 |
2.38e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:PRK12316 4551 RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYtPRE-LEHQLVDAGAKaifVLENFAHTVEQvlartevkhvvvasmgdmLGAKGAIVNLVVRRVKKlvpaWSipgh 193
Cdd:PRK12316 4631 LDPEY-PRErLAYMMEDSGAA---LLLTQSHLLQR------------------LPIPDGLASLALDRDED----WE---- 4680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 194 lsfktvlakgatlGFKRPN----VAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLRKPRPESLTFMC 269
Cdd:PRK12316 4681 -------------GFPAHDpavrLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH----ATGERYELTPDDRVLQFMS 4743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 270 alplyHIFALTVNSLMGLATGGNNILIPNPR--DIPAFVKELGRYRTNIFPGLNTLFNALMNNSEfRKLDFSSLILTFGG 347
Cdd:PRK12316 4744 -----FSFDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPSLRVYCFG 4817
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 GMAVQRPVAERWL-ELTGCPIHEGYGLSETSPVATANRLDTDDFTGT----IGIPLPSTEVEIRDEDGRTLPVGEIGEIC 422
Cdd:PRK12316 4818 GEAVAQASYDLAWrALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQLNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 423 IRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGI 495
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAV 4977
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 496 LECAAIGVADPHSGEAVKlFVVRKDPNLTE---------EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK12316 4978 REAVVIAQEGAVGKQLVG-YVVPQDPALADadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
60-516 |
2.49e-34 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 137.06 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 60 ALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYTP-----RE-----LEHQLV 129
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV---PLPLPmgfggREsyiaqLRGMLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 130 DAGAKAIFVLENFAHTVEQVLARTEVKHVvvasmgdmlgakgaivnlvvrrvkkLVPAWsipghlsFKTVLAKGATLgfk 209
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEATHGNPLLHV-------------------------LSHAW-------FKALPEADVAL--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 rPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlntAFLR---KPRPESltfMCA--LPLYHIFALTVNSL 284
Cdd:PRK09192 171 -PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR--------AISHdglKVRPGD---RCVswLPFYHDMGLVGFLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 MGLATGGNNILIPNpRDI---P-AFVKELGRYRTNI-----FpGLNtLFNALMNNSEFRKLDFSSLILTFGGG----MAV 351
Cdd:PRK09192 239 TPVATQLSVDYLPT-RDFarrPlQWLDLISRNRGTIsysppF-GYE-LCARRVNSKDLAELDLSCWRVAGIGAdmirPDV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 352 QRPVAERWLEL-------TGCpihegYGLSET------SPVAT---ANRLDTDDFTGT------------------IGIP 397
Cdd:PRK09192 316 LHQFAEAFAPAgfddkafMPS-----YGLAEAtlavsfSPLGSgivVEEVDRDRLEYQgkavapgaetrrvrtfvnCGKA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 398 LPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWqRPEETARAISPDGFFRTGDVGFMnAEGLTKIVDRKKDMILVSG 477
Cdd:PRK09192 391 LPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF-RDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIING 468
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 499271215 478 FNVFPNEIEEVAATHPGIL--ECAAIGVADpHSGEAVKLFV 516
Cdd:PRK09192 469 RNIWPQDIEWIAEQEPELRsgDAAAFSIAQ-ENGEKIVLLV 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-564 |
4.13e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 138.76 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:PRK12467 1574 RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVP 1653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYTPRELEHQLVDAGakaIFVLENFAHTVEQVLARTEVKHVVVASMGDMLGAKGAiVNLVVrrvkklvpawsipghl 194
Cdd:PRK12467 1654 LDPEYPRERLAYMIEDSG---IELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGYSD-SNPAV---------------- 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 195 sfktvlakgatlgfkrpNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtaflrkprpesLTFMCALPLY 274
Cdd:PRK12467 1714 -----------------NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ-----------LSAADVVLQF 1765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 275 HIFAL--TVNSLMG-LATGGNNILIPN--PRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGm 349
Cdd:PRK12467 1766 TSFAFdvSVWELFWpLINGARLVIAPPgaHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGE- 1844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 350 AVQRPVAERWLE-LTGCPIHEGYGLSETSPVATANRLDTDDFTGT----IGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:PRK12467 1845 ALEVEALRPWLErLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILDASLNPVPIGVAGELYLG 1924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILE 497
Cdd:PRK12467 1925 GVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVRE 2004
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 498 CAAIgVADPHSGEAVKLFVVRKDPNLTEEEV---------KRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK12467 2005 AVVI-AQDGANGKQLVAYVVPTDPGLVDDDEaqvalrailKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
61-564 |
4.61e-34 |
|
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: 134.91 E-value: 4.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKaifvle 140
Cdd:cd17656 14 LTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVR------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfaHTVEQVlartevkhvvvaSMGDMLGAKGAIVnlvvrrvkklVPAWSIPGHlsfktVLAKGATLgfkrpNVAPGDVAF 220
Cdd:cd17656 88 ---VVLTQR------------HLKSKLSFNKSTI----------LLEDPSISQ-----EDTSNIDY-----INNSDDLLY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANLLsNMAQMElWLNTAFLRKPRPESLTFMCALPLYH-IFAltvnslmGLATGGNNILIPNP 299
Cdd:cd17656 133 IIYTSGTTGKPKGVQLEHKNMV-NLLHFE-REKTNINFSDKVLQFATCSFDVCYQeIFS-------TLLSGGTLYIIREE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 300 --RDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSL--ILTFGGGMAVQRPVAErWLELTGCPIHEGYGLSE 375
Cdd:cd17656 204 tkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVkhIITAGEQLVITNEFKE-MLHEHNVHLHNHYGPSE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 376 TSpVATANRLDTDD---FTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF---- 448
Cdd:cd17656 283 TH-VVTTYTINPEAeipELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpne 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 449 --FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVrKDPNLTEE 526
Cdd:cd17656 362 rmYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV-MEQELNIS 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 499271215 527 EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17656 441 QLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
51-564 |
1.01e-33 |
|
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: 133.15 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd17652 3 APAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAkaifvlenfahtveqvlartevkHVVVASmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd17652 83 ARP-----------------------ALLLTT------------------------------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvaPGDVAFLQYTGGTTGVSKGATLTHANLlSNMAQMElwlnTAFLRkPRPESLTFMCALPLYHIFALTVnsLMGLATG 290
Cdd:cd17652 92 ----PDNLAYVIYTSGSTGRPKGVVVTHRGL-ANLAAAQ----IAAFD-VGPGSRVLQFASPSFDASVWEL--LMALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNNILIPNPRDIP--AFVKELGRYRTN---IFPGlntlfnALMNNSEFRKLDFSSLILtfgGGMAVQRPVAERWLelTGC 365
Cdd:cd17652 160 ATLVLAPAEELLPgePLADLLREHRIThvtLPPA------ALAALPPDDLPDLRTLVV---AGEACPAELVDRWA--PGR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 366 PIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISP 445
Cdd:cd17652 229 RMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 446 DGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEcAAIGVADPHSGEA--VKLFV 516
Cdd:cd17652 309 DPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKrlVAYVV 387
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 499271215 517 VRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17652 388 PAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
26-564 |
1.14e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.60 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 26 PAEIGPLTYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGI 105
Cdd:PRK12467 3086 ATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAV 3165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 106 LRAGFTVVNVNPLYtPRE-LEHQLVDAGAKaifVLENFAHTVEQvLARTEVKHVVVASMGDMLGAKGAivNLVVRrvkkl 184
Cdd:PRK12467 3166 LKAGGAYVPLDPEY-PRErLAYMIEDSGVK---LLLTQAHLLEQ-LPAPAGDTALTLDRLDLNGYSEN--NPSTR----- 3233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 185 vpawsipghlsfktvlakgatlgfkrpnVAPGDVAFLQYTGGTTGVSKGATLTH---ANLLSNMAQM-ELWLNTAFLRKp 260
Cdd:PRK12467 3234 ----------------------------VMGENLAYVIYTSGSTGKPKGVGVRHgalANHLCWIAEAyELDANDRVLLF- 3284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 261 rpesLTFMcalplyhiFALTV-NSLMGLATGGNNILIPNP-RDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRklDF 338
Cdd:PRK12467 3285 ----MSFS--------FDGAQeRFLWTLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGA--DC 3350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 SSL-ILTFGGGM-------AVQRPVAERWLeltgcpiHEGYGLSETSPVATANRLDTDDFTGT----IGIPLPSTEVEIR 406
Cdd:PRK12467 3351 ASLdIYVFGGEAvppaafeQVKRKLKPRGL-------TNGYGPTEAVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVL 3423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 407 DEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFN 479
Cdd:PRK12467 3424 DGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFR 3503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 480 VFPNEIEEVAATHPGILECAAIGVaDPHSGEAVKLFVVRKDPNLT-EEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGK 558
Cdd:PRK12467 3504 IELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGK 3582
|
....*.
gi 499271215 559 ILRKDL 564
Cdd:PRK12467 3583 VDRKAL 3588
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
61-565 |
6.83e-33 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 132.98 E-value: 6.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQ-SLGLAKGDRVAVMMPNILQNpvivygiLRAGFTVVNVNPLYTPreLEHQLVD--------- 130
Cdd:PRK05620 39 TTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEH-------LEVLFAVACMGAVFNP--LNKQLMNdqivhiinh 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAKAIFVLENFAHTVEQVLARTE-VKHVVVASMGDMLgakgaivnlvvrrvkklVPAWSIPGHL---SFKTVLAKGATL 206
Cdd:PRK05620 110 AEDEVIVADPRLAEQLGEILKECPcVRAVVFIGPSDAD-----------------SAAAHMPEGIkvySYEALLDGRSTV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 207 gFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLlsnmaqmelWLNTAFLRKPRPESLT----FMCALPLYHIFALTVn 282
Cdd:PRK05620 173 -YDWPELDETTAAAICYSTGTTGAPKGVVYSHRSL---------YLQSLSLRTTDSLAVThgesFLCCVPIYHVLSWGV- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 283 SLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL 362
Cdd:PRK05620 242 PLAAFMSGTPLVFPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TGCPIHEGYGLSETSPVATANRLDTddftGTIGiplpSTEVEIRDEDGRtLPV---------GEI--------GEICIRG 425
Cdd:PRK05620 322 YGVDVVHVWGMTETSPVGTVARPPS----GVSG----EARWAYRVSQGR-FPAsleyrivndGQVmestdrneGEIQVRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 426 PQVMAGYWQRP----------------EETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVA 489
Cdd:PRK05620 393 NWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 490 ATHPGILECAAIGVADPHSGE---AVKLFVVRKDPNL-TEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK05620 473 MAAPEVVECAVIGYPDDKWGErplAVTVLAPGIEPTReTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
58-559 |
9.04e-33 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 134.32 E-value: 9.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSlGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNplYTprelehqlvdAGAKAIF 137
Cdd:PRK06814 656 NGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FS----------AGIANIL 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENFAhtveqvlartEVKHVVV-------ASMGDMLGAKGAIVNLV-VRRVKKLVPAWsipghLSFKTVLAKGATLgFK 209
Cdd:PRK06814 723 SACKAA----------QVKTVLTsrafiekARLGPLIEALEFGIRIIyLEDVRAQIGLA-----DKIKGLLAGRFPL-VY 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwlntAFLRKP-RPESLTFmCALPLYHIFALTVNSLMGLA 288
Cdd:PRK06814 787 FCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQ-------VAARIDfSPEDKVF-NALPVFHSFGLTGGLVLPLL 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPNP---RDIPAFVkelgrYRTN--IFPGLNTLFNALMNNSEfrKLDFSSLILTFGGGMAVQRPVAERWLELT 363
Cdd:PRK06814 859 SGVKVFLYPSPlhyRIIPELI-----YDTNatILFGTDTFLNGYARYAH--PYDFRSLRYVFAGAEKVKEETRQTWMEKF 931
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 GCPIHEGYGLSETSPVATANrldTDDFT--GTIGIPLPSTEVEIRDEDGrtlpVGEIGEICIRGPQVMAGYWQrpEETAR 441
Cdd:PRK06814 932 GIRILEGYGVTETAPVIALN---TPMHNkaGTVGRLLPGIEYRLEPVPG----IDEGGRLFVRGPNVMLGYLR--AENPG 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 442 AISP--DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAAT-HPGILEcAAIGVADPHSGEAVKLFVVR 518
Cdd:PRK06814 1003 VLEPpaDGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALH-AAVSIPDARKGERIILLTTA 1081
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499271215 519 KDpnLTEEEVKRHC-AASLTNYKRPRYVEFRTELPKSNVGKI 559
Cdd:PRK06814 1082 SD--ATRAAFLAHAkAAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
46-566 |
1.38e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 132.85 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 46 AQYSW--RPAFTCmGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPlytprE 123
Cdd:PRK06060 15 SEAGWydRPAFYA-ADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP-----E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 124 LehqlvdagakaifvlenfaHTVEQVLARTEVKHVVVASMGDMLG--AKGAIVNlvvrrvkklvPAwsipghlsfkTVLA 201
Cdd:PRK06060 89 L-------------------HRDDHALAARNTEPALVVTSDALRDrfQPSRVAE----------AA----------ELMS 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 202 KGATLGFKRPNVAPGDV-AFLQYTGGTTGVSKGATLTHANLLSNMAQMelwLNTAFLRKPRPESLtfmCALPLYHIFALT 280
Cdd:PRK06060 130 EAARVAPGGYEPMGGDAlAYATYTSGTTGPPKAAIHRHADPLTFVDAM---CRKALRLTPEDTGL---CSARMYFAYGLG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 281 VNSLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKldFSSLILTFGGGMAVQRPVAERWL 360
Cdd:PRK06060 204 NSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDS--FRSLRCVVSAGEALELGLAERLM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 EL-TGCPIHEGYGLSETSPVATANRLDtDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:PRK06060 282 EFfGGIPILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 araISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK 519
Cdd:PRK06060 361 ---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVAT 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 499271215 520 DPNLTEEEVKRHC----AASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK06060 438 SGATIDGSVMRDLhrglLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
61-564 |
1.54e-32 |
|
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: 129.89 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKaIFVLE 140
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAK-LLLTQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvaPGDVAF 220
Cdd:cd17650 92 --------------------------------------------------------------------------PEDLAY 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANllsnmaqmelWLNTAFLRKPRPESLTFMCALPLYHIFALTVNS---LMGLATGGNniLIP 297
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRN----------VAHAAHAWRREYELDSFPVRLLQMASFSFDVFAgdfARSLLNGGT--LVI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDI----PAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSL-ILTFGGGMAVQRPVAERWLEL-TGCPIHEGY 371
Cdd:cd17650 166 CPDEVkldpAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMrLLIVGSDGCKAQDFKTLAARFgQGMRIINSY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 372 GLSETSPVAT-----ANRLDTDDFTgTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPD 446
Cdd:cd17650 246 GVTEATIDSTyyeegRDPLGDSANV-PIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVEN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEcAAIGVADPHSGEA--VKLFVVR 518
