|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1-560 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 1240.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 1 MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALM 80
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAK 160
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 161 GTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 241 TYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQ 320
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 321 QLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVP 400
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 401 PGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGV 480
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 481 QEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKVDNK 560
Cdd:PRK08974 481 LEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1-552 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 897.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 1 MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALM 80
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQ-SRGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLStAK 160
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLG-FK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 161 GTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK07059 159 GHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 241 TYGPLL----HPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNN 316
Cdd:PRK07059 239 WLQPAFekkpRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 317 KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDD 396
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 397 NEVPPGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 476 QHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
5-560 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 814.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 5 WLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNL 84
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVV 164
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 165 NFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGP 244
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 245 LLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDF 324
Cdd:PRK05677 246 NLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 325 SSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQP 404
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 405 GELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEV 483
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQC 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 484 AAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKVDNK 560
Cdd:PRK05677 485 AAIGVPDEKSGEAIKVFVVvKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGLK 562
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-554 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 774.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 5 WLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNL 84
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVV 164
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 165 NFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN---AT 241
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHqwlAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 242 YGPLLhPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQ 321
Cdd:PRK08751 247 TGKLE-EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 322 LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPP 401
Cdd:PRK08751 326 IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 402 GQPGELCVKGPQVMLGYWQRPDATDEIIK-NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGV 480
Cdd:PRK08751 406 GEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 481 QEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PRK08751 486 LEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-550 |
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: 732.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 25 LVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NPLYTPRELEHQLNDSGASAIVIvsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdAI 184
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 185 SFRSALHNGYRMQYvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlHPGKELVVTALPLYHIFA 264
Cdd:cd05936 105 SFTDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDL-LEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 265 LTINCLLFIELGGQNLLITNPRDIpGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAER 344
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 345 WVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDA 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 425 TDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKK 504
Cdd:cd05936 342 TAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1728558706 505 D-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05936 422 EgASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
5-553 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 728.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 5 WLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNL 84
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVV 164
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 165 NFVVKYIKRLVPKYHLPDAISFRSALHNG--YRMQYVKPELvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQGrgLSLKPVPVGL--DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 243 G-------PLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLN 315
Cdd:PRK12492 244 SqlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 316 NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDD 395
Cdd:PRK12492 324 HPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 396 DNEVPPGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:PRK12492 404 GNELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 475 MQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK12492 484 MAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-554 |
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: 574.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 25 LVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NPLYTPRELEHQLNDSGASAIVIvsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdai 184
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 185 sfrsalhngyrmqyvkpelvpedlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVVTALPLYHIFA 264
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPG-DVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 265 LTINCLLFIELGGQNLLITNpRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAER 344
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 345 WVKLTGQYLLEGYGLTECAPLVSVNPYDIDY-HSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPD 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPGErRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 424 ATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVK 503
Cdd:COG0318 315 ATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 504 KD-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:COG0318 395 RPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-552 |
4.68e-173 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 501.84 E-value: 4.68e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 3 KVWLNRYPADVPTEINPDRyQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMP 82
Cdd:PRK05605 13 KPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 83 NLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGT 162
Cdd:PRK05605 91 NCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 163 VVNFVVKYIKRLVPKYH--LPDAISFRSALHN---GYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ 237
Cdd:PRK05605 171 ALRLPIPALRKARAALTgpAPGTVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 238 VNAtYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPrDIPGLVKELAKYPFTAITGVNTLFNALLNNK 317
Cdd:PRK05605 251 GKA-WVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 318 EFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDD- 396
Cdd:PRK05605 329 EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 397 -NEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK05605 409 dETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 476 QHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-552 |
2.00e-155 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 454.36 E-value: 2.00e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKT-AVQHVILTRMGDqlstakgtvvnfvvkyikrlvPKYHLP 181
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEE---------------------DDPHTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 182 DAISFRSALHNGYRmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhPGKELVVTALPLYH 261
Cdd:PRK07656 143 KMKTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADW-AEYLGL--TEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 262 IFALT---INCLLfielGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MP 336
Cdd:PRK07656 219 VFGYKagvNAPLM----RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 337 VQQVvaERWVKLTG-QYLLEGYGLTECAPLVSVNPYDID--YHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQ 413
Cdd:PRK07656 295 VALL--ERFESELGvDIVLTGYGLSEASGVTTFNRLDDDrkTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 414 VMLGYWQRPDATDEIIKN-GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGS 492
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDAdGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 493 SGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07656 453 LGEVGKAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-560 |
1.67e-148 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 438.70 E-value: 1.67e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 1 MKKVWLNRYPADVPTEINPDrYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALM 80
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTISYD-IQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAK 160
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 161 GTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN-LEQVN 239
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 240 ATYGplLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLItnPR-DIPGLVKELAKYPFTAITGVNTLFNALLNNKE 318
Cdd:PRK06710 241 WLYN--CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 319 FQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNE 398
Cdd:PRK06710 317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 399 V-PPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:PRK06710 397 AlPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 478 PGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK 556
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRK 556
|
....
gi 1728558706 557 VDNK 560
Cdd:PRK06710 557 NEDE 560
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-551 |
1.10e-146 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 432.30 E-value: 1.10e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 20 DRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 100 IVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDK-TAVQHVILtrMGDqlsTAKGTVVNFVVKYikrlvpky 178
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlPTVRTVIV--EGD---GPAAPLAPEVGEY-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 179 hlpdaisfrSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtyGPLLHPgKELVVTALP 258
Cdd:PRK06187 149 ---------EELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA--WLKLSR-DDVYLVIVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHIFALTInCLLFIELGGQNLLItnPRDIPGLVKEL-AKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPV 337
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVIP--RRFDPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYD-----IDYHSGSIGLPVPSTEAKLVDDDDNEVPP--GQPGELCVK 410
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEdqlpgQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 411 GPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPS 490
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 491 GSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK06187 454 EKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-546 |
1.61e-142 |
|
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: 418.55 E-value: 1.61e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 29 FEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLY 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 109 TPRELEHQLNDSGASAIVivsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrs 188
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 189 alhngyrmqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGKELVVtALPLYHIFALTIN 268
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA--VNALAALDLGPDDVLLV-VAPLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 269 CLLFIELGGQNLLITNPRdiPGLVKEL-AKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWvK 347
Cdd:cd17631 158 TLPTLLRGGTVVILRKFD--PETVLDLiERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL-Q 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 LTGQYLLEGYGLTECAPLVSVN-PYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATD 426
Cdd:cd17631 235 ARGVKFVQGYGMTETSPGVTFLsPEDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 EIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP 506
Cdd:cd17631 315 AAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1728558706 507 S-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17631 395 AeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
29-461 |
7.05e-138 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 406.31 E-value: 7.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 29 FEQSVARYADQPAFVNM-GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDSGASAIVIVSNFahTLEKVVDKT-AVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHLPDaisf 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALgKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 rsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVV-TALPLYHIFAL 265
Cdd:pfam00501 154 ------------------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVlSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 266 TINCLLFIELGGQNLLI--TNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAE 343
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 344 RWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHS--GSIGLPVPSTEAKLVDDDD-NEVPPGQPGELCVKGPQVMLGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRslGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1728558706 421 RPDATDE-IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS 461
Cdd:pfam00501 376 DPELTAEaFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-556 |
2.22e-136 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 407.04 E-value: 2.22e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVN 103
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 104 VNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKG-TVVNFVVKyiKRLVPKYHLPD 182
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEiAVPAWLRA--EPPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISFRSALHNGYRmqyvKPELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPgkELVVTA-LPL 259
Cdd:PRK08314 169 VVAWKEALAAGLA----PPPHTagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTP--ESVVLAvLPL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 260 YHIFALtINCLLF-IELGGQNLLITN-PRDIPGLVkeLAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPV 337
Cdd:PRK08314 241 FHVTGM-VHSMNApIYAGATVVLMPRwDREAAARL--IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDDD-NEVPPGQPGELCVKGPQVML 416
Cdd:PRK08314 318 PEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD-RPKLQCLGIPTFGVDARVIDPETlEELPPGEVGEIVVHGPQVFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 417 GYWQRPDATDE--IIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGS 492
Cdd:PRK08314 397 GYWNRPEATAEafIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPR 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 493 SGEAVKIFVVKKDPS---LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK 556
Cdd:PRK08314 477 RGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-545 |
5.41e-135 |
|
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: 401.21 E-value: 5.41e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASaI 125
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK-V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNfaHTLEKVVDKTA----VQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYhlpdaisfrsalhngyrmqyvkP 201
Cdd:cd05911 86 IFTDP--DGLEKVKEAAKelgpKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPP----------------------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVVTALPLYHIFAL--TINCLLFielgGQN 279
Cdd:cd05911 142 KDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGS-NDVILGFLPLYHIYGLftTLASLLN----GAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 280 LLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ-YLLEGYG 358
Cdd:cd05911 217 VIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 359 LTECAPLVSVNPyDIDYHSGSIGLPVPSTEAKLVDDDDNE-VPPGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHT 436
Cdd:cd05911 297 MTETGGILTVNP-DGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 437 GDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEESLVT 515
Cdd:cd05911 376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTEKEVKD 455
|
490 500 510
....*....|....*....|....*....|...