Cdd:cd17650 325 PFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEArlCAYVVAA 403
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 499271215 519 KDPNLTeeEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17650 404 ATLNTA--ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
58-565 |
1.78e-32 |
|
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: 129.78 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIF 137
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VlenfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapgD 217
Cdd:cd05940 81 V------------------------------------------------------------------------------D 82
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLRKPrpESLTFMCaLPLYHIFALTVNSLMGLAtGGNNILIP 297
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGA----FFAGSGGALP--SDVLYTC-LPLYHSTALIVGWSACLA-SGATLVIR 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMavqRP-VAERWLELTGCP-IHEGYGLSE 375
Cdd:cd05940 155 KKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGL---RPdIWEEFKERFGVPrIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 376 TSpVATANRldtDDFTGTIG-IPL--------------PSTEVEIRDEDGRTLPV--GEIGE-IC-IRGPQVMAGYWQrP 436
Cdd:cd05940 232 GN-SGFINF---FGKPGAIGrNPSllrkvaplalvkydLESGEPIRDAEGRCIKVprGEPGLlISrINPLEPFDGYTD-P 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 437 EETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADP-HSG 509
Cdd:cd05940 307 AATEKKILRDVFkkgdawFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPgTDG 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 510 EA-VKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05940 387 RAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
62-530 |
2.84e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 130.50 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVnPLYTPRelehqlVDagakaifvLEN 141
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML-HQPTPR------TD--------LAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAHTVEQVLARTEVKHVVVAS----MGDMLGAKGAIVnlvvRRVKKLVPAWSIpghlsfktvlakgatlgfKRPNVAPGD 217
Cdd:PRK07768 96 WAEDTLRVIGMIGAKAVVVGEpflaAAPVLEEKGIRV----LTVADLLAADPI------------------DPVETGEDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSNMAQMelwlntaFLR-KPRPESLTFMCALPLYH----IFALTVNslmgLATGGN 292
Cdd:PRK07768 154 LALMQLTSGSTGSPKAVQITHGNLYANAEAM-------FVAaEFDVETDVMVSWLPLFHdmgmVGFLTVP----MYFGAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 293 NILIpNP----RDIPAFVKELGRYRTNIFPGLNTLFNA----LMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLElTG 364
Cdd:PRK07768 223 LVKV-TPmdflRDPLLWAELISKYRGTMTAAPNFAYALlarrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLD-AG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 365 CP-------IHEGYGLSET------SPVATANRLDTDDFT-------------------GTIGIPLPSTEVEIRDEDGRT 412
Cdd:PRK07768 301 ARfglrpeaILPAYGMAEAtlavsfSPCGAGLVVDEVDADllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 413 LPVGEIGEICIRGPQVMAGYwQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATH 492
Cdd:PRK07768 381 LPPRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARV 459
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 499271215 493 PGILE-CA-AIGVADPHSGEAvklFVVRKDPNL--TEEEVKR 530
Cdd:PRK07768 460 EGVRPgNAvAVRLDAGHSREG---FAVAVESNAfeDPAEVRR 498
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
39-564 |
7.96e-32 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 128.06 E-value: 7.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPL 118
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVDAGAKAIfvLENfahtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfkt 198
Cdd:cd17645 82 YPGERIAYMLADSSAKIL--LTN--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 vlakgatlgfkrpnvaPGDVAFLQYTGGTTGVSKGATLTHANLLsNMAQmelWLNTAFLRKPRPESLTFMCalplyHIFA 278
Cdd:cd17645 103 ----------------PDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCE---WHRPYFGVTPADKSLVYAS-----FSFD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 279 LTVNSLMGLATGGNNILIPnPRDIPAFVKELGRY-RTNifpGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRpvae 357
Cdd:cd17645 158 ASAWEIFPHLTAGAALHVV-PSERRLDLDALNDYfNQE---GITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKK---- 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 358 rwLELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPE 437
Cdd:cd17645 230 --IERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEA 511
Cdd:cd17645 308 LTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKY 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 499271215 512 VKLFVVRKDpNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17645 388 LVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
214-566 |
1.11e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 129.15 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 214 APGDVAFLQYTGGTTGVSKGATLTHANL----LSNMA-----QMELWLNTAflrkprpesltfmcalPLYHIFALTvNSL 284
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAivgygEDDVYLHTA----------------PLCHIGGLS-SAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 MGLATGGNNILIPN---------PRD--------IPAFVKELGRY-RTNI----FPGLNTLFNA-------LMNnsEFRK 335
Cdd:PLN02860 233 AMLMVGACHVLLPKfdakaalqaIKQhnvtsmitVPAMMADLISLtRKSMtwkvFPSVRKILNGggslssrLLP--DAKK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 336 LdFSSLILTFGGGMAvqrpvaERWLELTGCPIHEGYGLSETSPVATANRLDTDDFT---GT-IGIPLPSTEVEIR-DEDG 410
Cdd:PLN02860 311 L-FPNAKLFSAYGMT------EACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHqpqGVcVGKPAPHVELKIGlDESS 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 411 RTlpvgeiGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAA 490
Cdd:PLN02860 384 RV------GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 491 THPGILECAAIGVADPHSGEAVKLFV---------------VRKDPNLTEEEVKRHCAA-SLTNYKRPR-YVEFRTELPK 553
Cdd:PLN02860 458 QHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREkNLSRFKIPKlFVQWRKPFPL 537
|
410
....*....|...
gi 499271215 554 SNVGKILRKDLRG 566
Cdd:PLN02860 538 TTTGKIRRDEVRR 550
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
62-502 |
1.44e-31 |
|
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: 128.69 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNIlqnPVIVYGILRA----GFTVvnvnPLYT---PRELEHQLVDAGAK 134
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNR---PEWVWAELAAqaigALSL----GIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 135 AIFVLENfahtvEQV------LARTE-VKHVVVASMGDMlgakgaivnlvvRRVKKlvpawsiPGHLSFKTVLAKGATLG 207
Cdd:cd17641 86 VVIAEDE-----EQVdklleiADRIPsVRYVIYCDPRGM------------RKYDD-------PRLISFEDVVALGRALD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 208 FKRPNV--------APGDVAFLQYTGGTTGVSKGATLTHANLLSnmaqMELWLNTAFLRKPRPESLTFmcaLPLYHIFAL 279
Cdd:cd17641 142 RRDPGLyerevaagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLG----HCAAYLAADPLGPGDEYVSV---LPLPWIGEQ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 280 TVNSLMGLATG-------------------GNNILIPNPR-------DIPAFVKELGRYRTNIFP-GLNTLFNALmnNSE 332
Cdd:cd17641 215 MYSVGQALVCGfivnfpeepetmmedlreiGPTFVLLPPRvwegiaaDVRARMMDATPFKRFMFElGMKLGLRAL--DRG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 FR-------------------------KLDFSSLILTFGGGMAVQrPVAERWLELTGCPIHEGYGLSETSPVATANRLDT 387
Cdd:cd17641 293 KRgrpvslwlrlaswladallfrplrdRLGFSRLRSAATGGAALG-PDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 388 DDFTgTIGIPLPSTEVEIrdedgrtlpvGEIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVD 467
Cdd:cd17641 372 VDPD-TVGVPFPGTEVRI----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVID 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 499271215 468 RKKDMILVSGFNVF-PNEIEEVAATHPGILECAAIG 502
Cdd:cd17641 441 RAKDVGTTSDGTRFsPQFIENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
51-565 |
1.51e-31 |
|
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: 127.10 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVD 130
Cdd:cd17649 3 AVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 131 AGAkaifvlenfahtveqvlartevkHVVVASMGDMLgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkr 210
Cdd:cd17649 83 SGA-----------------------GLLLTHHPRQL------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 pnvapgdvAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaflrkpRPESltfmCALPLYHI-FALTVNSLM-GLA 288
Cdd:cd17649 97 --------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGL------TPGD----RELQFASFnFDGAHEQLLpPLI 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPNPRDIPA-----FVKELGRYRTNIFPGLNTLFNALMNNSEFRklDFSSLILTFGGGMAVQRPVAERWLElT 363
Cdd:cd17649 159 CGACVVLRPDELWASAdelaeMVRELGVTVLDLPPAYLQQLAEEADRTGDG--RPPSLRLYIFGGEALSPELLRRWLK-A 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 GCPIHEGYGLSETSPVATANRLDTDDFTG----TIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEET 439
Cdd:cd17649 236 PVRLFNAYGPTEATVTPLVWKCEAGAARAgasmPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELT 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 440 ARAISPDGFF-------RTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAV 512
Cdd:cd17649 316 AERFVPDPFGapgsrlyRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 513 KLFVVRKDPNLTE--EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd17649 396 AYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
72-565 |
4.05e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 127.83 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 72 KIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVLA 151
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 152 rtevkhvvvasmgdMLGAKGAIVNLVVRRVKKL-VPAWSIPGHLSFKTVLAKG-------ATLgFKRPNvaPGDVAFLQY 223
Cdd:PLN03102 131 --------------LLSSEDSNLNLPVIFIHEIdFPKRPSSEELDYECLIQRGeptpslvARM-FRIQD--EHDPISLNY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 224 TGGTTGVSKGATLTH-ANLLSNMAQMELWLNTAFlrkprPeslTFMCALPLYHIFALTVNSLMGlATGGNNILIpnpRDI 302
Cdd:PLN03102 194 TSGTTADPKGVVISHrGAYLSTLSAIIGWEMGTC-----P---VYLWTLPMFHCNGWTFTWGTA-ARGGTSVCM---RHV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 303 --PAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERwLELTGCPIHEGYGLSE-TSPV 379
Cdd:PLN03102 262 taPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKK-VQRLGFQVMHAYGLTEaTGPV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 380 ATA------NRLDTD---DFTGTIGIP-LPSTEVEIRDE--------DGRTLpvgeiGEICIRGPQVMAGYWQRPEETAR 441
Cdd:PLN03102 341 LFCewqdewNRLPENqqmELKARQGVSiLGLADVDVKNKetqesvprDGKTM-----GEIVIKGSSIMKGYLKNPKATSE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 442 AISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV---- 517
Cdd:PLN03102 416 AFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekg 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 518 ------RKDPNLTEE-EVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PLN03102 495 ettkedRVDKLVTRErDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
44-566 |
1.17e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 125.49 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 44 AVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPre 123
Cdd:PRK13383 44 TAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRS-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 124 lehqlvDAGAKAIFvlenfAHTVEQVLARTEVKHVVVASmgdmlGAKGAIVNlvvrrvkklvPAwsipghlsfktvlAKG 203
Cdd:PRK13383 122 ------DALAAALR-----AHHISTVVADNEFAERIAGA-----DDAVAVID----------PA-------------TAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 204 ATLGFKRPNVAP-GDVAFLqyTGGTTGVSKGATlTHANLLSNMAQMELWLNTAFLRKPRPESLtfmcALPLYHifALTVN 282
Cdd:PRK13383 163 AEESGGRPAVAApGRIVLL--TSGTTGKPKGVP-RAPQLRSAVGVWVTILDRTRLRTGSRISV----AMPMFH--GLGLG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 283 SLMGLATGGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMN-NSEFRKLD-FSSLILTFGGGMAVQRPVAERWL 360
Cdd:PRK13383 234 MLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 ELTGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRtlPVGE--IGEICIRGPQVMAGYwqrPEE 438
Cdd:PRK13383 314 DTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNR--PVGPrvTGRIFVGGELAGTRY---TDG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 439 TARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV- 517
Cdd:PRK13383 389 GGKAVV-DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVl 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499271215 518 RKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLRG 566
Cdd:PRK13383 468 HPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-564 |
1.36e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 128.15 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 33 TYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTV 112
Cdd:PRK12316 509 LQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 113 VNVNPLYTPRELEHQLVDAGAkaifvlenfahtveQVLartevkhVVVASMGDMLGAKGAIVNLVVRRvkklvPAWSIPG 192
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGV--------------QLL-------LSQSHLGRKLPLAAGVQVLDLDR-----PAAWLEG 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 193 HLSFKTVLAkgatlgfkrpnVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFlrkPRPESLTFMCALP 272
Cdd:PRK12316 643 YSEENPGTE-----------LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC----WMQQAY---GLGVGDTVLQKTP 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 273 LYhiFALTVNSLMG-LATGGNNILIP--NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDfSSLILTFGG-- 347
Cdd:PRK12316 705 FS--FDVSVWEFFWpLMSGARLVVAApgDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT-SLRRIVCSGea 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 --GMAVQRPVAERWLeltgCPIHEGYGLSETSPVAT-ANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:PRK12316 782 lpADAQEQVFAKLPQ----AGLYNLYGPTEAAIDVThWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLA 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQVMAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILEC 498
Cdd:PRK12316 858 GRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 937
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 499 AAIGVadphSGEAVKLFVVRKDP-NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK12316 938 AVLAV----DGKQLVGYVVLESEgGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-564 |
1.68e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.77 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 22 PPGVPAEIGpltyrsIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVI 101
Cdd:PRK12316 1996 PEAYPRGPG------VHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVA 2069
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 102 VYGILRAGFTVVNVNPLYtPRE-LEHQLVDAGAKAIFvlenfahTVEQVLARtevkhvvvasmgdmLGAKGAIVNLVVRR 180
Cdd:PRK12316 2070 LLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLL-------TQRHLLER--------------LPLPAGVARLPLDR 2127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 181 VKKLvPAWSIpghlsfktvlakgatlgfKRPNV--APGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelWLNTAFLR 258
Cdd:PRK12316 2128 DAEW-ADYPD------------------TAPAVqlAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ----AAGERYEL 2184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 259 KPRPESLTFMCalplyHIFALTVNSLMGLATGGNNILIPN-----PRDIPAFVKELGrYRTNIFPGlnTLFNALMNNSEF 333
Cdd:PRK12316 2185 SPADCELQFMS-----FSFDGAHEQWFHPLLNGARVLIRDdelwdPEQLYDEMERHG-VTILDFPP--VYLQQLAEHAER 2256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 RKLDFSSLILTFGGGmAVQRPVAERWLE-LTGCPIHEGYGLSETSPVATANRLDTDDFTGT----IGIPLPSTEVEIRDE 408
Cdd:PRK12316 2257 DGRPPAVRVYCFGGE-AVPAASLRLAWEaLRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNRRAYILDA 2335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 409 DGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVF 481
Cdd:PRK12316 2336 DLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIE 2415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 482 PNEIEEVAATHPGILECAAIGVADPhSGEAVKLFVVRKDP-NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:PRK12316 2416 LGEIEARLQAHPAVREAVVVAQDGA-SGKQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLD 2494
|
....