gi 1728558706 516 FCRRQLTGYKvpKL---VEFRDELPKSNVGKIL 545
Cdd:cd05911 456 YVAKKVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
14-552 |
1.00e-125 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 378.89 E-value: 1.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 14 PTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTvvnfvvkyikr 173
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGW----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 174 lvpkyhlpdaISFRSALHNGYRMQyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvnatYGPLLHPGK--- 250
Cdd:PRK08316 150 ----------LDFADWAEAGSVAE-PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAE-------YVSCIVAGDmsa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 251 -ELVVTALPLYHIFALTINCLLFIELGGQNLLITNPrDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHL 329
Cdd:PRK08316 212 dDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 330 SAGGG--MPVQqVVAERWVKLTGQYLLEGYGLTECAPLVSV-NPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGE 406
Cdd:PRK08316 291 GYYGAsiMPVE-VLKELRERLPGLRFYNCYGQTEIAPLATVlGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 407 LCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAV 486
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 487 GVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK08316 450 GLPDPKWIEAVTAVVVpKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-545 |
6.10e-119 |
|
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: 354.67 E-value: 6.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVVTALPLYHIFAltINCLLFIELGGQNLLITNPR 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL---TEGDVFLSTLPLFHIGG--LFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLV 366
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 367 SVN-PYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEE 445
Cdd:cd04433 156 ATGpPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 446 GFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGY 524
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 1728558706 525 KVPKLVEFRDELPKSNVGKIL 545
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-553 |
4.71e-114 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 350.50 E-value: 4.71e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 5 WLNRYPADVPTEIN-PDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPN 83
Cdd:PRK06178 14 QQAAWPAGIPREPEyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ-RGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 84 LLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTV 163
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 164 VNFVVKyikrlVPKYHLPDAISFRSALHN-GYRMQYVKPELvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATY 242
Cdd:PRK06178 173 LPDSLR-----APRLAAAGAIDLLPALRAcTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMVYTA----AAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 243 GPLLHPGKELVVTA--LPLYHIfALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQ 320
Cdd:PRK06178 242 YAVAVVGGEDSVFLsfLPEFWI-AGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 321 QLDFSSLhlsagggmpvQQVVA------------ERWVKLTGQYLLEG-YGLTE---CAPLVS-VNPYDIDYHSGSI--G 381
Cdd:PRK06178 321 EYDLSSL----------RQVRVvsfvkklnpdyrQRWRALTGSVLAEAaWGMTEthtCDTFTAgFQDDDFDLLSQPVfvG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 382 LPVPSTEAKLVDDDDNE-VPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILV 460
Cdd:PRK06178 391 LPVPGTEFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 461 SGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKlVEFRDELPKS 539
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMT 549
|
570
....*....|....
gi 1728558706 540 NVGKILRRELRDEA 553
Cdd:PRK06178 550 ATGKVRKQDLQALA 563
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-549 |
1.69e-113 |
|
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: 346.91 E-value: 1.69e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTP 110
Cdd:cd05904 15 ASAHPSRPALIDaaTGRALTYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 111 RELEHQLNDSGASAIVIVSNfahTLEKVvdKTAVQHVILtrMGDQLStakgtvvnfvvkyikrlvpkyhlpDAISFRSAL 190
Cdd:cd05904 94 AEIAKQVKDSGAKLAFTTAE---LAEKL--ASLALPVVL--LDSAEF------------------------DSLSFSDLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 191 HNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVVTALPLYHIFALTINCL 270
Cdd:cd05904 143 FEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE-DVFLCVLPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 271 LFIELGGQnLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLH-LSAGG---GMPVQQVVAER-- 344
Cdd:cd05904 222 GLLRLGAT-VVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRqIMSGAaplGKELIEAFRAKfp 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 345 WVKLtgqylLEGYGLTECAPLVSVNPYDI--DYHSGSIGLPVPSTEAKLVDDDDNEV-PPGQPGELCVKGPQVMLGYWQR 421
Cdd:cd05904 301 NVDL-----GQGYGMTESTGVVAMCFAPEkdRAKYGSVGRLVPNVEAKIVDPETGESlPPNQTGELWIRGPSIMKGYLNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 422 PDATDE-IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIF 500
Cdd:cd05904 376 PEATAAtIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAF 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1728558706 501 VVKK-DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05904 456 VVRKpGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
24-550 |
2.42e-108 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 334.62 E-value: 2.42e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERS-RAFAAYLQQGLGlkKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:TIGR03205 22 TLPDLLSKAAADYGPRPALEFRDRPITYTELEAMAeTAAAALLRAGYG--KDASVALYLGNTPDHPINFFGALKAGARVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASaIVIVSNFAHTL---EKVVDKTAVQHVILTRmgDQLSTAKGTvvnfvvkyikrlvPKYH 179
Cdd:TIGR03205 100 HLSPLDGERALSHKLSDSGAR-LLITSDLAALLpmaLKFLEKGLLDRLIVCE--DDNWGKVGT-------------PQAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 180 LPD---AISFRSALHNGYR-MQYvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-------QVNATYGpllhp 248
Cdd:TIGR03205 164 IPAdprIVTYADFVKGAAApAEW--PAVTPDDVALLQYTGGTTGLPKGAMLTHGNLTSAVSiydvwgkPSRATRG----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 249 GKELVVTALPLYHIFALTIncLLFIELGGQNLLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSL 327
Cdd:TIGR03205 237 DVERVICVLPLFHIYALTV--ILLRSLRRGDLISLHQRfDVAAVFRDIEEKRATVFPGVPTMWIALANDPSLEKRDLSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 328 HLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE-CAPLVSVNPYDIDyHSGSIGLPVPSTEAKLV--DDDDNEVPPGQP 404
Cdd:TIGR03205 315 ATIGSGGAPLPVEVANFFERKTGLKLKSGWGMTEtCSPGTGHPPEGPD-KPGSIGLMLPGIELDVVslDDPTKVLPPGEV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 405 GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVA 484
Cdd:TIGR03205 394 GELRIRGPNVTRGYWNRPEESAEAFVGDRFLTGDIGYMDTDGYFFLVDRKKDMIISGGFNVYPQMIEQAIYEHPGVQEVI 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 485 AVGVPSGSSGEAVKIFVVKKDPS--LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:TIGR03205 474 VIGIPDQYRGEAAKAFVKLRPGAkpFSLDELRAFLAGKLGKHELPVAVEFVDELPRTPVGKLSRHELR 541
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-553 |
3.16e-107 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 332.55 E-value: 3.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPA--FVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPN-----LLQYPVAlfgilRAGM 99
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNvpewvLTQFATA-----KIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 100 IVVNVNPLYTPRELEHQLNDSGASAIVIVSNFahtlekvvdKTAVQHVILTRMGDQLSTAK-GTVVNFVVKYIKRLV--- 175
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAADGF---------KDSDYVAMLYELAPELATCEpGQLQSARLPELRRVIflg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 176 -PKYhlPDAISFRSALHNG-----YRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPG 249
Cdd:PRK08315 165 dEKH--PGMLNFDELLALGravddAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMK--LTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 250 KELVVTaLPLYHIFAL---TINCLLFielgGQNLLITNPRDIPGLV-KELAKYPFTAITGVNTLFNALLNNKEFQQLDFS 325
Cdd:PRK08315 241 DRLCIP-VPLYHCFGMvlgNLACVTH----GATMVYPGEGFDPLATlAAVEEERCTALYGVPTMFIAELDHPDFARFDLS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 326 SLH--LSAGGGMPV---QQVVAErwvkltgQYLLE---GYGLTECAPlVS----VNPyDIDYHSGSIGLPVPSTEAKLVD 393
Cdd:PRK08315 316 SLRtgIMAGSPCPIevmKRVIDK-------MHMSEvtiAYGMTETSP-VStqtrTDD-PLEKRVTTVGRALPHLEVKIVD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 394 DDDNE-VPPGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIE 471
Cdd:PRK08315 387 PETGEtVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 472 DVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK08315 467 EFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMR 546
|
...
gi 1728558706 551 DEA 553
Cdd:PRK08315 547 EMM 549
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-549 |
7.06e-106 |
|
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: 324.82 E-value: 7.06e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIV 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpELvpEDL 208
Cdd:cd05935 81 S------------------------------------------------------------------------EL--DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVVTALPLYHIFALTINCLLFIELGGQNLLITNpRDI 288
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG--LTPS-DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-WDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 289 PGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSV 368
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 369 NPYdIDYHSGSIGLPVPSTEAKLVD-DDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE--IIKNG--WLHTGDIAVMD 443
Cdd:cd05935 243 NPP-LRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfIEIKGrrFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP---SLTEESLVTFCRRQ 520
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....*....
gi 1728558706 521 LTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-556 |
1.45e-105 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 328.22 E-value: 1.45e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:COG0365 19 AEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVIltrmgDQLSTAKGTVVnfvvkyIKRLVPKYHLPDAISFR 187
Cdd:COG0365 98 FGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAL-----EELPSLEHVIV------VGRTGADVPMEGDLDWD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 188 SALhnGYRMQYVKPELVP-EDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPL---LHPGkELVVTALPLYHIF 263
Cdd:COG0365 167 ELL--AAASAEFEPEPTDaDDPLFILYTSGTTGKPKGVVHTHGGYLVHA----ATTAKYvldLKPG-DVFWCTADIGWAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 264 ALTiNCLLFIELGGQNLLI----TNPRDIPGLVKELAKYPFTAITGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMPV 337
Cdd:COG0365 240 GHS-YIVYGPLLNGATVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVVAERWVKLTGQYLLEGYGLTE-CAPLVSvNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQ--V 414
Cdd:COG0365 319 NPEVWEWWYEAVGVPIVDGWGQTEtGGIFIS-NLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDATDEIIKN---GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSG 491
Cdd:COG0365 398 FRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 492 SSGEAVKIFVVKK-----DPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK 556
Cdd:COG0365 478 IRGQVVKAFVVLKpgvepSDELAKE-LQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-554 |
4.31e-103 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 319.88 E-value: 4.31e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKgtvvnfvvkyIKRLVPKyhlpdaisfrsalhngyrmq 197
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRK----------IDNFVEK-------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQ-YTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLHpGKELVVTALPLYHIFAltINCLLFIEL- 275
Cdd:PRK06839 147 -------NESASFIIcYTSGTTGKPKGAVLTQENMFWN--ALNNTFAIDLT-MHDRSIVLLPLFHIGG--IGLFAFPTLf 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 276 GGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGG----MPVQQVVAERwvkltGQ 351
Cdd:PRK06839 215 AGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTECAPLV-SVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIK 430
Cdd:PRK06839 290 LFGQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 431 NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-PSLT 509
Cdd:PRK06839 370 DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSsSVLI 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1728558706 510 EESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PRK06839 450 EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
19-553 |
3.59e-100 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 314.02 E-value: 3.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 19 PDRYQSLVDMFEQSVARYADQPAFV--NMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 97 AGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFahtleKVVDKTAVQHVILTRMGD----QLSTAKGTVVNFVVKYIK 172
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAF-----KTSDYHAMLQELLPGLAEgqpgALACERLPELRGVVSLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 173 RLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKEL 252
Cdd:PRK12583 168 APPPGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTEHDRL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 253 VVtALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:PRK12583 246 CV-PVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 333 GGMPVQQVVAERWVK-LTGQYLLEGYGLTECAPLV--SVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCV 409
Cdd:PRK12583 325 AGAPCPIEVMRRVMDeMHMAEVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 410 KGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PRK12583 405 RGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGV 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 489 PSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK12583 485 PDEKYGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-550 |
4.09e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 312.69 E-value: 4.09e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEER-SRAFAAYlqQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVN 105
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRiSRYIQAF--EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 106 PLYTPRELEHQLNDSGASAIVivsnfahtlekvVDKTAVQhvilTRMGDQLSTAKGtvvnfvvkyIKRLVPKYHLPDAIS 185
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLI------------VDPAPFV----ERALALLARVPS---------LKHVLTLGPVPDGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 186 FrSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVVTalPLYHIFAL 265
Cdd:PRK06188 149 L-LAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP-RFLMCT--PLSHAGGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 266 TINCLLfieLGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW 345
Cdd:PRK06188 225 FFLPTL---LRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 346 VKLTGQYLLEGYGLTECAPLVSV-----NPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQ 420
Cdd:PRK06188 302 IERFGPIFAQYYGQTEAPMVITYlrkrdHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 421 RPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIF 500
Cdd:PRK06188 382 RPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 501 VV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK06188 462 VVlRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-551 |
2.11e-97 |
|
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: 305.01 E-value: 2.11e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 37 ADQPAFV--NMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELE 114
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 115 HQLNDSGASaivivsnfahtlekvvdktavqhVILTRMGDQLSTAKGTVVnfVVKYIKRL---VPKYHLPDAISFRSALH 191
Cdd:cd05926 80 FYLADLGSK-----------------------LVLTPKGELGPASRAASK--LGLAILELaldVGVLIRAPSAESLSNLL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 192 NGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTaLPLYHIFALtINCLL 271
Cdd:cd05926 135 ADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK--LTPDDRTLVV-MPLFHVHGL-VASLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELGGQNLLITnPRDIPGLV-KELAKYPFTAITGVNTLFNALLNN------KEFQQLDF---SSLHLSAgggmpvqqVV 341
Cdd:cd05926 211 STLAAGGSVVLP-PRFSASTFwPDVRDYNATWYTAVPTIHQILLNRpepnpeSPPPKLRFirsCSASLPP--------AV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 342 AERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHS-GSIGLPVpSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQ 420
Cdd:cd05926 282 LEALEATFGAPVLEAYGMTEAAHQMTSNPLPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 421 RPDATDEI-IKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKI 499
Cdd:cd05926 361 NPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1728558706 500 FVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05926 441 AVVlREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-550 |
7.94e-96 |
|
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: 298.44 E-value: 7.94e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIvs 129
Cdd:cd05934 5 TYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 nfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvpeDLA 209
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLaNLEQVNATYGPLlhPGKELVVTALPLYHIFALTINCLLFIELGGQNLLItnPRDIP 289
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLT-FAGYYSARRFGL--GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 290 -GLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVA--ERWvkltGQYLLEGYGLTEcAPLV 366
Cdd:cd05934 160 sRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEfeERF----GVRLLEGYGMTE-TIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 367 SVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVK---GPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMD 443
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEESLVTFCRRQLT 522
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGeTLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 1728558706 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
20-550 |
9.71e-94 |
|
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: 295.82 E-value: 9.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 20 DRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:cd05959 1 EKYNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 100 IVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKgtvvnfvVKYIKRLVPKyH 179
Cdd:cd05959 80 VPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAA-E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 180 LPDAISfrSALHngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLHPGKELVV-TAL 257
Cdd:cd05959 152 AEQLKP--AATH-------------ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAE----LYArNVLGIREDDVCfSAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 258 PLYHIFALTiNCLLF-IELGGQNLLITNpRDIPGLV-KELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHL--SAGG 333
Cdd:cd05959 213 KLFFAYGLG-NSLTFpLSVGATTVLMPE-RPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 334 GMPVQqvVAERWVKLTGQYLLEGYGLTECAPLVSVN-PYDIDYhsGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGP 412
Cdd:cd05959 291 ALPAE--VGERWKARFGLDILDGIGSTEMLHIFLSNrPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 413 QVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGS 492
Cdd:cd05959 367 SSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 493 SGEAVKIFVVKK----DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05959 447 GLTKPKAFVVLRpgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-487 |
9.84e-94 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 298.55 E-value: 9.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 19 PDRYQSLVDMFEQSVARYADQPAFVNMG----EVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGI 94
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 95 LRAGMIVVnvnPLY---TPRELEHQLNDSGASaIVIVSNFAH--TLEKVVDKT-AVQHVILTRMGDQLSTAKgtvvnfvV 168
Cdd:COG1022 86 LAAGAVTV---PIYptsSAEEVAYILNDSGAK-VLFVEDQEQldKLLEVRDELpSLRHIVVLDPRGLRDDPR-------L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 169 KYIKRLVP---KYHLPDAISFRSAlhngyrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpl 245
Cdd:COG1022 155 LSLDELLAlgrEVADPAELEARRA------------AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 246 LHPGkELVVTALPLYHIFALTInCLLFIELGGQnllITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNN--------K 317
Cdd:COG1022 221 LGPG-DRTLSFLPLAHVFERTV-SYYALAAGAT---VAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqakaeeaG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 318 EFQQLDFS---------SLHLSAGGGMP----VQQVVAERWV--KL---------------------TGQY-------LL 354
Cdd:COG1022 296 GLKRKLFRwalavgrryARARLAGKSPSlllrLKHALADKLVfsKLrealggrlrfavsggaalgpeLARFfralgipVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 355 EGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDddnevppgqpGELCVKGPQVMLGYWQRPDATDE-IIKNGW 433
Cdd:COG1022 376 EGYGLTETSPVITVNRPG-DNRIGTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEaFDADGW 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1728558706 434 LHTGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:COG1022 445 LHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
23-554 |
9.84e-94 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 299.56 E-value: 9.84e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPA--FV------NMGEVMTFRKLEER-SRAfaAYLQQGLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPAlsFLldadplDRPETWTYAELLADvTRT--ANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGmIVVNVNPLYTPRELEHQLNDSGASAIVIVSNF-----AHTLEKVVDK-TAVQHVILTRMGDQLSTAKGTVVNFv 167
Cdd:PRK07529 103 GEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAAlPELRTVVEVDLARYLPGPKRLAVPL- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 168 vkyikrLVPKYHLPDaISFRSALHNGYRMQYVKPELV-PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplL 246
Cdd:PRK07529 181 ------IRRKAHARI-LDFDAELARQPGDRLFSGRPIgPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLG--L 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 247 HPGKeLVVTALPLYHIFALTINCLLFIeLGGQNLLITNP---RDiPGLVKEL----AKYPFTAITGVNTLFNALLnnkef 319
Cdd:PRK07529 252 GPGD-TVFCGLPLFHVNALLVTGLAPL-ARGAHVVLATPqgyRG-PGVIANFwkivERYRINFLSGVPTVYAALL----- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 320 QQ----LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDD 395
Cdd:PRK07529 324 QVpvdgHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVILD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 396 DN-----EVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
Cdd:PRK07529 404 DAgrylrDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 471 EDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEESLVTFCRRQLTG-YKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:PRK07529 484 EEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPA 563
|
....*..