gi 499271215 561 RKDL 564
Cdd:PRK12316 2495 RKAL 2498
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
62-453 |
3.02e-30 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 124.85 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHqlvdagAKaifvlen 141
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDL------AK------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAHTVEQVLARtevkhVVVASMGDMLG-AKGAIVNLVVRRVKKLVPAWSIpGHLSFKTVLAKGATLGFKR--PNVAPGDV 218
Cdd:cd05921 94 LKHLFELLKPG-----LVFAQDAAPFArALAAIFPLGTPLVVSRNAVAGR-GAISFAELAATPPTAAVDAafAAVGPDTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlntAFLRKPRPESLTFMCALPLYHIFALTVNSLMGLATGGNnILIPN 298
Cdd:cd05921 168 AKFLFTSGSTGLPKAVINTQRMLCANQAMLE-----QTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGT-LYIDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 299 PRDIPAFVKELGRYRTNIFP--------GLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL----TGCP 366
Cdd:cd05921 242 GKPMPGGFEETLRNLREISPtvyfnvpaGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALavatVGER 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 I--HEGYGLSETSPVATANRLDTDDfTGTIGIPLPSTEVeirdedgRTLPVGEIGEICIRGPQVMAGYWQRPEETARAIS 444
Cdd:cd05921 322 IpmMAGLGATETAPTATFTHWPTER-SGLIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFD 393
|
....*....
gi 499271215 445 PDGFFRTGD 453
Cdd:cd05921 394 EEGFYCLGD 402
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
35-453 |
6.46e-30 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 124.22 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKA-----LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAG 109
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLAERGADggwrrLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 110 FTVVNVNPLYT-----PRELEH--QLVDAGAkaIFVLEnfAHTVEQVLARTEVKHVVVASMGDMLGAkgaivnlvvrrvk 182
Cdd:PRK08180 119 VPYAPVSPAYSlvsqdFGKLRHvlELLTPGL--VFADD--GAAFARALAAVVPADVEVVAVRGAVPG------------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 183 klvpawsiPGHLSFKTVLAKGATLGFKR--PNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM-ELWlntAFLRK 259
Cdd:PRK08180 182 --------RAATPFAALLATPPTAAVDAahAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLaQTF---PFLAE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 260 PRPeslTFMCALPLYHIFALTVNSLMGLATGGNnILIPNPRDIPAFVKELGR--------YRTNIFPGLNTLFNALMNNS 331
Cdd:PRK08180 251 EPP---VLVDWLPWNHTFGGNHNLGIVLYNGGT-LYIDDGKPTPGGFDETLRnlreisptVYFNVPKGWEMLVPALERDA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 332 EFRKLDFSSLILTFGGGMAVQRPVAERWLELTG--C----PIHEGYGLSETSPVATaNRLDTDDFTGTIGIPLPSTEVEI 405
Cdd:PRK08180 327 ALRRRFFSRLKLLFYAGAALSQDVWDRLDRVAEatCgeriRMMTGLGMTETAPSAT-FTTGPLSRAGNIGLPAPGCEVKL 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499271215 406 RDEDGRTlpvgeigEICIRGPQVMAGYWQRPEETARAISPDGFFRTGD 453
Cdd:PRK08180 406 VPVGGKL-------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
224-565 |
8.41e-30 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 122.03 E-value: 8.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 224 TGGTTGVSKGATLTHANLlSNMAQmelwlntAFLRKPRPESLTFMCALPLYHifaltVNSLM----GLATGGNNILIP-- 297
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETL-TASVQ-------GFQRYFQLQQVNSFCVLPLYH-----VSGLMqfmrSFLTGGKLVILPyk 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 ---NPRDIPAFVKElgrYRTNIFPG-LNTLFNALMNN-SEFRkldfssLILTfGGGMAvqrpvaerWLEL------TGCP 366
Cdd:PRK07445 195 rlkSGQELPPNPSD---FFLSLVPTqLQRLLQLRPQWlAQFR------TILL-GGAPA--------WPSLleqarqLQLR 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSET-SPVATanrLDTDDF-TGTI--GIPLPSTEVEIRDedgrtlpvGEIGEICIRGPQVMAGYWQRpeetarA 442
Cdd:PRK07445 257 LAPTYGMTETaSQIAT---LKPDDFlAGNNssGQVLPHAQITIPA--------NQTGNITIQAQSLALGYYPQ------I 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 443 ISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIE-EVAATHPgILECAAIGVADPHSGEAVKLFVVRKDP 521
Cdd:PRK07445 320 LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEaAILATGL-VQDVCVLGLPDPHWGEVVTAIYVPKDP 398
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 499271215 522 NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07445 399 SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-558 |
2.76e-29 |
|
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: 119.02 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 216 GDVAFLQYTGGTTGVSKGATLTHANLLS------NMAQME-LWLNTAFLRKPRPESLTFMCALPLYHifALTVNSLMGLA 288
Cdd:cd05924 3 ADDLYILYTGGTTGMPKGVMWRQEDIFRmlmggaDFGTGEfTPSEDAHKAAAAAAGTVMFPAPPLMH--GTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGNNILIPNPR-DIPAFVKELGRYRTNIFP--G---LNTLFNALmnnSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL 362
Cdd:cd05924 81 LGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTivGdamARPLIDAL---RDAGPYDLSSLFAISSGGALLSPEVKQGLLEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 TgcP---IHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVeiRDEDGRTLPVGE--IGEICIRGpQVMAGYWQRPE 437
Cdd:cd05924 158 V--PnitLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSggVGWIARRG-HIPLGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDGFFR---TGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVkL 514
Cdd:cd05924 233 KTAETFPEVDGVRyavPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV-V 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499271215 515 FVVRKDPN--LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGK 558
Cdd:cd05924 312 AVVQLREGagVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
211-564 |
3.35e-29 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 121.65 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDVAFLQYTGGTTGVSKGATLThanllsnmaqmelwlNTAFLRKP---RPESL---------TFMCALPLYHIFA 278
Cdd:PRK05857 164 ADQGSEDPLAMIFTSGTTGEPKAVLLA---------------NRTFFAVPdilQKEGLnwvtwvvgeTTYSPLPATHIGG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 279 L--TVNSLM--GLA-TGGNNILipnprdipAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSL-ILTFGGGMAVQ 352
Cdd:PRK05857 229 LwwILTCLMhgGLCvTGGENTT--------SLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLrLVGYGGSRAIA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 353 RPVaeRWLELTGCPIHEGYGLSETSpvATANRLDTDDFT------GTIGIPLPSTEVEIRDEDG------RTLPVGEIGE 420
Cdd:PRK05857 301 ADV--RFIEATGVRTAQVYGLSETG--CTALCLPTDDGSivkieaGAVGRPYPGVDVYLAATDGigptapGAGPSASFGT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 421 ICIRGPQVMAGYWQRPEETaRAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:PRK05857 377 LWIKSPANMLGYWNNPERT-AEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAAC 455
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 501 IGVADPHSGEAVKLFVVRKDP--NLTEEEVKRHCAASL----TNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK05857 456 YEIPDEEFGALVGLAVVASAEldESAARALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-564 |
4.27e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.45 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 33 TYRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTV 112
Cdd:PRK12316 3055 LERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAY 3134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 113 VNVNPLYTPRELEHQLVDAGAKAIFVLEnfahtveqvlartevkHVVVASmgdmlgAKGAIVNLVVRRvkklvpawsipg 192
Cdd:PRK12316 3135 VPLDPEYPEERLAYMLEDSGAQLLLSQS----------------HLRLPL------AQGVQVLDLDRG------------ 3180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 193 hlsfktvlAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQM-ELWLNTAFLRKPRPESLTF-MCA 270
Cdd:PRK12316 3181 --------DENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMqQAYGLGVGDRVLQFTTFSFdVFV 3252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 271 LPLYhiFALTVNSLMGLATGGnniLIPNPRDIPAFVKELGRYRTNIFPGLNTLFNAlmnnsEFRKLDFSSLILTFGGGMA 350
Cdd:PRK12316 3253 EELF--WPLMSGARVVLAGPE---DWRDPALLVELINSEGVDVLHAYPSMLQAFLE-----EEDAHRCTSLKRIVCGGEA 3322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 351 VQRPVAERWLelTGCPIHEGYGLSETSPVATANRL-DTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVM 429
Cdd:PRK12316 3323 LPADLQQQVF--AGLPLYNLYGPTEATITVTHWQCvEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLA 3400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGV 503
Cdd:PRK12316 3401 RGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV 3480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499271215 504 AdphsGEAVKLFVVRKDPNLT-EEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK12316 3481 D----GRQLVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
61-565 |
6.45e-28 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 116.87 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYtPRE-LEHQLVDAGAKaifvl 139
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH-PLQrLQEILQDTGAK----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 enfahtveqvlartevkhVVVASmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvAPGDVA 219
Cdd:cd05918 99 ------------------VVLTS---------------------------------------------------SPSDAA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 220 FLQYTGGTTGVSKGATLTHANLLSNM-AQMEL--------WLNTAflrkprpeSLTF-MCalpLYHIFaltvnslMGLAT 289
Cdd:cd05918 110 YVIFTSGSTGKPKGVVIEHRALSTSAlAHGRAlgltsesrVLQFA--------SYTFdVS---ILEIF-------TTLAA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNnILIPNPR----DIPAFVKELGryrtnifpgLNTLF-----NALMNNSEFRKLdfSSLILtfgGGMAVQRPVAERWL 360
Cdd:cd05918 172 GGC-LCIPSEEdrlnDLAGFINRLR---------VTWAFltpsvARLLDPEDVPSL--RTLVL---GGEALTQSDVDTWA 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 361 EltGCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTE--VEIRDEDgRTLPVGEIGEICIRGPQVMAGYWQRPEE 438
Cdd:cd05918 237 D--RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCwvVDPDNHD-RLVPIGAVGELLIEGPILARGYLNDPEK 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 439 TARA-----------ISPDG--FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEE-VAATHPGILECAAIgVA 504
Cdd:cd05918 314 TAAAfiedpawlkqeGSGRGrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHhLRQSLPGAKEVVVE-VV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 505 DPHSGEAVKL---FVVRKDPNLTE------------------EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKD 563
Cdd:cd05918 393 KPKDGSSSPQlvaFVVLDGSSSGSgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRA 472
|
..
gi 499271215 564 LR 565
Cdd:cd05918 473 LR 474
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
51-564 |
9.93e-28 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 116.92 E-value: 9.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKgdrvavmmpnilQNPVIVYG------------ILRAGFTVVNVNpL 118
Cdd:PRK04813 18 FPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPD------------KSPIIVFGhmspemlatflgAVKAGHAYIPVD-V 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVD-AGAKAIFVLENFAHTVEQVlartevkHVVVASmgdmlgakgaivnlvvrrvkklvpawsipghlSFK 197
Cdd:PRK04813 85 SSPAERIEMIIEvAKPSLIIATEELPLEILGI-------PVITLD--------------------------------ELK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 198 TVLAKGATLGFKRPnVAPGDVAFLQYTGGTTGVSKGATLTHANLLS--NmaqmelWLNTAFlrkPRPESLTFMcALPLYH 275
Cdd:PRK04813 126 DIFATGNPYDFDHA-VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSftN------WMLEDF---ALPEGPQFL-NQAPYS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 276 iFALTVNSLM-GLATGGNniLIPNPRDIPAFVKELgryrtniFPGLNTL-FN-----------ALMNNSeFRKLDFSSLI 342
Cdd:PRK04813 195 -FDLSVMDLYpTLASGGT--LVALPKDMTANFKQL-------FETLPQLpINvwvstpsfadmCLLDPS-FNEEHLPNLT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 343 LTFGGGMAVQRPVAERWLELTgcP---IHEGYGLSETSpVA------TANRLDTDDfTGTIGIPLPSTEVEIRDEDGRTL 413
Cdd:PRK04813 264 HFLFCGEELPHKTAKKLLERF--PsatIYNTYGPTEAT-VAvtsieiTDEMLDQYK-RLPIGYAKPDSPLLIIDEEGTKL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 414 PVGEIGEICIRGPQVMAGYWQRPEETARA-ISPDG--FFRTGDVGFMnaegltkivdrKKDMILVSG-------FNVFPN 483
Cdd:PRK04813 340 PDGEQGEIVISGPSVSKGYLNNPEKTAEAfFTFDGqpAYHTGDAGYL-----------EDGLLFYQGridfqikLNGYRI 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 484 EIEEVaATH----PGILECAAIGVADPHSGEAVKLFVVRKDPNLTEE-----EVKRHCAASLTNYKRPRYVEFRTELPKS 554
Cdd:PRK04813 409 ELEEI-EQNlrqsSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREfeltkAIKKELKERLMEYMIPRKFIYRDSLPLT 487
|
570
....*....|
gi 499271215 555 NVGKILRKDL 564
Cdd:PRK04813 488 PNGKIDRKAL 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
58-488 |
1.23e-27 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.73 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGlAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYTPREL--EHQ------LV 129
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESArrHHQerllsiIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 130 DAGAKAIFVLENFAHTVEQVlartevkhvvvasmgDMLGAKGAivnlvvrrvkklvpawsiPGHLSFKTVLAKGATlGFK 209
Cdd:PRK05691 114 DAEPRLLLTVADLRDSLLQM---------------EELAAANA------------------PELLCVDTLDPALAE-AWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 RPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNmaqmELWLNTAFLRKPRPESlTFMCALPLYHIFALTVNSLMGLAT 289
Cdd:PRK05691 160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVAN----EQLIRHGFGIDLNPDD-VIVSWLPLYHDMGLIGGLLQPIFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNNILIPnprdiPAF--------VKELGRYRTNIFPGLN---TLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAER 358
Cdd:PRK05691 235 GVPCVLMS-----PAYflerplrwLEAISEYGGTISGGPDfayRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLER 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 359 WLE-LTGCPIHE-----GYGLSE-TSPVA--------TANRLDTDDF--------TGTI----GIPLPSTEVEIRD-EDG 410
Cdd:PRK05691 310 FAEkFAACGFDPdsffaSYGLAEaTLFVSggrrgqgiPALELDAEALarnraepgTGSVlmscGRSQPGHAVLIVDpQSL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 411 RTLPVGEIGEICIRGPQVMAGYWQRPEETARA-ISPDG--FFRTGDVGFMNaEGLTKIVDRKKDMILVSGFNVFPNEIEE 487
Cdd:PRK05691 390 EVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEK 468
|
.