gi 1728558706 549 LR-DEAR 554
Cdd:PRK07529 564 LRrDAIR 570
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-551 |
2.30e-90 |
|
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: 284.95 E-value: 2.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVivsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvpeDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-VNA-TYGP---LLHpgkelvvtALPLYHIFAL--TINCL 270
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVRAlVDAwRWTEddvLLH--------VLPLHHVHGLvnALLCP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 271 LFIelggQNLLITNPRDIPGLVKEL-AKYPFTAITGVNTLFNALL--NNKEFQQLDFSS--------LHLSAGGGMPVQq 339
Cdd:cd05941 153 LFA----GASVEFLPKFDPKEVAISrLMPSITVFMGVPTIYTRLLqyYEAHFTDPQFARaaaaerlrLMVSGSAALPVP- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 340 vVAERWVKLTGQYLLEGYGLTECAPLVSvNPYDIDYHSGSIGLPVPSTEAKLVDDDDNE-VPPGQPGELCVKGPQVMLGY 418
Cdd:cd05941 228 -TLEEWEAITGHTLLERYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 419 WQRPDAT-DEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEA 496
Cdd:cd05941 306 WNKPEATkEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 497 VKIFVVKKD--PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05941 386 VVAVVVLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-551 |
4.16e-90 |
|
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: 283.84 E-value: 4.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 nfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvpEDLA 209
Cdd:cd05972 81 ----------------------------------------------------------------------------EDPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGKELVVTALP--LYHIFALTINCLLfieLGGQNLLITNPR- 286
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDIHWNIADPgwAKGAWSSFFGPWL---LGATVFVYEGPRf 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 DIPGLVKELAKYPFTAITGVNTLFNaLLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLV 366
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 367 SVNPyDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVK--GPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDE 444
Cdd:cd05972 239 GNFP-DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-----PSLTEEsLVTFCRR 519
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepsEELAEE-LQGHVKK 396
|
490 500 510
....*....|....*....|....*....|..
gi 1728558706 520 QLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-550 |
5.37e-90 |
|
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: 280.70 E-value: 5.37e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygpLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITN 284
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGER---LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTG-QYLLEGYGLTECA 363
Cdd:cd05917 78 SFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 364 PLV--SVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPP-GQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDI 439
Cdd:cd05917 158 PVStqTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 440 AVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEESLVTFCR 518
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrLKEGAELTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 1728558706 519 RQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
16-550 |
4.04e-87 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 279.56 E-value: 4.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 16 EINPDRYQSLVDMFEQSVARYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:PLN02246 16 DIYIPNHLPLHDYCFERLSEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAhtlEKVVDKTAVQHVILTRMGDQlstakgtvvnfvvkyikr 173
Cdd:PLN02246 95 ASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYV---DKLKGLAEDDGVTVVTIDDP------------------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 174 lvpkyhlPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELV 253
Cdd:PLN02246 154 -------PEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 254 V-TALPLYHIFALtiNCLLFIEL-GGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSA 331
Cdd:PLN02246 227 IlCVLPMFHIYSL--NSVLLCGLrVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 332 GGGMPVQQVVaERWV--KLTGQYLLEGYGLTECAPLVSV------NPYDIDyhSGSIGLPVPSTEAKLVDDDDNE-VPPG 402
Cdd:PLN02246 305 SGAAPLGKEL-EDAFraKLPNAVLGQGYGMTEAGPVLAMclafakEPFPVK--SGSCGTVVRNAELKIVDPETGAsLPRN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 403 QPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQ 481
Cdd:PLN02246 382 QPGEICIRGPQIMKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 482 EVAAVGVPSGSSGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PLN02246 462 DAAVVPMKDEVAGEVPVAFVVRSNGSeITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-555 |
2.90e-83 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 268.28 E-value: 2.90e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMM----PNLLQYpvalFGILRAGMIVVNVNPLYTPRELEHQLNDSG 121
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 122 ASAIVIVSNFAHTLEKVVDKTAVQHViLTRMGDqlstAKGTvvnfvvkyikrlvpkyhLPDAISFRSALHngyrmqyvkp 201
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGAPHV-ETLDAD----GTGS-----------------LLEAAAAAPDDF---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 202 ELVP---EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG-----PLLHpgkelvvtALPLYHIFAL--TINCLL 271
Cdd:PRK07514 149 ETVPrgaDDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRftpddVLIH--------ALPIFHTHGLfvATNVAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIelGGQnlLITNPRDIPGLVkeLAKYP-FTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVqqvVAE---RWVK 347
Cdd:PRK07514 221 LA--GAS--MIFLPKFDPDAV--LALMPrATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPL---LAEthrEFQE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 LTGQYLLEGYGLTECAPLVSvNPYDIDYHSGSIGLPVPSTEAKLVDDDDN-EVPPGQPGELCVKGPQVMLGYWQRPDAT- 425
Cdd:PRK07514 292 RTGHAILERYGMTETNMNTS-NPYDGERRAGTVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTa 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 426 DEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KK 504
Cdd:PRK07514 371 EEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVpKP 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 505 DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARG 555
Cdd:PRK07514 451 GAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-550 |
7.22e-83 |
|
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: 265.48 E-value: 7.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 39 QPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLN 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALR-NLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 119 DSGASAIVIVSnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqy 198
Cdd:cd05919 80 DCEARLVVTSA--------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 199 vkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNML--ANLEQVNATYgplLHPGKELVVTAlPLYHIFALTiNCLLF-IEL 275
Cdd:cd05919 91 -------DDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAREALG---LTPGDRVFSSA-KMFFGYGLG-NSLWFpLAV 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 276 GGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLE 355
Cdd:cd05919 159 GASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILD 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 356 GYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLH 435
Cdd:cd05919 239 GIGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 436 TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLV- 514
Cdd:cd05919 318 TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLAr 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 1728558706 515 ---TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05919 398 dihRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-551 |
5.19e-80 |
|
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: 260.26 E-value: 5.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVDK-TAVQHVILTRMGDqlstakgtvvnfvvkyiKRLVPkyHLPDAISFRSALHNGyRMQYVKPELVPEDL 208
Cdd:cd12119 106 DFLPLLEAIAPRlPTVEHVVVMTDDA-----------------AMPEP--AGVGVLAYEELLAAE-SPEYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVVTALPLYHIFA--LTINCLLFielgGQNLLITNPR 286
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPVVPMFHVNAwgLPYAAAMV----GAKLVLPGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 DIPG-LVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTECAPL 365
Cdd:cd12119 241 LDPAsLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 366 VSVN---------PYDIDYH-SGSIGLPVPSTEAKLVDDDDNEVP--PGQPGELCVKGPQVMLGYWQRPDATDEIIKNGW 433
Cdd:cd12119 320 GTVArppsehsnlSEDEQLAlRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEALTEDGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 434 LHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE-AVKIFVVKKDPSLTEES 512
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErPLAVVVLKEGATVTAEE 479
|
490 500 510
....*....|....*....|....*....|....*....
gi 1728558706 513 LVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd12119 480 LLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-550 |
5.73e-79 |
|
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: 255.00 E-value: 5.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 48 VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVI 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 128 VSNFAHTlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvKPELVPED 207
Cdd:cd05903 80 PERFRQF-----------------------------------------------------------------DPAAMPDA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVVTALPLYHIFALTINCLLFIELGGQNLL--ITNP 285
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG---LGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdIWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 286 RDIPGLVKElakypftaiTGVNTLFNA------LLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGL 359
Cdd:cd05903 172 DKALALMRE---------HGVTFMMGAtpfltdLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGS 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 360 TECA-PLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGD 438
Cdd:cd05903 243 TECPgAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEESLVTFC 517
Cdd:cd05903 323 LARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVAYL 402
|
490 500 510
....*....|....*....|....*....|....
gi 1728558706 518 RRQ-LTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05903 403 DRQgVAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
21-558 |
6.91e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 257.66 E-value: 6.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 21 RYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:PRK07470 5 RVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 101 VVNVNPLYTPRELEHQLNDSGASAIVIVSNFAhtlekvvdktavQHVILTRmgdqlsTAKGTVVNFVVKYIKRLVPKYhl 180
Cdd:PRK07470 84 WVPTNFRQTPDEVAYLAEASGARAMICHADFP------------EHAAAVR------AASPDLTHVVAIGGARAGLDY-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 181 pDAISfrsALHNGYRmqyVKPELVP-EDLAFLQYTGGTTGVAKGAMLTHRNM-------LANLeqVNATygplLHPGKEL 252
Cdd:PRK07470 144 -EALV---ARHLGAR---VANAAVDhDDPCWFFFTSGTTGRPKAAVLTHGQMafvitnhLADL--MPGT----TEQDASL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 253 VVTalPLYHifALTINCLLFIELGGQNLLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSA 331
Cdd:PRK07470 211 VVA--PLSH--GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 332 GGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNP---YDID----YHSGSIGLPVPSTEAKLVDDDDNEVPPGQP 404
Cdd:PRK07470 287 YAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPpalHDAEdgpdARIGTCGFERTGMEVQIQDDEGRELPPGET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 405 GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVA 484
Cdd:PRK07470 367 GEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVA 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 485 AVGVPSGSSGE-AVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD--EARGKVD 558
Cdd:PRK07470 447 VLGVPDPVWGEvGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREelEERGLLD 523
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
8-554 |
1.04e-78 |
|
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: 257.38 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 8 RYPADVPteinpDRY--------QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVAL 79
Cdd:COG1021 7 PWPEEFA-----ARYreagywrgETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 80 MMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS--------NFAHTLEKVVDktAVQHVILTr 151
Cdd:COG1021 81 QLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVP--SLRHVLVV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 152 mGDQlstakgtvvnfvvkyikrlvpkyhlPDAISFrSALHNGyRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNM 231
Cdd:COG1021 158 -GDA-------------------------GEFTSL-DALLAA-PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 232 LANLEQVNATYGplLHPGKELVVtALPLYHIFALTINCLL-FIELGGQNLLITNPRdiPGLVKEL-AKYPFTAITGVNTL 309
Cdd:COG1021 210 LYSVRASAEICG--LDADTVYLA-ALPAAHNFPLSSPGVLgVLYAGGTVVLAPDPS--PDTAFPLiERERVTVTALVPPL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 310 FNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEcaPLVSVN----PYDIDYHSgsIGLPV- 384
Cdd:COG1021 285 ALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTrlddPEEVILTT--QGRPIs 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 385 PSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDA-----TDeiikNGWLHTGDIAVMDEEGFLRIVDRKKDMIL 459
Cdd:COG1021 361 PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHnarafTP----DGFYRTGDLVRRTPDGYLVVEGRAKDQIN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 460 VSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCR-RQLTGYKVPKLVEFRDELPK 538
Cdd:COG1021 437 RGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLReRGLAAFKLPDRLEFVDALPL 516
|
570
....*....|....*.
gi 1728558706 539 SNVGKILRRELRDEAR 554
Cdd:COG1021 517 TAVGKIDKKALRAALA 532
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-487 |
2.93e-77 |
|
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: 250.98 E-value: 2.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLY---TPRELEHQLNDSGASAI 125
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 vIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvP 205
Cdd:cd05907 82 -FVED--------------------------------------------------------------------------P 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPLLHPGK-ELVVTALPLYHIFALTINCLLFIELGGQnllITN 284
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNA----LALAERLPATEgDRHLSFLPLAHVFERRAGLYVPLLAGAR---IYF 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLVKELAKYPFTAITGVNTLFNALLNN-----------KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYL 353
Cdd:cd05907 160 ASSAETLLDDLSEVRPTVFLAVPRVWEKVYAAikvkavpglkrKLFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 354 LEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDddnevppgqpGELCVKGPQVMLGYWQRPDATDE-IIKNG 432
Cdd:cd05907 239 YEGYGLTETSAVVTLNPPG-DNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEaLDADG 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 433 WLHTGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-552 |
7.43e-77 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 251.03 E-value: 7.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQ-YPV--ALFGIlraGMIVVNVNPLYTPRELE 114
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEmILVihALQQL---GAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 115 HQLNDSGASAIVIVSNFAHTLekvvdktavqhviltrmgdqlstakgtVVNFVVKYikrlvpkyhlpdaisfrSALHNGy 194
Cdd:PRK03640 93 WQLDDAEVKCLITDDDFEAKL---------------------------IPGISVKF-----------------AELMNG- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 195 rmQYVKPELVPE----DLAFLQYTGGTTGVAKGAMLTHRNMLAnleqvnATYGPLLHPG---KELVVTALPLYHIFALTI 267
Cdd:PRK03640 128 --PKEEAEIQEEfdldEVATIMYTSGTTGKPKGVIQTYGNHWW------SAVGSALNLGlteDDCWLAAVPIFHISGLSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 nclLF--IELGGQNLLIT--NPRDIPGLVKElakYPFTAITGVNTLFNALLnnKEFQQLDFSSlHLSA---GGGmPVQQV 340
Cdd:PRK03640 200 ---LMrsVIYGMRVVLVEkfDAEKINKLLQT---GGVTIISVVSTMLQRLL--ERLGEGTYPS-SFRCmllGGG-PAPKP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 341 VAERwVKLTGQYLLEGYGLTE-CAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDdNEVPPGQPGELCVKGPQVMLGYW 419
Cdd:PRK03640 270 LLEQ-CKEKGIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 420 QRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGeAVKI 499
Cdd:PRK03640 348 NREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG-QVPV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1728558706 500 FVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK03640 427 AFVVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
14-559 |
2.44e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 251.24 E-value: 2.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 14 PTEINPDRYQSLVDMFEQSVARYA----DQPAFVNMGEVMTFRKLEERSRAFAAYL-QQGLGLkkGDRVALMMPNLLQYP 88
Cdd:PRK07786 4 LTLAQEQPYLARRQNWVNQLARHAlmqpDAPALRFLGNTTTWRELDDRVAALAGALsRRGVGF--GDRVLILMLNRTEFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 89 VALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTrMGDqlsTAKGTVVNFvv 168
Cdd:PRK07786 82 ESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVV-AGG---SSDDSVLGY-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 169 kyikrlvpkyhlPDAISFRSALHngyrmqyvKPELVPEDL-AFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLH 247
Cdd:PRK07786 156 ------------EDLLAEAGPAH--------APVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTG--QAMTCLRTNGAD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 248 PGKELVVTALPLYHIFALTiNCLLFIELGGQNLLI-TNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSS 326
Cdd:PRK07786 214 INSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 327 LHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSV-NPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPG 405
Cdd:PRK07786 293 RVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMlLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 406 ELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAA 485
Cdd:PRK07786 373 EIVYRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAV 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 486 VGVPSGSSGEaVKIFVVKKDPS---LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRdEARGKVDN 559
Cdd:PRK07786 453 IGRADEKWGE-VPVAVAAVRNDdaaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR-ERYGACVN 527
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-552 |
3.47e-76 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 251.21 E-value: 3.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAFV-NMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIvivsnFAHTLEKvvdKTAVQHVILTrMGDQLSTAKGTVVnfvvkyIKRLVPKYhlpD 182
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMF-----FAPTLFK---QTRPVDLILP-LQNQLPQLQQIVG------VDKLAPAT---S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISFRSALHNGYRMQYvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygpLLHPGKELVVTALPLYHI 262
Cdd:PRK06087 165 SLSLSQIIADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR---LNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 263 FALTINCLLFIELGGQNLL--ITNPRDIPGLvkeLAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQV 340
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLldIFTPDACLAL---LEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 341 VAERwVKLTGQYLLEGYGLTECAPLVSVNPYD-IDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYW 419
Cdd:PRK06087 318 VARE-CQQRGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 420 QRPDATDEIIKN-GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVK 498
Cdd:PRK06087 397 DEPELTARALDEeGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 499 IFVVKKDPSLT---EESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06087 477 AYVVLKAPHHSltlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-551 |
5.77e-76 |
|
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: 246.49 E-value: 5.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAivivs 129
Cdd:cd05912 3 TFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 nfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvpEDLA 209
Cdd:cd05912 77 ----------------------------------------------------------------------------DDIA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPgKELVVTALPLYHIFALTIncLLFIELGGQNLLITNPRDIP 289
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG--LTE-DDNWLCALPLFHISGLSI--LMRSVIYGMTVYLVDKFDAE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 290 GLVKELAKYPFTAITGVNTLFNALLnnKEFQQLDFSSLHLSAGGGMPVQQVVAERwVKLTGQYLLEGYGLTE-CAPLVSV 368
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTEtCSQIVTL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 369 NPYDIDYHSGSIGLPVPSTEAKLVDDDdneVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFL 448
Cdd:cd05912 233 SPEDALNKIGSAGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 449 RIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPsLTEESLVTFCRRQLTGYKVPK 528
Cdd:cd05912 310 YVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYKVPK 388
|
490 500
....*....|....*....|...
gi 1728558706 529 LVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05912 389 KIYFVDELPRTASGKLLRHELKQ 411
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-550 |
1.00e-74 |
|
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: 244.31 E-value: 1.00e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 39 QPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEhqln 118
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 119 dsgasaivivsnfahtleKVVDKTAVQHVILTrmgDQLSTAkgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqy 198
Cdd:cd05958 77 ------------------YILDKARITVALCA---HALTAS--------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 199 vkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYGP-LLHPG-KELVVTALPLYHIFALTINCLLFIELG 276
Cdd:cd05958 97 -------DDICILAFTSGTTGAPKATMHFHRDPLASAD----RYAVnVLRLReDDRFVGSPPLAFTFGLGGVLLFPFGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLI--TNPRDIPGLVkelAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHL--SAGGGMPVQqvVAERWVKLTGQY 352
Cdd:cd05958 166 ASGVLLeeATPDLLLSAI---ARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKcvSAGEALPAA--LHRAWKEATGIP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 LLEGYGLTECAPL-VSVNPYDIdyHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQvmlGYWQRPDATDE-IIK 430
Cdd:cd05958 241 IIDGIGSTEMFHIfISARPGDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRtYVQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 431 NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKK-----D 505
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1728558706 506 PSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05958 396 PVLARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
35-551 |
1.33e-74 |
|
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: 246.67 E-value: 1.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 35 RYADQP---AFVN--MGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYT 109
Cdd:cd17642 26 RYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 110 PRELEHQLNDSGASaIVIVSNfaHTLEKVVDktavqhviltrmgdqlstakgtvVNFVVKYIKRLV---PKYHLPDAISF 186
Cdd:cd17642 105 ERELDHSLNISKPT-IVFCSK--KGLQKVLN-----------------------VQKKLKIIKTIIildSKEDYKGYQCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 ----RSALHNGYRMQYVKPELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QVNATYGPLLHPGKElVVTALPL 259
Cdd:cd17642 159 ytfiTQNLPPGFNEYDFKPPSFdrDEQVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIFGNQIIPDTA-ILTVIPF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 260 YHIFALTINCLLFIelGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMP--- 336
Cdd:cd17642 238 HHGFGMFTTLGYLI--CGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPlsk 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 337 -VQQVVAERwVKLTGqyLLEGYGLTECAPLVSVNPyDIDYHSGSIGLPVPSTEAKLVDDDDNE-VPPGQPGELCVKGPQV 414
Cdd:cd17642 316 eVGEAVAKR-FKLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDLDTGKtLGPNERGELCVKGPMI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSS 493
Cdd:cd17642 392 MKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 494 GEAVKIFVVKK-DPSLTEESLVTFCRRQLTGYKvpKL---VEFRDELPKSNVGKILRRELRD 551
Cdd:cd17642 472 GELPAAVVVLEaGKTMTEKEVMDYVASQVSTAK--RLrggVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-551 |
2.35e-74 |
|
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: 243.11 E-value: 2.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 47 EVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIV 126
Cdd:cd05971 5 EKVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 127 IvsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpDAisfrsalhngyrmqyvkpelvPE 206
Cdd:cd05971 84 T------------------------------------------------------DG---------------------SD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVVTALPLYHIFALtINCLLFIELGGQNLLITNPR 286
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFN-LFPRDGDLYWTPADWAWIGGL-LDVLLPSLYFGVPVLAHRMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 --DIPGLVKELAKYpftaitGVNTLF---NAL-LNNKEFQQLDFSSLHLSA---GGGMPVQQVVAerWVKLT-GQYLLEG 356
Cdd:cd05971 167 kfDPKAALDLMSRY------GVTTAFlppTALkMMRQQGEQLKHAQVKLRAiatGGESLGEELLG--WAREQfGVEVNEF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 357 YGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQ--VMLGYWQRPDATDEIIKNGWL 434
Cdd:cd05971 239 YGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 435 HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLV 514
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1728558706 515 ----TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05971 399 reiqELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
213-546 |
3.87e-74 |
|
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: 239.09 E-value: 3.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 213 YTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKeLVVTALPLYHIFALTINcLLFIELGGQNLLITNpRDIPGLV 292
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTEAD-VYLNMLPLFHIAGLNLA-LATFHAGGANVVMEK-FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 293 KELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVqqvVAERWVKLTGQYLLEGYGLTECAPLVSVNPYD 372
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPE---TIQRFEETTGATFWSLYGQTETSGLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 373 idYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVD 452
Cdd:cd17637 159 --ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 453 RK--KDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVK-IFVVKKDPSLTEESLVTFCRRQLTGYKVPKL 529
Cdd:cd17637 237 RKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKKPRY 316
|
330
....*....|....*..