gi 499271215 488 V 488
Cdd:PRK05691 469 T 469
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
217-565 |
2.18e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 113.60 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlntAFLRKPRpeslTFMCALPLYHIFALTVnsLMGLATGGNNILI 296
Cdd:PRK07824 36 DVALVVATSGTTGTPKGAMLTAAALTASADATH-----DRLGGPG----QWLLALPAHHIAGLQV--LVRSVIAGSEPVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 P------NPRDIPAFVKELG---RYrTNIFPglNTLFNALMNNSEFRKL-DFSSLILtfgGGMAVQRPVAERWLELtGCP 366
Cdd:PRK07824 105 LdvsagfDPTALPRAVAELGggrRY-TSLVP--MQLAKALDDPAATAALaELDAVLV---GGGPAPAPVLDAAAAA-GIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVATANrldtddftgtiGIPLPSteVEIRDEDGRtlpvgeigeICIRGPQVMAGYwqRPEETARAISPD 446
Cdd:PRK07824 178 VVRTYGMSETSGGCVYD-----------GVPLDG--VRVRVEDGR---------IALGGPTLAKGY--RNPVDPDPFAEP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 447 GFFRTGDVGFMNaEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRK-DPNLTE 525
Cdd:PRK07824 234 GWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDgGPAPTL 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499271215 526 EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07824 313 EALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-565 |
2.71e-27 |
|
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: 115.61 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 62 TFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLEN 141
Cdd:cd05915 26 TYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 142 FAHTVEQVLArtevkhvVVASMGDmlgakgaivNLVVRRVKKLVPAWSIPGHLSFKTVlakgatlgfkRPnVAPGDVAFL 221
Cdd:cd05915 106 LLPLVEAIRG-------ELKTVQH---------FVVMDEKAPEGYLAYEEALGEEADP----------VR-VPERAACGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 222 QYTGGTTGVSKGATLTHANLLSNMAQMELWlnTAFLRKPRPeslTFMCALPLYHI----FALTVNslmglATGGNNILIP 297
Cdd:cd05915 159 AYTTGTTGLPKGVVYSHRALVLHSLAASLV--DGTALSEKD---VVLPVVPMFHVnawcLPYAAT-----LVGAKQVLPG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 NPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGG-------MAVQRPVAERWLELTGCPihEG 370
Cdd:cd05915 229 PRLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGsaaprslIARFERMGVEVRQGYGLT--ET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 371 YGLS---------ETSPVATANRLDTDD----FTGTIGIPLPSTEVEirDEDGRTLPVgeigeICIRGPQVMAGYWQRPE 437
Cdd:cd05915 307 SPVVvqnfvkshlESLSEEEKLTLKAKTglpiPLVRLRVADEEGRPV--PKDGKALGE-----VQLKGPWITGGYYGNEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 438 ETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV 517
Cdd:cd05915 380 ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVV 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 499271215 518 RKDPNLTEEEVKRHCAASLTNYKR-PRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05915 460 PRGEKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
43-565 |
3.11e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 115.71 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 43 HAVAQYSWRPAFT-CMGKAltfSDLNTHSakigawlqslgLAKGDRVAVMMPNIlqnPVIV---YGILRAGFTVVNVNPL 118
Cdd:PLN02479 41 HGSVRYTWAQTYQrCRRLA---SALAKRS-----------IGPGSTVAVIAPNI---PAMYeahFGVPMAGAVVNCVNIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YTPRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKhvvvasmgdmlgAKGAIvnlvvRRVKKLVPAWSIPGHLSFKT 198
Cdd:PLN02479 104 LNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEK------------KKSSF-----KPPLLIVIGDPTCDPKSLQY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 VLAKGAT-----LGFKRPNVA---PGD----VAfLQYTGGTTGVSKGATLTH--ANLLSnMAQMELWlntaflrkPRPES 264
Cdd:PLN02479 167 ALGKGAIeyekfLETGDPEFAwkpPADewqsIA-LGYTSGTTASPKGVVLHHrgAYLMA-LSNALIW--------GMNEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 265 LTFMCALPLYHI----FALTVNSLMGlatggNNILIpnpRDIP--AFVKELGRYRTNIFPGLNTLFNALMNNS-EFRKLD 337
Cdd:PLN02479 237 AVYLWTLPMFHCngwcFTWTLAALCG-----TNICL---RQVTakAIYSAIANYGVTHFCAAPVVLNTIVNAPkSETILP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 338 FSSLILTFGGGmAVQRPVAERWLELTGCPIHEGYGLSETS---------------PVATANRLDTDDFTGTIGI------ 396
Cdd:PLN02479 309 LPRVVHVMTAG-AAPPPSVLFAMSEKGFRVTHTYGLSETYgpstvcawkpewdslPPEEQARLNARQGVRYIGLegldvv 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 397 ------PLPSteveirdeDGRTlpvgeIGEICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKK 470
Cdd:PLN02479 388 dtktmkPVPA--------DGKT-----MGEIVMRGNMVMKGYLKNPKANEEAFA-NGWFHSGDLGVKHPDGYIEIKDRSK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 471 DMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV------RKDPNLTEEEVKRHCAASLTNYKRPRY 544
Cdd:PLN02479 454 DIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTlkpgvdKSDEAALAEDIMKFCRERLPAYWVPKS 533
|
570 580
....*....|....*....|.
gi 499271215 545 VEFrTELPKSNVGKILRKDLR 565
Cdd:PLN02479 534 VVF-GPLPKTATGKIQKHVLR 553
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
61-561 |
3.15e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 115.81 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGlAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYTP-RELEHQLVDAgakaifvl 139
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVPqGGAHDERVSA-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 enfahtveqVLARTEVKHVVVASmgdmlgakgAIVNLVVRRVKKLvPAWSIPGHLSFKTV-LAKGATLGFKRPNvAPgDV 218
Cdd:PRK05850 104 ---------VLRDTSPSVVLTTS---------AVVDDVTEYVAPQ-PGQSAPPVIEVDLLdLDSPRGSDARPRD-LP-ST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLSNMAQMelwLNTAFLRKPR--PESLTFMCALPLYHIfaltvnslMGLATGgnnILI 296
Cdd:PRK05850 163 AYLQYTSGSTRTPAGVMVSHRNVIANFEQL---MSDYFGDTGGvpPPDTTVVSWLPFYHD--------MGLVLG---VCA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 297 P----------------------------NPRDI---PAFVKELGRYRTNifpglntlfnalmnNSEFRKLDFSSLILTF 345
Cdd:PRK05850 229 PilggcpavltspvaflqrparwmqllasNPHAFsaaPNFAFELAVRKTS--------------DDDMAGLDLGGVLGII 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 346 GGGMAVQRPVAERWLE------LTGCPIHEGYGLSE-TSPVAT---------------------ANRLDTDDFTGTIGIP 397
Cdd:PRK05850 295 SGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEaTVYVATrepgqppesvrfdyeklsaghAKRCETGGGTPLVSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 398 LP-STEVEIRDEDGRT-LPVGEIGEICIRGPQVMAGYWQRPEETAR----------AISPDG-FFRTGDVGFMnAEGLTK 464
Cdd:PRK05850 375 SPrSPTVRIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERtfgatlvdpsPGTPEGpWLRTGDLGFI-SEGELF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 465 IVDRKKDMILVSGFNVFPNEIEE-VAATHPGilECAAIGVADPHSGEAVKLFVVRKDPNLTEE------EVKRHCAASLT 537
Cdd:PRK05850 454 IVGRIKDLLIVDGRNHYPDDIEAtIQEITGG--RVAAISVPDDGTEKLVAIIELKKRGDSDEEamdrlrTVKREVTSAIS 531
|
570 580
....*....|....*....|....*...
gi 499271215 538 NYKRPRYVEF----RTELPKSNVGKILR 561
Cdd:PRK05850 532 KSHGLSVADLvlvaPGSIPITTSGKIRR 559
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
83-558 |
3.54e-27 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 116.35 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 83 AKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNplYTP--RELEHQLVDAGAKAIFVLENF------AHTVEQVlarTE 154
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YTAgvKGLTSAITAAEIKTIFTSRQFldkgklWHLPEQL---TQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 155 VKHVVVASMGDmlgakgaivnlVVRRVKKLvpaWsIPGHLsfktVLAKGATLGFKrpnvaPGDVAFLQYTGGTTGVSKGA 234
Cdd:PRK08043 328 VRWVYLEDLKD-----------DVTTADKL---W-IFAHL----LMPRLAQVKQQ-----PEDAALILFTSGSEGHPKGV 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 235 TLTHANLLSNMAQMELWLNtaFLRKPRpesltFMCALPLYHIFALTVNSLMGLATGGNNILIPNP---RDIPAFVKElgR 311
Cdd:PRK08043 384 VHSHKSLLANVEQIKTIAD--FTPNDR-----FMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyRIVPELVYD--R 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 312 YRTNIFpGLNTLfnaLMNNSEF-RKLDFSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETSPVATANrLDTDDF 390
Cdd:PRK08043 455 NCTVLF-GTSTF---LGNYARFaNPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSIN-VPMAAK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 391 TGTIGIPLPSTeveirdeDGRTLPVGEI---GEICIRGPQVMAGYW--QRP-------EETARAISPDGFFRTGDVGFMN 458
Cdd:PRK08043 530 PGTVGRILPGM-------DARLLSVPGIeqgGRLQLKGPNIMNGYLrvEKPgvlevptAENARGEMERGWYDTGDIVRFD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 459 AEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVrkDPNLTEEEV----KRHCAA 534
Cdd:PRK08043 603 EQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DSELTREKLqqyaREHGVP 680
|
490 500
....*....|....*....|....
gi 499271215 535 SLTnykRPRYVEFRTELPKSNVGK 558
Cdd:PRK08043 681 ELA---VPRDIRYLKQLPLLGSGK 701
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
57-565 |
4.22e-27 |
|
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: 115.74 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 57 MGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPV---------IVYGILRAGFTvvnvnplytPRELEHQ 127
Cdd:cd05966 81 QSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIamlacarigAVHSVVFAGFS---------AESLADR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 128 LVDAGAKAIFvlenfahTVEQVLARTEV---KHVVvasmGDMLGAKGAIVN-LVVRRVKKLVPaWSIPGHLSFKTVLAKg 203
Cdd:cd05966 152 INDAQCKLVI-------TADGGYRGGKViplKEIV----DEALEKCPSVEKvLVVKRTGGEVP-MTEGRDLWWHDLMAK- 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 204 atlgfKRPNVAPG-----DVAFLQYTGGTTGVSKGATLTHANLLsnmaqmeLWLNTAFlrkprpeSLTFMcalplYH--- 275
Cdd:cd05966 219 -----QSPECEPEwmdseDPLFILYTSGSTGKPKGVVHTTGGYL-------LYAATTF-------KYVFD-----YHpdd 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 276 IFALTVNslMGLATGGNNIL---------------IPNPRDIPAFVKELGRYRTNIFPGLNTLFNALM--NNSEFRKLDF 338
Cdd:cd05966 275 IYWCTAD--IGWITGHSYIVygplangattvmfegTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMkfGDEWVKKHDL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 SSLIL--TFGGGMAvqrPVAERWL-ELTG---CPIHEGYGLSET-----SPVATAnrldTDDFTGTIGIPLPSTEVEIRD 407
Cdd:cd05966 353 SSLRVlgSVGEPIN---PEAWMWYyEVIGkerCPIVDTWWQTETggimiTPLPGA----TPLKPGSATRPFFGIEPAILD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 408 EDGRTLPVGEIGEICIRG--PQVMAGYW---QRPEETARAISPDGFFrTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFP 482
Cdd:cd05966 426 EEGNEVEGEVEGYLVIKRpwPGMARTIYgdhERYEDTYFSKFPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 483 NEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-----PNLtEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVG 557
Cdd:cd05966 505 AEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepsDEL-RKELRKHVRKEIGPIATPDKIQFVPGLPKTRSG 583
|
....*...