gi 1728558706 530 VEFRDELPKSNVGKILR 546
Cdd:cd17637 317 VVFVEALPKTADGSIDR 333
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-551 |
5.71e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 244.04 E-value: 5.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEKVVDktavqhviLTRMGDQLSTAKGTVVNFVVKYIKRL--VPKYHLPDaisfRSAlhnGYRMQYvkpel 203
Cdd:PRK08276 88 IVSAALADTAAELAA--------ELPAGVPLLLVVAGPVPGFRSYEEALaaQPDTPIAD----ETA---GADMLY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 vpedlaflqyTGGTTGVAKGAM--LTHRNMLANLEQ--VNATYGPLLHPGKELVVTAlPLYHIfALTINCLLFIELGGqn 279
Cdd:PRK08276 148 ----------SSGTTGRPKGIKrpLPGLDPDEAPGMmlALLGFGMYGGPDSVYLSPA-PLYHT-APLRFGMSALALGG-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 280 LLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLNNKEF--QQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEG 356
Cdd:PRK08276 214 TVVVMEKfDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 357 YGLTECAPLVSVNPYDIDYHSGSIGLPVPStEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEI-IKNGWLH 435
Cdd:PRK08276 294 YASSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAArNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 436 TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV-----VKKDPSLTE 510
Cdd:PRK08276 373 VGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadgADAGDALAA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1728558706 511 EsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK08276 453 E-LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
32-551 |
2.95e-73 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 243.60 E-value: 2.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 32 SVARYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYT 109
Cdd:PLN02574 48 SHHNHNGDTALIDssTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 110 PRELEHQLNDSGASaivivsnFAHTLEKVVDKtavqhviLTRMGdqlstakgtvvnfvvkyikrlVPKYHLPDAISF--- 186
Cdd:PLN02574 128 LGEIKKRVVDCSVG-------LAFTSPENVEK-------LSPLG---------------------VPVIGVPENYDFdsk 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 RSALHNGYRMQYVKPELVP------EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-VNATYGPLLHPGKELV-VTALP 258
Cdd:PLN02574 173 RIEFPKFYELIKEDFDFVPkpvikqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfVRFEASQYEYPGSDNVyLAALP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHIFALTINCLLFIELGgQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNN-KEFQQLDFSSLHLSAGGGMPV 337
Cdd:PLN02574 253 MFHIYGLSLFVVGLLSLG-STIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKaKGVCGEVLKSLKQVSCGAAPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVVAERWVK-LTGQYLLEGYGLTECAPLVS--VNPYDIDYHSgSIGLPVPSTEAKLVD-DDDNEVPPGQPGELCVKGPQ 413
Cdd:PLN02574 332 SGKFIQDFVQtLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYS-SVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 414 VMLGYWQRPDATD-EIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGS 492
Cdd:PLN02574 411 VMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKE 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 493 SGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PLN02574 491 CGEIPVAFVVRRQGStLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-552 |
4.72e-73 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 242.96 E-value: 4.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 4 VWLNRYPAdVPTeinPDRYqSLVDMFEQSVARYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMM 81
Cdd:PLN02330 14 IFRSRYPS-VPV---PDKL-TLPDFVLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 82 PNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASaiVIVSNFAHtLEKVvdktavqhviltrmgdqlstaKG 161
Cdd:PLN02330 88 PNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAK--LIVTNDTN-YGKV---------------------KG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 162 TVVNFVVkyikrlVPKYHLPDAISFRSALHNGYRM--QYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN 239
Cdd:PLN02330 144 LGLPVIV------LGEEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 240 ATYGPLLhPGKELVVTALPLYHIFALTINCLLFIELGGQnLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEF 319
Cdd:PLN02330 218 FSVGPEM-IGQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 320 QQLDFSSLHLSA--GGGMPVQ-QVVAERWVKLTGQYLLEGYGLTE--CAPLVSVNPydiDYHSG-----SIGLPVPSTEA 389
Cdd:PLN02330 296 EEFDLSKLKLQAimTAAAPLApELLTAFEAKFPGVQVQEAYGLTEhsCITLTHGDP---EKGHGiakknSVGFILPNLEV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 390 KLVDDDDNE-VPPGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
Cdd:PLN02330 373 KFIDPDTGRsLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAP 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 468 NEIEDVVMQHPGVQEVAAVGVPSGSSGE-AVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:PLN02330 453 AELEAILLTHPSVEDAAVVPLPDEEAGEiPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR 532
|
....*.
gi 1728558706 547 RELRDE 552
Cdd:PLN02330 533 RLLKEK 538
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-550 |
7.51e-73 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 239.65 E-value: 7.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 60 AFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAG----MIVVNVNPLYTPRELEHQLNDSGAsAIVIVsnfahtl 135
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGG-RIVLA------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 136 ekvvDKTAVQHViltRMGDQLSTAKGTVVnfvvkyikrlvpkyhlpDAISFRSALHNGYRMqyvkpELVPEDLAFLQYTG 215
Cdd:cd05922 76 ----DAGAADRL---RDALPASPDPGTVL-----------------DADGIRAARASAPAH-----EVSHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 216 GTTGVAKGAMLTHRNMLANLEQVNATYGplLHpGKELVVTALPLYHIFALTIncLLFIELGGQNLLITNPRDIP-GLVKE 294
Cdd:cd05922 127 GSTGSPKLVRLSHQNLLANARSIAEYLG--IT-ADDRALTVLPLSYDYGLSV--LNTHLLRGATLVLTNDGVLDdAFWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 295 LAKYPFTAITGVNTLFnALLNNKEFQQLDFSSLHL--SAGGGMPvQQVVAERWVKLTGQYLLEGYGLTECAPLVS-VNPY 371
Cdd:cd05922 202 LREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYltQAGGRLP-QETIARLRELLPGAQVYVMYGQTEATRRMTyLPPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 372 DIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDA-TDEIIKNGWLHTGDIAVMDEEGFLRI 450
Cdd:cd05922 280 RILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLFI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 451 VDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSgSSGEAVKIFVVKKDPSLTEESLVtFCRRQLTGYKVPKLV 530
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPDKIDPKDVLR-SLAERLPPYKVPATV 437
|
490 500
....*....|....*....|
gi 1728558706 531 EFRDELPKSNVGKILRRELR 550
Cdd:cd05922 438 RVVDELPLTASGKVDYAALR 457
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
23-552 |
5.69e-72 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 239.66 E-value: 5.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDK-TAVQHVILTRMGDQLSTAKGtvvnfvVKYIKrLVPKYHLP 181
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWLLDAPASVSVPAG------WSTAP-LPPLDAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 182 DAISFRsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTH-------RNMLANLEqvnatygplLHPGkELVV 254
Cdd:PRK06155 173 PAAAVQ-----------------PGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLE---------IGAD-DVLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 255 TALPLYHIFALtiNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGG 334
Cdd:PRK06155 226 TTLPLFHTNAL--NAFFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 335 MPVQQVVA--ERwvklTGQYLLEGYGLTEC-APLVSVNPYDidyHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKG 411
Cdd:PRK06155 304 VPAALHAAfrER----FGVDLLDGYGSTETnFVIAVTHGSQ---RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 412 PQ---VMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PRK06155 377 DEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728558706 489 PSGSSGEAVKIFVVKKD-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06155 457 PSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-546 |
7.25e-72 |
|
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: 233.16 E-value: 7.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnLEQVNATYGPLLHPGKELVVTalPLYHIFALTINCLLFIeLGGQNLLITNPR 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR-AAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACL-LTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW-VKLTGQYLLEGYGLTECAPL 365
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 366 VSVNPYD-IDYHSGSIGLPVPSTEAKLVDDddnevppgqpGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMD 443
Cdd:cd17638 157 TMCRPGDdAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEESLVTFCRRQLT 522
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 1728558706 523 GYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
38-551 |
6.79e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 232.78 E-value: 6.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNM--GEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH 115
Cdd:PRK09088 10 QRLAAVDLalGRRWTYAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 116 QLNDSGASAIVivsnfahtlekvvdktavqhviltrmGDQLSTAKGTVVNFVVKYIKRLvpKYHLPDAisfrsalhngyr 195
Cdd:PRK09088 89 LLQDAEPRLLL--------------------------GDDAVAAGRTDVEDLAAFIASA--DALEPAD------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 196 mqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNmlanLEQVNATYGPLLHPGKELV-VTALPLYHIFALTINCLLFIE 274
Cdd:PRK09088 129 ----TPSIPPERVSLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSfLCDAPMFHIIGLITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 275 LGGqNLLITNPRDIPGLVKELAKyPFTAIT---GVNTLFNALLNNKEFqqlDFSSL-HLSA--GGGMPVQQVVAERWVKl 348
Cdd:PRK09088 201 VGG-SILVSNGFEPKRTLGRLGD-PALGIThyfCVPQMAQAFRAQPGF---DAAALrHLTAlfTGGAPHAAEDILGWLD- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 349 TGQYLLEGYGLTECAPL--VSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATD 426
Cdd:PRK09088 275 DGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 EII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD 505
Cdd:PRK09088 355 RAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1728558706 506 PSLTE-ESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK09088 435 GAPLDlERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
23-550 |
7.79e-70 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 233.42 E-value: 7.79e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFV---NMGEVMTF--RKL-EERSRAfaAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIfesSGGVVRRYsyLELnEEINRT--ANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 97 AGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKV--VDKTAVQHVILTRMGdqLSTAKGtVVNFvvkyiKRL 174
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIqqEDATPLRHICLTRVA--LPADDG-VSSF-----TQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 vpKYHLPDAISFRsalhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNML-ANLE---QVNATYgpllhpgK 250
Cdd:PRK08008 157 --KAQQPATLCYA-------------PPLSTDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYsawQCALRD-------D 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 251 ELVVTALPLYHI-FALTINCLLFiELGGQNLLI-----------------TNPRDIPGLVKELAKYPFTAITGVNTLFNA 312
Cdd:PRK08008 215 DVYLTVMPAFHIdCQCTAAMAAF-SAGATFVLLekysarafwgqvckyraTITECIPMMIRTLMVQPPSANDRQHCLREV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 313 L--LNNKEFQQLDFSslhlsagggmpvqqvvaERWvkltGQYLLEGYGLTECapLVSV---NPYDiDYHSGSIGLPVPST 387
Cdd:PRK08008 294 MfyLNLSDQEKDAFE-----------------ERF----GVRLLTSYGMTET--IVGIigdRPGD-KRRWPSIGRPGFCY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 388 EAKLVDDDDNEVPPGQPGELCVKG---PQVMLGYWQRPDATDEIIK-NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGF 463
Cdd:PRK08008 350 EAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 464 NVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVG 542
Cdd:PRK08008 430 NVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSG 509
|
....*...
gi 1728558706 543 KILRRELR 550
Cdd:PRK08008 510 KIIKKNLK 517
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-553 |
9.00e-70 |
|
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: 232.61 E-value: 9.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQGLglKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VivsnfahTLEKVVDKTAVQHVIltrmgDQLSTAKgtvvnfvVKYIKRLVPKYHLPD------AISFRSAlhNGYRMQYV 199
Cdd:cd05909 83 L-------TSKQFIEKLKLHHLF-----DVEYDAR-------IVYLEDLRAKISKADkckaflAGKFPPK--WLLRIFGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 200 KPELvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVVTALPLYHIFALTINCLLFIELGGQN 279
Cdd:cd05909 142 APVQ-PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 280 LLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKefQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGL 359
Cdd:cd05909 218 VFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 360 TECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVD-DDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGD 438
Cdd:cd05909 296 TECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 439 IAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQ-EVAAVGVPSGSSGEavKIFVVKKDPSLTEESLVTFC 517
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDIL 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 1728558706 518 RR-QLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05909 454 KNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-551 |
1.12e-67 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 227.65 E-value: 1.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 28 MF-EQSVARYADQPAFV--NMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:PRK13391 1 MYpGIHAQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NPLYTPRELEHQLNDSGASAiVIVSnfAHTLEkvVDKTAVQHV--ILTRMgdqLSTAKGTVVNFVvkyikrlvpkyHLPD 182
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARA-LITS--AAKLD--VARALLKQCpgVRHRL---VLDGDGELEGFV-----------GYAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISfrsalhnGYRMQYVKPELVPEDLaflQYTGGTTGVAKGAmlthRNMLANLEQVNATygPLLHPGKELV--------V 254
Cdd:PRK13391 141 AVA-------GLPATPIADESLGTDM---LYSSGTTGRPKGI----KRPLPEQPPDTPL--PLTAFLQRLWgfrsdmvyL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 255 TALPLYHIfALTINCLLFIELGGQNLLITN--PRDIPGLVKelaKYPFTAITGVNTLFNALLNNKEFQQL--DFSSLHLS 330
Cdd:PRK13391 205 SPAPLYHS-APQRAVMLVIRLGGTVIVMEHfdAEQYLALIE---EYGVTHTQLVPTMFSRMLKLPEEVRDkyDLSSLEVA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 331 AGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPStEAKLVDDDDNEVPPGQPGELCVK 410
Cdd:PRK13391 281 IHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 411 GPQvMLGYWQRPDATDEI--IKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PRK13391 360 GGR-PFEYLNDPAKTAEArhPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 489 PSGSSGEAVKIFV-----VKKDPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK13391 439 PNEDLGEEVKAVVqpvdgVDPGPALAAE-LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
33-550 |
1.62e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 226.02 E-value: 1.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAFVNMGE-VMTFRKLEERSRAFAAylqqglGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPR 111
Cdd:PRK07787 9 VAAAADIADAVRIGGrVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 112 ELEHQLNDSGASAIvivsnfahtlekvvdktavqhviLTRMGDQLSTakgtvvnfvvkyikrlVPkyHLPDAISFRSALh 191
Cdd:PRK07787 83 ERRHILADSGAQAW-----------------------LGPAPDDPAG----------------LP--HVPVRLHARSWH- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 192 ngyrmqyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVVTALPLYHIFALTINCLL 271
Cdd:PRK07787 121 -------RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ---WTADDVLVHGLPLFHVHGLVLGVLG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELGGQnlLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLdFSSLHLSAGGGMPVQQVVAERWVKLTGQ 351
Cdd:PRK07787 191 PLRIGNR--FVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGH 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTECAPLVSVNPyDIDYHSGSIGLPVPSTEAKLVDDDDNEVP--PGQPGELCVKGPQVMLGYWQRPDATDEII 429
Cdd:PRK07787 268 RPVERYGMTETLITLSTRA-DGERRPGWVGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 -KNGWLHTGDIAVMDEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPS 507
Cdd:PRK07787 347 tADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV 426
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1728558706 508 lTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07787 427 -AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
35-555 |
5.62e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 225.54 E-value: 5.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 35 RYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELE 114
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 115 HQLNDSGASAIVIVSNFAhtlekvVDKTAVQHVILTRMGDQLSTakgtvvnfvvkyikRLVPKYHLPDAISFRSAlhngy 194