gi 499271215 558 KILRKDLR 565
Cdd:cd05966 584 KIMRRILR 591
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
61-470 |
7.72e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 115.46 E-value: 7.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIfvle 140
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI---- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 nfahtveqVLARTEVKHVVvasmgDMLGaKGAIVNLVVRRVKKLVPAWSIPGH--LSFKTVLAKGATLGFKRPNVAPG-- 216
Cdd:PTZ00216 198 --------VCNGKNVPNLL-----RLMK-SGGMPNTTIIYLDSLPASVDTEGCrlVAWTDVVAKGHSAGSHHPLNIPEnn 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 217 -DVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTafLRKPRPESLTFMCALPLYHIFALTVNSLMgLATGgnnIL 295
Cdd:PTZ00216 264 dDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLND--LIGPPEEDETYCSYLPLAHIMEFGVTNIF-LARG---AL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 296 I--PNPRDIP-AFVK---ELGRYRTNIFPGLNTLFN------------------------------ALMNNSE------- 332
Cdd:PTZ00216 338 IgfGSPRTLTdTFARphgDLTEFRPVFLIGVPRIFDtikkaveaklppvgslkrrvfdhayqsrlrALKEGKDtpywnek 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 ----FRKLDFSSLILTFGGGMAVQRPVAErWLELTGCPIHEGYGLSETSPVATANRLDtDDFTGTIGIPLPSTEVEIRDE 408
Cdd:PTZ00216 418 vfsaPRAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTETVCCGGIQRTG-DLEPNAVGQLLKGVEMKLLDT 495
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271215 409 DG---------RtlpvgeiGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKK 470
Cdd:PTZ00216 496 EEykhtdtpepR-------GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
213-565 |
3.38e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 112.43 E-value: 3.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 213 VAPGDVAFLQYTGGTTGVSKGATLTHANLL----SNMAQMELwlntaflrkprPESLTFMCALPLYHIFALTVNSLMGLA 288
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAfagrALTERFGL-----------TRDDVCYVSMPLFHSNAVMAGWAPAVA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 289 TGGnniLIPNPRDIPA--FVKELGRYRTNIFPGLNTLFNALMNNSEfrKLDFSSLILTFG-GGMAVQRPVAE---RWlel 362
Cdd:PRK13388 216 SGA---AVALPAKFSAsgFLDDVRRYGATYFNYVGKPLAYILATPE--RPDDADNPLRVAfGNEASPRDIAEfsrRF--- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 363 tGCPIHEGYGLSETSPVATanrLDTDDFTGTIGIPLPSTE-----------VEIRDEDGRTL-PVGEIGEIC-IRGPQVM 429
Cdd:PRK13388 288 -GCQVEDGYGSSEGAVIVV---REPGTPPGSIGRGAPGVAiynpetltecaVARFDAHGALLnADEAIGELVnTAGAGFF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 430 AGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSG 509
Cdd:PRK13388 364 EGYYNNPEATAERMR-HGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 510 EAVKLFVVRKDP-NLTEEEVKRHCAAS--LTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK13388 443 DQVMAALVLRDGaTFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
61-527 |
5.85e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 112.52 E-value: 5.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGlAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYTPRELEH-QLVDAgakaifVL 139
Cdd:PRK07769 56 LTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHvGRLHA------VL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 140 ENFAHTVeqVLARTEvkhvvvasmgdmlGAKGaivnlvVRRVKKLVPAWSIPGHLSFKTVL-AKGATlgFKRPNVAPGDV 218
Cdd:PRK07769 126 DDCTPSA--ILTTTD-------------SAEG------VRKFFRARPAKERPRVIAVDAVPdEVGAT--WVPPEANEDTI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKGATLTHANLLSNMAQM----ELWLNTaflrkprpESLTFmcaLPLYHIfaltvnslMGLAT----- 289
Cdd:PRK07769 183 AYLQYTSGSTRIPAGVQITHLNLPTNVLQVidalEGQEGD--------RGVSW---LPFFHD--------MGLITvllpa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 -GGNNILIPNPRdipAFVKELGR----------YRTNIFPGL-NTLFN-----ALMNNSEfRKLDFSSLILTFGGGMAVQ 352
Cdd:PRK07769 244 lLGHYITFMSPA---AFVRRPGRwirelarkpgGTGGTFSAApNFAFEhaaarGLPKDGE-PPLDLSNVKGLLNGSEPVS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 353 RPVAERWLE------LTGCPIHEGYGLSE------TSPVATANR---LDTDDF-TGTI---------GIPLPSTEVEIRD 407
Cdd:PRK07769 320 PASMRKFNEafapygLPPTAIKPSYGMAEatlfvsTTPMDEEPTviyVDRDELnAGRFvevpadapnAVAQVSAGKVGVS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 408 E-----DGRT---LPVGEIGEICIRGPQVMAGYWQRPEETARAI---------------SPDG--FFRTGDVG-FMNAEg 461
Cdd:PRK07769 400 EwavivDPETaseLPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegAPDDalWVRTGDYGvYFDGE- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 462 lTKIVDRKKDMILVSGFNVFPNEIEEVA-----ATHPGILecAAIGV----------ADPHSGeavklfvVRKDPNLTEE 526
Cdd:PRK07769 479 -LYITGRVKDLVIIDGRNHYPQDLEYTAqeatkALRTGYV--AAFSVpanqlpqvvfDDSHAG-------LKFDPEDTSE 548
|
.
gi 499271215 527 E 527
Cdd:PRK07769 549 Q 549
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-530 |
1.33e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 109.86 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAiFVLE 140
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDA-FIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAhtveqvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghlsfktvlakgatlgfkrpnvapGDVAF 220
Cdd:cd05910 82 PKA------------------------------------------------------------------------DEPAA 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 LQYTGGTTGVSKGATLTHANLlsnMAQMELwLNTAFlrKPRPESLTfmcaLPLYHIFALtVNSLMGLATggnniLIP--- 297
Cdd:cd05910 90 ILFTSGSTGTPKGVVYRHGTF---AAQIDA-LRQLY--GIRPGEVD----LATFPLFAL-FGPALGLTS-----VIPdmd 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 298 -------NPRDIPAFVKELGRyrTNIFpGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLELT--GCPIH 368
Cdd:cd05910 154 ptrparaDPQKLVGAIRQYGV--SIVF-GSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEIL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 369 EGYGLSETSPVA--------TANRLDTDDFTGT-IGIPLPSTEV---EIRDE------DGRTLPVGEIGEICIRGPQVMA 430
Cdd:cd05910 231 TPYGATEALPVSsigsrellATTTAATSGGAGTcVGRPIPGVRVriiEIDDEpiaewdDTLELPRGEIGEITVTGPTVTP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 431 GYWQRPEETARAISPDG----FFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADP 506
Cdd:cd05910 311 TYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKP 390
|
490 500
....*....|....*....|....
gi 499271215 507 hsGEAVKLFVVRKDPnLTEEEVKR 530
Cdd:cd05910 391 --GCQLPVLCVEPLP-GTITPRAR 411
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
215-565 |
1.80e-25 |
|
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: 109.41 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 215 PGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMElwlNTAFLRKPRPESLTFMCAlplyHIFALTVNSLMGLATGGNNI 294
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS---ERYFGRDNGDEAVLFFSN----YVFDFFVEQMTLALLNGQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 LIPNPR---DIPAFVKELGRYRTNIFPGLNTLFNALmnnsEFRKLDfsSLILTFGGGMAVQRPVAERWLELTGCPIHEGY 371
Cdd:cd17648 166 VVPPDEmrfDPDRFYAYINREKVTYLSGTPSVLQQY----DLARLP--HLKRVDAAGEEFTAPVFEKLRSRFAGLIINAY 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 372 GLSETSPVATANRLDTDD-FTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-- 448
Cdd:cd17648 240 GPTETTVTNHKRFFPGDQrFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqt 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 449 ------------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKL-- 514
Cdd:cd17648 320 eqerargrnarlYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQky 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499271215 515 ---FVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIlrkDLR 565
Cdd:cd17648 400 lvgYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL---DVR 450
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-564 |
1.92e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 108.97 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMelwlNTAFlrkPRPESLTFMCALPLYHIFALTVNSLMGLATG 290
Cdd:PRK08308 96 VNYLAEEPSLLQYSSGTTGEPKLIRRSWTEIDREIEAY----NEAL---NCEQDETPIVACPVTHSYGLICGVLAALTRG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNNILI--PNPRDIPAFVKElgrYRTNIFPGLNTLFNALmnnSEFRKLDFsslilTFGGGMAVQRPVAERWL-ELTGCPI 367
Cdd:PRK08308 169 SKPVIItnKNPKFALNILRN---TPQHILYAVPLMLHIL---GRLLPGTF-----QFHAVMTSGTPLPEAWFyKLRERTT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 H--EGYGLSETSPVATANRLDTddfTGTIGIPLPSTEVEI-RDEDgrtlpvgEIGEICIRGPQvmagywqrpeetaRAIs 444
Cdd:PRK08308 238 YmmQQYGCSEAGCVSICPDMKS---HLDLGNPLPHVSVSAgSDEN-------APEEIVVKMGD-------------KEI- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 445 pdgffRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVrKDPNLT 524
Cdd:PRK08308 294 -----FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEID 367
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 499271215 525 EEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK08308 368 PVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-564 |
2.16e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.80 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 7 QQAGSSTAKIWlgSYPPGVPAEigpltyRSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGD 86
Cdd:PRK05691 1111 DAAERAQLAQW--GQAPCAPAQ------AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDV 1182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 87 RVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKaifVLENFAHTVEQVlarTEVKHVVVASMgDM 166
Cdd:PRK05691 1183 CVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVE---LLLTQSHLLERL---PQAEGVSAIAL-DS 1255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 167 LGAKGaivnlvvrrvkklvpaWsipghlsfktvlakgatlgfkrPNVAPG------DVAFLQYTGGTTGVSKGATLTHAN 240
Cdd:PRK05691 1256 LHLDS----------------W----------------------PSQAPGlhlhgdNLAYVIYTSGSTGQPKGVGNTHAA 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 241 LLSNMAQME----LWLNTAFLRKPrPESL---TFMCALPLyhifaLTVNSLMgLATGGNNiliPNPRDIPAFVKELGRYR 313
Cdd:PRK05691 1298 LAERLQWMQatyaLDDSDVLMQKA-PISFdvsVWECFWPL-----ITGCRLV-LAGPGEH---RDPQRIAELVQQYGVTT 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 314 TNIFPGLNTLFNalmnnSEFRKLDFSSLILTFGGGMAVQRPVAERWLE-LTGCPIHEGYGLSETSPVATANRLDTDDFTG 392
Cdd:PRK05691 1368 LHFVPPLLQLFI-----DEPLAAACTSLRRLFSGGEALPAELRNRVLQrLPQVQLHNRYGPTETAINVTHWQCQAEDGER 1442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 393 T-IGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTK 464
Cdd:PRK05691 1443 SpIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGALE 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 465 IVDRKKDMILVSGFNVFPNEIEEVAATHPGIlECAAIGVADPHSG-EAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPR 543
Cdd:PRK05691 1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGV-AQAAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPA 1601
|
570 580
....*....|....*....|.
gi 499271215 544 YVEFRTELPKSNVGKILRKDL 564
Cdd:PRK05691 1602 QLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
211-565 |
1.65e-24 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 107.16 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 211 PNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESLTFMCALPLYHIFALTVnSLMGLATG 290
Cdd:PRK05851 147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLD------AATDVGCSWLPLYHDMGLAF-LLTAALAG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNNILIPNPrdipAF-------VKELGRYRTNIFPGLNTLFNALMNNSE-FRKLDFSSLILTFGGGMAVQRPVAERWLE- 361
Cdd:PRK05851 220 APLWLAPTT----AFsaspfrwLSWLSDSRATLTAAPNFAYNLIGKYARrVSDVDLGALRVALNGGEPVDCDGFERFATa 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 362 -----LTGCPIHEGYGLSE-----TSPV----ATANRLDTDDFTGT-----IGIPLPSTEVEIRDEDGRTLPVG-EIGEI 421
Cdd:PRK05851 296 mapfgFDAGAAAPSYGLAEstcavTVPVpgigLRVDEVTTDDGSGArrhavLGNPIPGMEVRISPGDGAAGVAGrEIGEI 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 422 CIRGPQVMAGYWQRPeetarAISPDGFFRTGDVGFMNAEGLTkIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAI 501
Cdd:PRK05851 376 EIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 502 GVADPHSGEAVKL-----FVVRKDPNLTEEEVKR---HCAASltnykrPRYVEFRT--ELPKSNVGKILRKDLR 565
Cdd:PRK05851 450 AVGTGEGSARPGLviaaeFRGPDEAGARSEVVQRvasECGVV------PSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
61-565 |
1.93e-24 |
|
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: 106.11 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQlVDAGAKAIFVLE 140
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDR-VDRGGAVYAAVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQVLartevkhvVVASMGDMLGAKgaivnlVVRRVKKLVPAwsipGHLSfkTVLAKGatlgfkrpnVAPGDVaf 220
Cdd:cd05974 80 ENTHADDPML--------LYFTSGTTSKPK------LVEHTHRSYPV----GHLS--TMYWIG---------LKPGDV-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 221 lqytggttgvskgatltHANLLSNMAQMELWLNtaflrkprpesltfmcalplyhIFAltvnslmGLATGGNNILIPNPR 300
Cdd:cd05974 129 -----------------HWNISSPGWAKHAWSC----------------------FFA-------PWNAGATVFLFNYAR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 301 -DIPAFVKELGRYRTNIFPGLNTLFNALM--NNSEFRkldfSSLILTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETS 377
Cdd:cd05974 163 fDAKRVLAALVRYGVTTLCAPPTVWRMLIqqDLASFD----VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 378 pVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRtlPVGEiGEICI-----RGPQVMAGYWQRPEETARAISpDGFFRTG 452
Cdd:cd05974 239 -ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA--PATE-GEVALdlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 453 DVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVV-----RKDPNlTEEE 527
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPE-TALE 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 499271215 528 VKRHCAASLTNYKRPRYVEFRtELPKSNVGKILRKDLR 565
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
39-476 |
3.83e-24 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 106.82 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 39 EFFDHAVAQYSWRpaftcmgkalTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQnpVIVYGILRAGFTVVNVnPL 118
Cdd:PLN02430 65 RIVDGKVGPYMWK----------TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQ--WIVAMEACAAHSLICV-PL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 119 YT---PRELEHQLVDAGAKAIFVLEnfahtveqvlarTEVKHVVVAsmgDMLGAKgaivnlvvrRVKKLVPAWSIPGHLS 195
Cdd:PLN02430 132 YDtlgPGAVDYIVDHAEIDFVFVQD------------KKIKELLEP---DCKSAK---------RLKAIVSFTSVTEEES 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 196 FKtvlakGATLGFK-----------RPNVA------PGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTaFLR 258
Cdd:PLN02430 188 DK-----ASQIGVKtyswidflhmgKENPSetnppkPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQ-FED 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 259 KPRPESLtFMCALPLYHI-------FALTVNSLMGLATGGNNILIPN------------PR-------DIPAFVKELGRY 312
Cdd:PLN02430 262 KMTHDDV-YLSFLPLAHIldrmieeYFFRKGASVGYYHGDLNALRDDlmelkptllagvPRvferiheGIQKALQELNPR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 313 RTNIFPGLNTLFNALMNNSEFRK--------LDFSSLILTFGG-------GMAVQRPVAERWLELTGCP-IHEGYGLSET 376
Cdd:PLN02430 341 RRLIFNALYKYKLAWMNRGYSHKkaspmadfLAFRKVKAKLGGrlrllisGGAPLSTEIEEFLRVTSCAfVVQGYGLTET 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 377 SPVATANRLDTDDFTGTIGIPlpSTEVEIRDEDGRTL---PVGE--IGEICIRGPQVMAGYWQRPEETARAISpDGFFRT 451
Cdd:PLN02430 421 LGPTTLGFPDEMCMLGTVGAP--AVYNELRLEEVPEMgydPLGEppRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHT 497
|
490 500
....*....|....*....|....*
gi 499271215 452 GDVGFMNAEGLTKIVDRKKDMILVS 476
Cdd:PLN02430 498 GDIGEILPNGVLKIIDRKKNLIKLS 522
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
51-565 |
4.79e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 105.92 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 51 RPAFTCMGKALTFSDLNTHSAKIGAWLqsLGLAKGDR---VAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQ 127
Cdd:PRK07867 19 DRGLYFEDSFTSWREHIRGSAARAAAL--RARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 128 LVDAGAKAIFVLENFAHTVEQVLarTEVKHVVVASmgdmlgakgaivnlvvrrvkklvPAWSipghlsfkTVLAKGATLG 207
Cdd:PRK07867 97 IAHADCQLVLTESAHAELLDGLD--PGVRVINVDS-----------------------PAWA--------DELAAHRDAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 208 FKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLS---NMAQMelwlntaflRKPRPESLTFMCaLPLYHIFALTVNSL 284
Cdd:PRK07867 144 PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASagvMLAQR---------FGLGPDDVCYVS-MPLFHSNAVMAGWA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 MGLATGGNNILipnPRDIPA--FVKELGRYRTnifpglnTLFN------ALMNNSEFRKLDFS-SLILTFGG-GMAVQrp 354
Cdd:PRK07867 214 VALAAGASIAL---RRKFSAsgFLPDVRRYGA-------TYANyvgkplSYVLATPERPDDADnPLRIVYGNeGAPGD-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 355 vAERWLELTGCPIHEGYGLSETSpVATANRLDTDdfTGTIGIPLPstEVEIRDED-GRTLPVGE------------IGEI 421
Cdd:PRK07867 282 -IARFARRFGCVVVDGFGSTEGG-VAITRTPDTP--PGALGPLPP--GVAIVDPDtGTECPPAEdadgrllnadeaIGEL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 422 C-IRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:PRK07867 356 VnTAGPGGFEGYYNDPEADAERMR-GGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAV 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499271215 501 IGVADPHSGEAVKLFVV-RKDPNLTEEEVKRHCAAS--LTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK07867 435 YAVPDPVVGDQVMAALVlAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLS 502
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
36-564 |
5.29e-24 |
|
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: 105.21 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 36 SIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNV 115
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 116 NPLYTPRELEHQLVDAGakaIFVLenfahtVEQvlartevkhvvvasmgdmlgakgaivnlvvrrvkklvpawsipghls 195
Cdd:cd17644 81 DPNYPQERLTYILEDAQ---ISVL------LTQ----------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 196 fktvlakgatlgfkrpnvaPGDVAFLQYTGGTTGVSKGATLTHANL--LSNMAQMELWLnTAFLRKPRPESLTFMCALPl 273
Cdd:cd17644 105 -------------------PENLAYVIYTSGSTGKPKGVMIEHQSLvnLSHGLIKEYGI-TSSDRVLQFASIAFDVAAE- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 yHIFALtvnslmgLATGGNNILIPNP--RDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDF-SSLILTFGGGMA 350
Cdd:cd17644 164 -EIYVT-------LLSGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 351 VQRPVAERWLELTGCPIH--EGYGLSETSPVATANRLDTDDFTG----TIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR 424
Cdd:cd17644 236 VQPELVRQWQKNVGNFIQliNVYGPTEATIAATVCRLTQLTERNitsvPIGRPIANTQVYILDENLQPVPVGVPGELHIG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQVMAGYWQRPEETARAISPDGF--------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGIL 496
Cdd:cd17644 316 GVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 497 ECAAIGVADPHSGEAVKLFVVRKDPN-LTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:cd17644 396 TAVVIVREDQPGNKRLVAYIVPHYEEsPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
213-565 |
6.65e-24 |
|
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: 104.82 E-value: 6.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 213 VAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESLTFMCaLPLYHIFAL---TVNSLMGlat 289
Cdd:cd05937 84 VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLK------NGDRTYTC-MPLYHGTAAflgACNCLMS--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 gGNNILIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMavqRP-VAERWLELTGCP-I 367
Cdd:cd05937 154 -GGTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGL---RPdIWERFRERFNVPeI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 HEGYglSETSPVATANRLDTDDFT-GTIG--------------IPL---PSTEVEIRDEdgRT-----LPVGEIGEICIR 424
Cdd:cd05937 230 GEFY--AATEGVFALTNHNVGDFGaGAIGhhglirrwkfenqvVLVkmdPETDDPIRDP--KTgfcvrAPVGEPGEMLGR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GP----QVMAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPG 494
Cdd:cd05937 306 VPfknrEAFQGYLHNEDATESKLVRDVFrkgdiyFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 495 ILECAAIGVADP-HSGEA----VKLFVVRKDP-NLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05937 386 IAEANVYGVKVPgHDGRAgcaaITLEESSAVPtEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
59-565 |
7.07e-23 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 102.72 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPV-------------IVYGilraGFTVVNVnplyTPR--E 123
Cdd:PRK10524 83 RTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFamlacarigaihsVVFG----GFASHSL----AARidD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 124 LEHQLV---DAGAKAIFVLeNFAHTVEQVLARTEVK--HVvvasmgdmlgakgaivnLVVRRvkKLVPAWSIPGH-LSFK 197
Cdd:PRK10524 155 AKPVLIvsaDAGSRGGKVV-PYKPLLDEAIALAQHKprHV-----------------LLVDR--GLAPMARVAGRdVDYA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 198 TVLAKgaTLGFKRPN--VAPGDVAFLQYTGGTTGVSKGA---TLTHANLLsnMAQMElwlnTAFLRKPrpeSLTFMCALP 272
Cdd:PRK10524 215 TLRAQ--HLGARVPVewLESNEPSYILYTSGTTGKPKGVqrdTGGYAVAL--ATSMD----TIFGGKA---GETFFCASD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 273 L-------YHIFA-LtvnsLMGLATggnnIL---IPNPRDIPAFVKELGRYRtnifpgLNTLFNA--------LMNNSEF 333
Cdd:PRK10524 284 IgwvvghsYIVYApL----LAGMAT----IMyegLPTRPDAGIWWRIVEKYK------VNRMFSAptairvlkKQDPALL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 RKLDFSSLILTFGGGMAVQRPVAeRWL-ELTGCPIHEGYGLSETS-PV-ATANRL-DTDDFTGTIGIPLPSTEVEIRDE- 408
Cdd:PRK10524 350 RKHDLSSLRALFLAGEPLDEPTA-SWIsEALGVPVIDNYWQTETGwPIlAIARGVeDRPTRLGSPGVPMYGYNVKLLNEv 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 409 DGRTLPVGEIGEICIRGP------QVMAG--------YWQRPEETAraispdgfFRTGDVGFMNAEGLTKIVDRKKDMIL 474
Cdd:PRK10524 429 TGEPCGPNEKGVLVIEGPlppgcmQTVWGdddrfvktYWSLFGRQV--------YSTFDWGIRDADGYYFILGRTDDVIN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 475 VSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLT---------EEEVKRHCAASLTNYKRPRYV 545
Cdd:PRK10524 501 VAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadrearlalEKEIMALVDSQLGAVARPARV 580
|
570 580
....*....|....*....|
gi 499271215 546 EFRTELPKSNVGKILRKDLR 565
Cdd:PRK10524 581 WFVSALPKTRSGKLLRRAIQ 600
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
212-487 |
2.39e-22 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 100.89 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 NVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwLNTAFLRKPRPESL-TFMCALPLYHIFALTVNSLMGLATG 290
Cdd:cd05933 146 SQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKA----ASQHMDLRPATVGQeSVVSYLPLSHIAAQILDIWLPIKVG 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 291 GNnILIPNPRDIP-AFVKELGRYRTNIFPGLNTLFN---------------------------------ALMNNSE---- 332
Cdd:cd05933 222 GQ-VYFAQPDALKgTLVKTLREVRPTAFMGVPRVWEkiqekmkavgaksgtlkrkiaswakgvgletnlKLMGGESpspl 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 ---------FRK----LDFSSLILTFGGGMAVQRPVAERWLELTgCPIHEGYGLSETSPVATANRLDTDDFTgTIGIPLP 399
Cdd:cd05933 301 fyrlakklvFKKvrkaLGLDRCQKFFTGAAPISRETLEFFLSLN-IPIMELYGMSETSGPHTISNPQAYRLL-SCGKALP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 400 STEVEI--RDEDGrtlpvgeIGEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVS- 476
Cdd:cd05933 379 GCKTKIhnPDADG-------IGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAg 451
|
330
....*....|.
gi 499271215 477 GFNVFPNEIEE 487
Cdd:cd05933 452 GENVPPVPIED 462
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
52-564 |
6.08e-22 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 100.50 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 52 PAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDA 131
Cdd:PRK10252 475 PALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 132 GAKAIFvlenfahTVEQVLARtevkhvvvasmgdMLGAKGAIVnlvvrrvkklvpawsipghLSFKTVLAKGATLGFKRP 211
Cdd:PRK10252 555 RPSLLI-------TTADQLPR-------------FADVPDLTS-------------------LCYNAPLAPQGAAPLQLS 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 nvAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMaqmeLWLNTAF--------LRKPrPES---------LTFMCalply 274
Cdd:PRK10252 596 --QPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL----LWMQNHYpltaddvvLQKT-PCSfdvsvweffWPFIA----- 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 275 hifaltvnslmglatgGNNILIPNP---RDIPAFVKELGRYR---TNIFPGLNTLFNALMNnSEFRKLDFSSLILTFGGG 348
Cdd:PRK10252 664 ----------------GAKLVMAEPeahRDPLAMQQFFAEYGvttTHFVPSMLAAFVASLT-PEGARQSCASLRQVFCSG 726
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 349 MAVQRPVAERWLELTGCPIHEGYGLSETSPVAT---ANRLDTDDFTGT---IGIPLPSTEVEIRDEDGRTLPVGEIGEIC 422
Cdd:PRK10252 727 EALPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypAFGEELAAVRGSsvpIGYPVWNTGLRILDARMRPVPPGVAGDLY 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 423 IRGPQVMAGYWQRPEETARAISPDGF------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGIL 496
Cdd:PRK10252 807 LTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVE 886
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499271215 497 ECAAIGV----ADPHSGEAVKL---FVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK10252 887 QAVTHACvinqAAATGGDARQLvgyLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
53-500 |
6.35e-22 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 99.73 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 53 AFTCM------GKALTFSDLNTHSAKIGAWLQ-SLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELE 125
Cdd:cd05905 1 AYTLLdskgkeATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 126 hqlvdagakaiFVLENFAHTVEQvlaRTEVKHVVVASMGDMLGAKGAIVNLVVrrVKKLVPAWSIPGHLSFKTVLAKgat 205
Cdd:cd05905 81 -----------FLLGTCKVRVAL---TVEACLKGLPKKLLKSKTAAEIAKKKG--WPKILDFVKIPKSKRSKLKKWG--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 206 lgfKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNtafLRKPRP--ESLTFMCALPLYHifalTVns 283
Cdd:cd05905 142 ---PHPPTRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACE---LYESRPlvTVLDFKSGLGLWH----GC-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 284 LMGLATGGNNILIP------NPrdiPAFVKELGRYR-TNIFPGLNTLFNALMN---NSEFRKL---DFSSL---ILTFGG 347
Cdd:cd05905 210 LLSVYSGHHTILIPpelmktNP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDlssTLASLKNrdvNLSSLrmcMVPCEN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 348 gmavqRP---VAERWLEL--------------TGCPIH-----EGYGLSETSPV-----ATAN---RLDTDDFTGTI--- 394
Cdd:cd05905 287 -----RPrisSCDSFLKLfqtlglspravsteFGTRVNpficwQGTSGPEPSRVyldmrALRHgvvRLDERDKPNSLplq 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 395 --GIPLPSTEVEIRDEDGRTL-PVGEIGEICIRGPQVMAGYWQRPEET------------ARAISPDGFFRTGDVGFMNA 459
Cdd:cd05905 362 dsGKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETndtfkvfpstrlSTGITNNSYARTGLLGFLRP 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 499271215 460 E----------GLTKIVDRKKDMILVSGFNVFPNEIEE-VAATHPGILECAA 500
Cdd:cd05905 442 TkctdlnveehDLLFVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAV 493
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
484-558 |
3.62e-21 |
|
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: 87.60 E-value: 3.62e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499271215 484 EIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKD-PNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGK 558
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
35-564 |
6.71e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 97.55 E-value: 6.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 35 RSIGEFFDHAVAQYSWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVN 114
Cdd:PRK05691 3720 QSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLP 3799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 115 VNPLYTPRELEhQLVDAGAKAIFVLEnfAHTVEQVLArtevkhvvvasMGDMLGAKGAIVNLVVRRVKKLVPAWSIPGHL 194
Cdd:PRK05691 3800 LDPGLPAQRLQ-RIIELSRTPVLVCS--AACREQARA-----------LLDELGCANRPRLLVWEEVQAGEVASHNPGIY 3865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 195 SfktvlakgatlgfkrpnvAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLN---------TAflrkprpeSL 265
Cdd:PRK05691 3866 S------------------GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLAlseadviaqTA--------SQ 3919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 266 TF------MCALPLYhifaltvnslmglatGGNNILIPN--PRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEfRKLD 337
Cdd:PRK05691 3920 SFdisvwqFLAAPLF---------------GARVEIVPNaiAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDR-QALD 3983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 338 FSSLILTFGGGMAVQrpVAERWLE-LTGCPIHEGYGLSETSPVATANRLDTDDFTGT---IGIPLPSTEVEIRDEDGRTL 413
Cdd:PRK05691 3984 GLRWMLPTGEAMPPE--LARQWLQrYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELV 4061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 414 PVGEIGEICIRGPQVMAGYWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIE 486
Cdd:PRK05691 4062 PLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIE 4141
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 487 EVAATHPGILEcAAIGVADPHSGEAVKLFVVRKDPNLTE----EEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRK 562
Cdd:PRK05691 4142 ARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTVLAQgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRK 4220
|
..
gi 499271215 563 DL 564
Cdd:PRK05691 4221 AL 4222
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
22-490 |
1.31e-20 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 95.58 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 22 PPGVpaeigpltyrSIGEFFDHAVAQYSWRPAF-------TCMGKA--LTFSDLNTHSAKIGAWLQSLGlAKGDRVAVMM 92
Cdd:PRK12476 31 PPGT----------TLISLIERNIANVGDTVAYryldhshSAAGCAveLTWTQLGVRLRAVGARLQQVA-GPGDRVAILA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 93 PNILQNPVIVYGILRAGFTVVnvnPLYTPRELEH-QLVDAgakaifVLENFAHTVeqVLARTEVKHVVvasmgdmlgaKG 171
Cdd:PRK12476 100 PQGIDYVAGFFAAIKAGTIAV---PLFAPELPGHaERLDT------ALRDAEPTV--VLTTTAAAEAV----------EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 172 AIVNLVVRRVKKLVPAWSIPghlsfktvlaKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELW 251
Cdd:PRK12476 159 FLRNLPRLRRPRVIAIDAIP----------DSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 252 LNtafLRKPRPESLTFmcaLPLYHIFALTVnsLMGLATGGNNILIPNPRdipAFVKELGRYRTNIFPGLNT--LFNALMN 329
Cdd:PRK12476 229 ID---LLDRNTHGVSW---LPLYHDMGLSM--IGFPAVYGGHSTLMSPT---AFVRRPQRWIKALSEGSRTgrVVTAAPN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 330 NS-----------EFRKLDFSSLILTFGggmavQRPVAERWLE----------LTGCPIHEGYGLSE-TSPVAT------ 381
Cdd:PRK12476 298 FAyewaaqrglpaEGDDIDLSNVVLIIG-----SEPVSIDAVTtfnkafapygLPRTAFKPSYGIAEaTLFVATiapdae 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 382 ---------------ANRLDTDDFTGTI----GIPLPSTEVEIRDED-GRTLPVGEIGEICIRGPQVMAGYWQRPEETAR 441
Cdd:PRK12476 373 psvvyldreqlgagrAVRVAADAPNAVAhvscGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 442 ----------------AISPDG--FFRTGDVGFMnAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAA 490
Cdd:PRK12476 453 tfgaklqsrlaegshaDGAADDgtWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
58-565 |
1.72e-20 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 94.41 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGftvvnvnplytprelehqlvdagakAIF 137
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIG-------------------------VET 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 138 VLENFAHTVEQVLartevkHVVVASmgdmlGAKGAIVNLVvrrvKKLvpawsipgHLSFKTVLAKGATLGFKrpnvapgD 217
Cdd:cd05939 56 ALINSNLRLESLL------HCITVS-----KAKALIFNLL----DPL--------LTQSSTEPPSQDDVNFR-------D 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 218 VAFLQYTGGTTGVSKGATLTHANLLSnMAQMelwlnTAFLRKPRPESLTFMCaLPLYHifalTVNSLMGLAT---GGNNI 294
Cdd:cd05939 106 KLFYIYTSGTTGLPKAAVIVHSRYYR-IAAG-----AYYAFGMRPEDVVYDC-LPLYH----SAGGIMGVGQallHGSTV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 LIPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMavqRPvaERWLELTG----CPIHEG 370
Cdd:cd05939 175 VIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGL---RP--QIWEQFVRrfgiPQIGEF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 371 YGLSEtspvATANRLDTDDFTGTIG---IPLPS------------TEVEIRDEDGRTLPV--GE----IGEICIRGP-QV 428
Cdd:cd05939 250 YGATE----GNSSLVNIDNHVGACGfnsRILPSvypirlikvdedTGELIRDSDGLCIPCqpGEpgllVGKIIQNDPlRR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 429 MAGYWQRpEETARAI------SPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIG 502
Cdd:cd05939 326 FDGYVNE-GATNKKIardvfkKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 503 VADPHS-GEAVKLFVVRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:cd05939 405 VEVPGVeGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
58-551 |
3.27e-20 |
|
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: 94.28 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 58 GKALTFSDLNTHSAKIG-AWLQSLGLAKGDRVAVMMPNilqNPVIVY---GILRAGFTVVNVNPLYTPRELEHQLVDAGA 133
Cdd:cd05938 3 GETYTYRDVDRRSNQAArALLAHAGLRPGDTVALLLGN---EPAFLWiwlGLAKLGCPVAFLNTNIRSKSLLHCFRCCGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 134 KAIFVLENFAHTVEQVLA--RTEVKHVVVASMGDMLGAKGAIVNLVVRRVKKLVPAwSIPGHLSFKTVlakgatlgfkrp 211
Cdd:cd05938 80 KVLVVAPELQEAVEEVLPalRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPA-SLRAHVTIKSP------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 nvapgdvAFLQYTGGTTGVSKGATLTHANLLSNMaqmelwlNTAFLRKPRPESLTFMCaLPLYHIFALTVNSLMGLATGG 291
Cdd:cd05938 147 -------ALYIYTSGTTGLPKAARISHLRVLQCS-------GFLSLCGVTADDVIYIT-LPLYHSSGFLLGIGGCIELGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 292 NNILIPNprdIPA--FVKELGRYRTNIFPGLNTLFNALMNNSEfRKLDFS-SLILTFGGGMavqRP-VAERWLELTGcPI 367
Cdd:cd05938 212 TCVLKPK---FSAsqFWDDCRKHNVTVIQYIGELLRYLCNQPQ-SPNDRDhKVRLAIGNGL---RAdVWREFLRRFG-PI 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 368 H--EGYGLSETSpVATANrldtddFTGTIG------------IPL------PSTEVEIRDEDGRTLPV--GEIG-EIC-I 423
Cdd:cd05938 284 RirEFYGSTEGN-IGFFN------YTGKIGavgrvsylykllFPFelikfdVEKEEPVRDAQGFCIPVakGEPGlLVAkI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 424 RGPQVMAGYWQRPEETARAI------SPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILE 497
Cdd:cd05938 357 TQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQE 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 498 CAAIGVADP-HSGE----AVKLfvvRKDPNLTEEEVKRHCAASLTNYKRPRYVEFRTEL 551
Cdd:cd05938 437 VNVYGVTVPgHEGRigmaAVKL---KPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
195-488 |
3.40e-20 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 94.70 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 195 SFKTVLAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESLT----FMCA 270
Cdd:PLN02614 202 AWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSA------NAALTvkdvYLSY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 271 LPLYHIF-------ALTVNSLMGLATGGNNILIPNPRDI-PAFVKELGRYRTNIFPGLNT------LFNALMNNSEFR-- 334
Cdd:PLN02614 276 LPLAHIFdrvieecFIQHGAAIGFWRGDVKLLIEDLGELkPTIFCAVPRVLDRVYSGLQKklsdggFLKKFVFDSAFSyk 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 335 ------------------KLDFSSLILTFGGGMAV----QRPVA---ERWLELTGC-PIHEGYGLSETSPVATANRLDTD 388
Cdd:PLN02614 356 fgnmkkgqshveasplcdKLVFNKVKQGLGGNVRIilsgAAPLAshvESFLRVVACcHVLQGYGLTESCAGTFVSLPDEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 389 DFTGTIGIPLPSTEVEIR---DEDGRTLPVGEIGEICIRGPQVMAGYWQRpEETARAISPDGFFRTGDVGFMNAEGLTKI 465
Cdd:PLN02614 436 DMLGTVGPPVPNVDIRLEsvpEMEYDALASTPRGEICIRGKTLFSGYYKR-EDLTKEVLIDGWLHTGDVGEWQPNGSMKI 514
|
330 340
....*....|....*....|....
gi 499271215 466 VDRKKDMI-LVSGFNVFPNEIEEV 488
Cdd:PLN02614 515 IDRKKNIFkLSQGEYVAVENIENI 538
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
214-473 |
1.90e-19 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 92.10 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 214 APGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQmelwlntafLRKPRPE---SLTFMCALPLYHIFALTVNSLM---GL 287
Cdd:PLN02387 248 SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAG---------VMTVVPKlgkNDVYLAYLPLAHILELAAESVMaavGA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 288 ATG----------GNNILIPNPRDIPAFVKE--------LGRYRTNIFPGLN-------TLFN-------ALMNNSEF-- 333
Cdd:PLN02387 319 AIGygspltltdtSNKIKKGTKGDASALKPTlmtavpaiLDRVRDGVRKKVDakgglakKLFDiaykrrlAAIEGSWFga 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 334 ---RKLDFSSLIL-----TFGG-------GMAVQRPVAERWLELT-GCPIHEGYGLSETSPVATANRLDtDDFTGTIGIP 397
Cdd:PLN02387 399 wglEKLLWDALVFkkiraVLGGrirfmlsGGAPLSGDTQRFINIClGAPIGQGYGLTETCAGATFSEWD-DTSVGRVGPP 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 398 LPSTEVEIRD-EDGRTL----PVGEiGEICIRGPQVMAGYWQRPEETARAISPDG----FFRTGDVGFMNAEGLTKIVDR 468
Cdd:PLN02387 478 LPCCYVKLVSwEEGGYLisdkPMPR-GEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDR 556
|
....*
gi 499271215 469 KKDMI 473
Cdd:PLN02387 557 KKDIV 561
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
42-476 |
5.27e-19 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 90.67 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 42 DHAVAQYSWrpaftcmgkaLTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVnvnPLYT- 120
Cdd:PLN02861 69 DSKVGPYVW----------LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYV---PLYDt 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 121 --PRELEHQLVDAGAKAIFVLENFAHTVEQVLARTEVKHVVVASMGDmlgakgaIVNLVVRRVKKLVPAWsipghLSFKT 198
Cdd:PLN02861 136 lgANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVSFGD-------VSSEQKEEAEELGVSC-----FSWEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 199 VLAKGaTLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflRKPRPESLTFMCALPLYHIF- 277
Cdd:PLN02861 204 FSLMG-SLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVT--DRVATEEDSYFSYLPLAHVYd 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 278 ------ALTVNSLMGLATGGNNILIPNPRDI-PAFVKELGRYRTNIFPGLN-----------TLF----NALMNNSE--- 332
Cdd:PLN02861 281 qvietyCISKGASIGFWQGDIRYLMEDVQALkPTIFCGVPRVYDRIYTGIMqkissggmlrkKLFdfayNYKLGNLRkgl 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 333 --------FRKLDFSSLILTFGG-------GMAVQRPVAERWLELTGCP-IHEGYGLSETSPVATANRLDTDDFTGTIGI 396
Cdd:PLN02861 361 kqeeasprLDRLVFDKIKEGLGGrvrlllsGAAPLPRHVEEFLRVTSCSvLSQGYGLTESCGGCFTSIANVFSMVGTVGV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 397 PLPSTEVeirdedgRTLPVGEIG----------EICIRGPQVMAGYWQRPEETARAISpDGFFRTGDVGFMNAEGLTKIV 466
Cdd:PLN02861 441 PMTTIEA-------RLESVPEMGydalsdvprgEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKII 512
|
490
....*....|
gi 499271215 467 DRKKDMILVS 476
Cdd:PLN02861 513 DRKKNIFKLS 522
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
220-561 |
8.27e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 90.19 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 220 FLQYTGGTTGVSKGATLTHANLL-----SNMAQMELWLNTAFLRKPRPESLTFmcalplyHIFaltvnsLMGLATGGNNI 294
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGPHLvglkyYWRSIIEKDIPTVVFSHSSIGWVSF-------HGF------LYGSLSLGNTF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 295 L-----IPNPRDIPA-FVKELGRYRTNIFPGLNTLFNALMNNSE-----FRKLDFSSLILTFGGGMAVQRPVAERWLELT 363
Cdd:PTZ00237 325 VmfeggIIKNKHIEDdLWNTIEKHKVTHTLTLPKTIRYLIKTDPeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 364 GCPIHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIR---GPQVMAGYWQRPEETA 440
Cdd:PTZ00237 405 KIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 441 RAISP-DGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEA-VKLFVVR 518
Cdd:PTZ00237 485 QLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVpIGLLVLK 564
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499271215 519 K-------DPNLTEEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKILR 561
Cdd:PTZ00237 565 QdqsnqsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
200-476 |
3.81e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 88.24 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 200 LAKGATLGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWlntAFLRKPRPEslTFMCALPLYHIFAL 279
Cdd:PTZ00342 288 MTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKH---SIFKKYNPK--THLSYLPISHIYER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 280 TVNSLMGLATGGNNILipnPRDIPAFVKELGRYRTNIFPGLNTLFNALMNN--SEFRKLDF------------------- 338
Cdd:PTZ00342 363 VIAYLSFMLGGTINIW---SKDINYFSKDIYNSKGNILAGVPKVFNRIYTNimTEINNLPPlkrflvkkilslrksnnng 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 339 ------------SSLI---------LTFGGGMAVQRPVAERWLELTGCPIHEGYGLSETS-PVATANRLDTDdfTGTIGI 396
Cdd:PTZ00342 440 gfskflegithiSSKIkdkvnpnleVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFVQHADDNN--TESIGG 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 397 PL-PSTEVEIRD----EDGRTLPVGEIgeiCIRGPQVMAGYWQRPEETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKD 471
Cdd:PTZ00342 518 PIsPNTKYKVRTwetyKATDTLPKGEL---LIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKG 594
|
....*
gi 499271215 472 MILVS 476
Cdd:PTZ00342 595 LVKLS 599
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
59-565 |
3.45e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.81 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 59 KALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPV-------------IVYGilraGFTvvnvnplytPRELE 125
Cdd:PRK00174 97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVamlacarigavhsVVFG----GFS---------AEALA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 126 HQLVDAGAKAIFV------------LENfahTVEQVLARTE-VKHVvvasmgdmlgakgaivnLVVRRVKKLVPaWSiPG 192
Cdd:PRK00174 164 DRIIDAGAKLVITadegvrggkpipLKA---NVDEALANCPsVEKV-----------------IVVRRTGGDVD-WV-EG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 193 H-LSFKTVLAKgatlgfkrpnvAPGDVA----------FLQYTGGTTGVSKGATLTHANLLsnmaqmeLWLntaflrkpr 261
Cdd:PRK00174 222 RdLWWHELVAG-----------ASDECEpepmdaedplFILYTSGSTGKPKGVLHTTGGYL-------VYA--------- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 262 peSLTFmcalplYHIFAL---------------TVNSLM--G-LATGGNNIL---IPNPRDIPAFVKELGRYRTNIF--- 317
Cdd:PRK00174 275 --AMTM------KYVFDYkdgdvywctadvgwvTGHSYIvyGpLANGATTLMfegVPNYPDPGRFWEVIDKHKVTIFyta 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 318 PglnTLFNALMN--NSEFRKLDFSSL-ILtfggGmAVQRPV---AERWL-ELTG---CPIHEGYGLSET-----SPVATA 382
Cdd:PRK00174 347 P---TAIRALMKegDEHPKKYDLSSLrLL----G-SVGEPInpeAWEWYyKVVGgerCPIVDTWWQTETggimiTPLPGA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 383 nrldTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRG--PQVMAGYW---QRPEETARAISPDGFFrTGDVGFM 457
Cdd:PRK00174 419 ----TPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYgdhERFVKTYFSTFKGMYF-TGDGARR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 458 NAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGEAVKLFVVRKDPNLTEE----EVKRHCA 533
Cdd:PRK00174 494 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDelrkELRNWVR 573
|
570 580 590
....*....|....*....|....*....|..
gi 499271215 534 ASLTNYKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PRK00174 574 KEIGPIAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
79-461 |
2.90e-16 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 81.79 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 79 SLGLAK--GDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLENFAHTVEQVlartevk 156
Cdd:PRK06334 59 ATKVSKypDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQT------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 157 hvvvasMGDmlGAKGAIVNLVVRRVKKLVPAW-----SIPGHLSFKTVLAKgatlgFKRPNVAPGDVAFLQYTGGTTGVS 231
Cdd:PRK06334 132 ------HGE--DAEYPFSLIYMEEVRKELSFWekcriGIYMSIPFEWLMRW-----FGVSDKDPEDVAVILFTSGTEKLP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 232 KGATLTHANLLSNmaqmelwlNTAFLRKPRPESLTFMCA-LPLYHIFALTVNSLMGLATGGNNILIPNPRDIPAFVKELG 310
Cdd:PRK06334 199 KGVPLTHANLLAN--------QRACLKFFSPKEDDVMMSfLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMID 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 311 RYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQRPVAERWLEL-TGCPIHEGYGLSETSPVATANRLDTDD 389
Cdd:PRK06334 271 EAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTECSPVITINTVNSPK 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499271215 390 FTGTIGIPLPSTEVEIRDEDGRT-LPVGEIGEICIRGPQVMAGYW-QRPEETARAISPDGFFRTGDVGFMNAEG 461
Cdd:PRK06334 351 HESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHG 424
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-564 |
5.04e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 82.14 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 52 PAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDA 131
Cdd:PRK05691 2205 PALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS 2284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 132 GAkaifvlenfahtveqvlartevkhVVVASMGDMLGAKGAIVNLVVRrvkklvpaWSIPGHLSfktVLA--KGATLgfk 209
Cdd:PRK05691 2285 GI------------------------GLLLSDRALFEALGELPAGVAR--------WCLEDDAA---ALAaySDAPL--- 2326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 rPNVA-PGDVAFLQYTGGTTGVSKGATLTHANLLSNMAqmelwlntAFLRK--PRPESltfmCALPLYHI-F-ALTVNSL 284
Cdd:PRK05691 2327 -PFLSlPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQ--------AVIERfgMRADD----CELHFYSInFdAASERLL 2393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 285 MGLATGGNNILIP----NPRDIPAFVKElgrYRTNIFpGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAV-----QRPV 355
Cdd:PRK05691 2394 VPLLCGARVVLRAqgqwGAEEICQLIRE---QQVSIL-GFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALtgehlQRIR 2469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWLELtgcpIHEGYGLSET--SPVAT--ANRLDTDDFTGTIGIPLPSTEVEIRDEDGRTLPVGEIGEICIRGPQVMAG 431
Cdd:PRK05691 2470 QAFAPQL----FFNAYGPTETvvMPLAClaPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 432 YWQRPEETARAISPDGF-------FRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVA 504
Cdd:PRK05691 2546 YHDRPGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALD 2625
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 505 DPhSGEAVKLFVVRKDPNLTEEE-------VKRHCAASLTNYKRPRYVEFRTELPKSNVGKILRKDL 564
Cdd:PRK05691 2626 TP-SGKQLAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
45-565 |
1.48e-15 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 79.94 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 45 VAQYsWRPAFTCMGKALTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPREL 124
Cdd:PLN02654 106 IAIY-WEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 125 EHQLVDAGAKAIFVlenfAHTVEQVLARTEVKHVVVASMgDMLGAKGAIVNLVV-----RRVKKLVPAWSIPGHLSFKTV 199
Cdd:PLN02654 185 AQRIVDCKPKVVIT----CNAVKRGPKTINLKDIVDAAL-DESAKNGVSVGICLtyenqLAMKREDTKWQEGRDVWWQDV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 200 LAKGATlGFKRPNVAPGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMelwLNTAFLRKPrpeSLTFMCALPLYHIFAL 279
Cdd:PLN02654 260 VPNYPT-KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATT---FKYAFDYKP---TDVYWCTADCGWITGH 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 280 TVNSLMGLATGGNNIL---IPNPRDIPAFVKELGRYRTNIFPGLNTLFNALMNNSEFRKLDFSSLILTFGGGMAVQ-RPV 355
Cdd:PLN02654 333 SYVTYGPMLNGATVLVfegAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGSVGEPiNPS 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 356 AERWL-ELTG---CPIHEGYGLSET-----SPVATANRLDTddftGTIGIPLPSTEVEIRDEDGRTLPvGEI-GEICIRG 425
Cdd:PLN02654 413 AWRWFfNVVGdsrCPISDTWWQTETggfmiTPLPGAWPQKP----GSATFPFFGVQPVIVDEKGKEIE-GECsGYLCVKK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 426 P-----QVMAGYWQRPEETARAISPdGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAA 500
Cdd:PLN02654 488 SwpgafRTLYGDHERYETTYFKPFA-GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAV 566
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499271215 501 IGVADPHSGEAVKLFVVRKDPNLTEEEVKRHCAASLTN----YKRPRYVEFRTELPKSNVGKILRKDLR 565
Cdd:PLN02654 567 VGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNqigaFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
61-565 |
1.85e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 70.11 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMP-NIlqNPVIVY-GILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFv 138
Cdd:PLN03052 209 MTLSELRSQVSRVANALDALGFEKGDAIAIDMPmNV--HAVIIYlAIILAGCVVVSIADSFAPSEIATRLKISKAKAIF- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 139 lenfahtVEQVLARTEVKH-----VVVA--SMGDMLGAKGAIVNLVVRRvkklvpawsipGHLSFKTVLAKGATLgfKRP 211
Cdd:PLN03052 286 -------TQDVIVRGGKSIplysrVVEAkaPKAIVLPADGKSVRVKLRE-----------GDMSWDDFLARANGL--RRP 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 212 N-----VAPGDvAF--LQYTGGTTGVSKGATLTHANLLSNMA----QMEL-------WlntaflrkprPESLTFMCALPL 273
Cdd:PLN03052 346 DeykavEQPVE-AFtnILFSSGTTGEPKAIPWTQLTPLRAAAdawaHLDIrkgdivcW----------PTNLGWMMGPWL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 274 yhIFALTVN-SLMGLATGGnniliPNPRDIPAFVKELGRYRTNIFPglnTLFNALMNNSEFRKLDFSSlILTFGG-GMAV 351
Cdd:PLN03052 415 --VYASLLNgATLALYNGS-----PLGRGFAKFVQDAKVTMLGTVP---SIVKTWKNTNCMAGLDWSS-IRCFGStGEAS 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 352 QrpvAERWLELTG----CPIHEGYGLSET-SPVATANRLDTDDFtGTIGIPLPSTEVEIRDEDGRTLP--VGEIGEICIr 424
Cdd:PLN03052 484 S---VDDYLWLMSragyKPIIEYCGGTELgGGFVTGSLLQPQAF-AAFSTPAMGCKLFILDDSGNPYPddAPCTGELAL- 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 425 GPQVMAG------------YWQ-RPEETARAISPDG--FFRTGDvGFMNAEGltkivdRKKDMILVSGFNVFPNEIEEVA 489
Cdd:PLN03052 559 FPLMFGAsstllnadhykvYFKgMPVFNGKILRRHGdiFERTSG-GYYRAHG------RADDTMNLGGIKVSSVEIERVC 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 490 -ATHPGILECAAIGVADPHSG-EAVKLFVVRKDP---NLTEEEVKRHCAASLTNYKRP----RYVEFRTELPKSNVGKIL 560
Cdd:PLN03052 632 nAADESVLETAAIGVPPPGGGpEQLVIAAVLKDPpgsNPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVM 711
|
....*
gi 499271215 561 RKDLR 565
Cdd:PLN03052 712 RRVLR 716
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
355-536 |
7.38e-12 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 67.48 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 355 VAERWleltGCPIHEGYGLSETSP-VA--TANR----LDTDDFTgtigiplpsteVEIRD-EDGRTLPVGEIGEICIrgp 426
Cdd:COG1541 223 IEERW----GIKAYDIYGLTEVGPgVAyeCEAQdglhIWEDHFL-----------VEIIDpETGEPVPEGEEGELVV--- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 427 qvmagywqrpeeTAraISPDGF----FRTGDVGFMNAE----GLT-----KIVDRKKDMILVSGFNVFPNEIEEVAATHP 493
Cdd:COG1541 285 ------------TT--LTKEAMplirYRTGDLTRLLPEpcpcGRThprigRILGRADDMLIIRGVNVFPSQIEEVLLRIP 350
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499271215 494 GILECAAIGVADPHSGEAVKLFVVRkDPNLTEEEVKRHCAASL 536
Cdd:COG1541 351 EVGPEYQIVVDREGGLDELTVRVEL-APGASLEALAEAIAAAL 392
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
370-565 |
3.27e-11 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 65.66 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 370 GYGLSETSPVATANRLDTddfTGTIGIPLPSTEVEIRDedgrtlpvgeiGEICIRGPQVMAGYWQRpeetaRAISP---- 445
Cdd:PRK09029 270 GYGLTEMASTVCAKRADG---LAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQ-----GQLVPlvnd 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 446 DGFFRTGDVGFMNAEGLTkIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVADPHSGE---AvklfVVRKDPN 522
Cdd:PRK09029 331 EGWFATRDRGEWQNGELT-ILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQrpvA----VVESDSE 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499271215 523 LTEEEVKRHCAASLTNYKRP-RYVEFRTELPKSNVgKILRKDLR 565
Cdd:PRK09029 406 AAVVNLAEWLQDKLARFQQPvAYYLLPPELKNGGI-KISRQALK 448
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
214-499 |
5.70e-11 |
|
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: 64.80 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 214 APGDVAFLQYTGGTTGVSKGATLTHANLLSNMAQMELWLNTAflrkprPESLTFMCALPLYHIFalTVNSLMGLATGGNN 293
Cdd:cd17654 116 TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT------SEDILFLTSPLTFDPS--VVEIFLSLSSGATL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 294 ILIPNP-RDIPA-FVKEL-GRYRTNIFPGLNTLFNALMNNSEFRKL--DFSSL-ILTFGGGMAVQRPVAERWL-ELTGCP 366
Cdd:cd17654 188 LIVPTSvKVLPSkLADILfKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLrVLALGGEPFPSLVILSSWRgKGNRTR 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 367 IHEGYGLSETSPVATANRLDTDDFTGTIGIPLPSTEVEIRDEDGRT----LPVGEIGEICIrgpqvMAGYWQRPEETARA 442
Cdd:cd17654 268 IFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEgtgqVFLGGLNRVCI-----LDDEVTVPKGTMRA 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 499271215 443 ispdgffrTGDVgFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECA 499
Cdd:cd17654 343 --------TGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA 390
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
210-454 |
1.29e-10 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 64.01 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 210 RPNVAPGD--VAFLQYTGGTTGVSKGATLTHANLlsnmaqMELWLNTAFLRKPRPESLTFMCALPLYHIFALtvNSLMG- 286
Cdd:cd17632 215 LFRPEPDDdpLALLIYTSGSTGTPKGAMYTERLV------ATFWLKVSSIQDIRPPASITLNFMPMSHIAGR--ISLYGt 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 287 LATGGNNILIPNPrDIPAFVKELGRYR-TNIF--PGLNTL----FNALMNNSEFRKLDFSSL-----------IL--TFG 346
Cdd:cd17632 287 LARGGTAYFAAAS-DMSTLFDDLALVRpTELFlvPRVCDMlfqrYQAELDRRSVAGADAETLaervkaelrerVLggRLL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 347 GGMAVQRPVAER---WLE-LTGCPIHEGYGLSETSPVAtanrLDtddftGTIGIPlPSTEVEIRD--EDG--RTLPVGEI 418
Cdd:cd17632 366 AAVCGSAPLSAEmkaFMEsLLDLDLHDGYGSTEAGAVI----LD-----GVIVRP-PVLDYKLVDvpELGyfRTDRPHPR 435
|
250 260 270
....*....|....*....|....*....|....*.
gi 499271215 419 GEICIRGPQVMAGYWQRPEETARAISPDGFFRTGDV 454
Cdd:cd17632 436 GELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
61-560 |
9.25e-07 |
|
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: 51.80 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNILQNPVIVYGILRAGFTVVNVNPLYTPRELEHQLVDAGAKAIFVLE 140
Cdd:TIGR01217 115 VTWAELRRQVASLAAALRALGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLFTVD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 141 NFAHTVEQVLARTEVKHvVVASMGDMlgAKGAIVNLVVRRVKKlvpAWSIPGHLSFKTVLA--KGATLGFKRpnVAPGDV 218
Cdd:TIGR01217 195 GYRYNGKEHDRRDKVAE-VRKELPTL--RAVVHIPYLGPRETE---APKIDGALDLEDFTAaaQAAELVFEQ--LPFDHP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 219 AFLQYTGGTTGVSKgaTLTHA---NLLSNMAQMELWLNTaflrkpRPESLTFmcalplyhiFALTVNSLM------GLAT 289
Cdd:TIGR01217 267 LWILFSSGTTGLPK--CIVHSaggTLVQHLKEHGLHCDL------GPGDRLF---------YYTTTGWMMwnwlvsGLAT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 290 GGNNILIPNPRDIP---AFVKELGRYRTNIFpGLNTLFNALMNNSEF---RKLDFSSL--ILTFGGGMavqRPVAERWLe 361
Cdd:TIGR01217 330 GATLVLYDGSPGFPatnVLWDIAERTGATLF-GTSAKYVMACRKAGVhpaRTHDLSALqcVASTGSPL---PPDGFRWV- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 362 ltgcpiHEGY-----------GLSETSPVATANRLdTDDFTGTIGIPLPSTEVEIRDEDGRTLpVGEIGE-ICIRG-PQV 428
Cdd:TIGR01217 405 ------YDEIkadvwlasisgGTDICSCFAGANPT-LPVHIGEIQAPGLGTAVQSWDPEGKPV-TGEVGElVCTNPmPSM 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 429 MAGYWQRPE----ETARAISPDGFFRTGDVGFMNAEGLTKIVDRKKDMILVSGFNVFPNEIEEVAATHPGILECAAIGVA 504
Cdd:TIGR01217 477 PIRFWNDPDgskyRDAYFDTYPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQE 556
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499271215 505 DPHSGEAVKLFV-----VRKDPNLTeEEVKRHCAASLTNYKRPRYVEFRTELPKSNVGKIL 560
Cdd:TIGR01217 557 QPDGGYRVVLFVhlapgATLDDALL-DRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRV 616
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
61-95 |
9.80e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 9.80e-05
10 20 30
....*....|....*....|....*....|....*
gi 499271215 61 LTFSDLNTHSAKIGAWLQSLGLAKGDRVAVMMPNI 95
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNI 149
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
450-565 |
4.69e-03 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 39.80 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499271215 450 RTGDV------GFMNAEGltkivdRKKDMILVSGFNVFPNEIEEVA-ATHPGILECAAIGVADPHSG-EAVKLFVVRKDP 521
Cdd:PLN03051 360 RHGDImkrtpgGYFCVQG------RADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGpELLVIFLVLGEE 433
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499271215 522 NLT-----EEEVKRHCAASLTNYKRPRY----VEFRTELPKSNVGKILRKDLR 565
Cdd:PLN03051 434 KKGfdqarPEALQKKFQEAIQTNLNPLFkvsrVKIVPELPRNASNKLLRRVLR 486
|
|
| |