Cdd:PRK06145 93 YILGDAGAKLLLVDEEFD------AIVALETPKIVIDAAAQADS--------------RRLAQGGLEIPPQAAVA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 195 rmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNM-LANLEQVNATygPLLHPGKELVVTalPLYHIFALTINCLLFI 273
Cdd:PRK06145 148 ----------PTDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIAL--GLTASERLLVVG--PLYHVGAFDLPGIAVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 274 ELGGQnLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MPVQQVVAERWVKLTGQ 351
Cdd:PRK06145 214 WVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGekTPESRIRDFTRVFTRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLlEGYGLTECaplVSVNPY-----DIDyHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATD 426
Cdd:PRK06145 293 YI-DAYGLTET---CSGDTLmeagrEIE-KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 EIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE-AVKIFVVKKD 505
Cdd:PRK06145 368 EAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGErITAVVVLNPG 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1728558706 506 PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARG 555
Cdd:PRK06145 448 ATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELNG 497
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
30-551 |
1.60e-66 |
|
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: 223.72 E-value: 1.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 30 EQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYT 109
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALA-ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 110 PRELEHQLNDSGASAIVIVSNFAHTlekvvdktavqhviltrmgDQLSTAKGTvvnfvvkyikrlvPKYHLP----DAIS 185
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEYE-------------------DLLAEGDPD-------------FEWIPPadewDPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 186 frsalhngyrmqyvkpelvpedlafLQYTGGTTGVAKGAMLTHRN-MLANLEQVnATYGPLLHPGkelVVTALPLYHI-- 262
Cdd:cd12118 138 -------------------------LNYTSGTTGRPKGVVYHHRGaYLNALANI-LEWEMKQHPV---YLWTLPMFHCng 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 263 --FALTINCLlfielGGQNLLITNPrDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFS-SLHLSAGGGMPVQQ 339
Cdd:cd12118 189 wcFPWTVAAV-----GGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 340 VVAErwVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSI----------GLPVPSTEAKLVDDDDNEVP-PG---QPG 405
Cdd:cd12118 263 VLAK--MEELGFDVTHVYGLTETYGPATVCAWKPEWDELPTeerarlkarqGVRYVGLEEVDVLDPETMKPvPRdgkTIG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 406 ELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAA 485
Cdd:cd12118 341 EIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 486 VGVPSGSSGEAVKIFV-VKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRdELPKSNVGKILRRELRD 551
Cdd:cd12118 421 VARPDEKWGEVPCAFVeLKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
21-551 |
3.15e-66 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 223.56 E-value: 3.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 21 RYQSLVDMFEQSVAR-YADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEgRGGKTAFIDDISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 100 IVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTA-VQHVILTrmGDQLSTAKgTVVNFVVKYIKRLVPky 178
Cdd:TIGR02262 81 VPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPhLEHRVVV--GRPEAGEV-QLAELLATESEQFKP-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 179 hlpdaisfrSALHngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLHPGKELVV-TA 256
Cdd:TIGR02262 156 ---------AATQ-------------ADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAE----LYArNTLGIREDDVCfSA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 257 LPLYHIFALTiNCLLFIELGGQNLLITNPRDIPGLV-KELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGM 335
Cdd:TIGR02262 210 AKLFFAYGLG-NALTFPMSVGATTVLMGERPTPDAVfDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 336 PVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVN-PYDIDYhsGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQV 414
Cdd:TIGR02262 289 ALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNlPGDVRY--GTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSS 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSG 494
Cdd:TIGR02262 367 ATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 495 EAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:TIGR02262 447 IKPKAFVVlRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-551 |
8.60e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 222.65 E-value: 8.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 48 VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVI 127
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 128 VSNFAHTLEKVVDKTavqhviltrmgdqlstakgtVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYR--MQYVKPELVP 205
Cdd:PRK12406 90 HADLLHGLASALPAG--------------------VTVLSVPTPPEIAAAYRISPALLTPPAGAIDWEgwLAQQEPYDGP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 --EDLAFLQYTGGTTGVAKGamlTHRN-----MLANLEQVNAT-YGplLHPGKELVVTAlPLYHIfALTINCLLFIELGG 277
Cdd:PRK12406 150 pvPQPQSMIYTSGTTGHPKG---VRRAaptpeQAAAAEQMRALiYG--LKPGIRALLTG-PLYHS-APNAYGLRAGRLGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 qnLLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLN--NKEFQQLDFSSL----HLSAGGGMPVQQVVAERWvkltG 350
Cdd:PRK12406 223 --VLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLrhviHAAAPCPADVKRAMIEWW----G 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 351 QYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVML-GYWQRPDATDEII 429
Cdd:PRK12406 297 PVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVkIFVVKKDP--S 507
Cdd:PRK12406 377 RGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL-MAVVEPQPgaT 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1728558706 508 LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK12406 456 LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-550 |
9.90e-66 |
|
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: 220.45 E-value: 9.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLYtprelehqlndsgasaivivS 129
Cdd:cd05969 2 TFAQLKVLSARFANVLKS-LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLF--------------------S 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAhtlekvvdktavQHVILTRMgdQLSTAKGTVVNfvvkyikrlvpkyhlpdaisfrsalhngyrmQYVKPELVPEDLA 209
Cdd:cd05969 58 AFG------------PEAIRDRL--ENSEAKVLITT-------------------------------EELYERTDPEDPT 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHPGKELVVTALP------LYHIFALTINCLLFIELGGQnlliT 283
Cdd:cd05969 93 LLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDLHPDDIYWCTADPgwvtgtVYGIWAPWLNGVTNVVYEGR----F 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPRDIPGLVKELA-KYPFTAITGVNTLFNAllNNKEFQQLDFSSLHLSAGGGMPVQQVVAeRW-VKLTGQYLLEGYGLTE 361
Cdd:cd05969 167 DAESWYGIIERVKvTVWYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTWWQTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 362 CAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKG--PQVMLGYWQRPDATDEIIKNGWLHTGDI 439
Cdd:cd05969 244 TGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYLTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 440 AVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEE---SLVT 515
Cdd:cd05969 324 AYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlKEGFEPSDElkeEIIN 403
|
490 500 510
....*....|....*....|....*....|....*
gi 1728558706 516 FCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05969 404 FVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
35-551 |
1.25e-65 |
|
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: 222.88 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 35 RYADQPAFVnmGEVMTFRKLEERSRAFAAYLQQGLglKKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLYTPRELE 114
Cdd:cd05931 13 TFLDDEGGR--EETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 115 HQ------LNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTvvnfvvkyikrlvpkyhlpdaisfrs 188
Cdd:cd05931 86 HAerlaaiLADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAA-------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 189 alhngyrmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVVTALPLYHIFALTIN 268
Cdd:cd05931 140 --------DWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG---LDPGDVVVSWLPLYHDMGLIGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 269 CLLFIELGGQNLLITnPRDI---PGL-VKELAKYPFTaITGV-NtlFnAL------LNNKEFQQLDFSSLHLSAGGGMPV 337
Cdd:cd05931 209 LLTPLYSGGPSVLMS-PAAFlrrPLRwLRLISRYRAT-ISAApN--F-AYdlcvrrVRDEDLEGLDLSSWRVALNGAEPV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVVAERWVKLTGQY------LLEGYGLTECAPLVSVNP---------YDIDYHSG----------------SIGLPVPS 386
Cdd:cd05931 284 RPATLRRFAEAFAPFgfrpeaFRPSYGLAEATLFVSGGPpgtgpvvlrVDRDALAGravavaaddpaarelvSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 387 TEAKLVDDDDN-EVPPGQPGELCVKGPQVMLGYWQRPDATDEIIK-------NGWLHTGDIAVMDeEGFLRIVDRKKDMI 458
Cdd:cd05931 364 QEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLI 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 459 LVSGFNVYPNEIEDVVMQ-HPGVQE--VAAVGVPSGSSGEAVKIFVVKKDP-SLTEESLVTFCRRQL-TGYKVP----KL 529
Cdd:cd05931 443 IVRGRNHYPQDIEATAEEaHPALRPgcVAAFSVPDDGEERLVVVAEVERGAdPADLAAIAAAIRAAVaREHGVApadvVL 522
|
570 580
....*....|....*....|..
gi 1728558706 530 VEfRDELPKSNVGKILRRELRD 551
Cdd:cd05931 523 VR-PGSIPRTSSGKIQRRACRA 543
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
19-555 |
5.57e-65 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 221.47 E-value: 5.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 19 PDRyqSLVDMFEQSVARYADQPAFVNM----GEV--MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALF 92
Cdd:PRK13295 22 HDR--TINDDLDACVASCPDKTAVTAVrlgtGAPrrFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 93 GILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNF-----AHTLEKVVDK-TAVQHVILTRMGDQLSTAKgtvvnf 166
Cdd:PRK13295 99 ACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPElPALRHVVVVGGDGADSFEA------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 167 vvkyiKRLVPKYHL-PDAISFRSALHNGyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvNATYGPL 245
Cdd:PRK13295 173 -----LLITPAWEQePDAPAILARLRPG-----------PDDVTQLIYTSGTTGEPKGVMHTANTLMAN----IVPYAER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 246 LHPGKELVV-TALPLYHIFALTINCLLFIELGGQNLL--ITNPRDIPGLVKE------LAKYPFTAitgvntlfnALLNN 316
Cdd:PRK13295 233 LGLGADDVIlMASPMAHQTGFMYGLMMPVMLGATAVLqdIWDPARAAELIRTegvtftMASTPFLT---------DLTRA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 317 KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYH-SGSIGLPVPSTEAKLVDDD 395
Cdd:PRK13295 304 VKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERaSTTDGCPLPGVEVRVVDAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 396 DNEVPPGQPGELCVKGPQVMLGYWQRPD--ATDEiikNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PRK13295 384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQlnGTDA---DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEAL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 474 VMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQ-LTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK13295 461 LYRHPAIAQVAIVAYPDERLGERACAFVVpRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
....
gi 1728558706 552 EARG 555
Cdd:PRK13295 541 MLRG 544
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
27-543 |
3.76e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 218.60 E-value: 3.76e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:PRK07798 7 DLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTA-VQHVIltRMGDQLSTAkgtvvnfvvkyikrlvpkyHLPDAIS 185
Cdd:PRK07798 86 RYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPkLRTLV--VVEDGSGND-------------------LLPGAVD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 186 FRSALHNGyRMQYVKPELVPEDLAFLqYTGGTTGVAKGAMLTHRNM-LANLEQVNATYGPLLHPGKELVVTAL------- 257
Cdd:PRK07798 145 YEDALAAG-SPERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDEEELAKRAAagpgmrr 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 258 ----PLYHIFAL--TINCLLFielGGQNLLITNPR-DIPGLVKELAKYPFTAITGVNT-----LFNALLNNKEFqqlDFS 325
Cdd:PRK07798 223 fpapPLMHGAGQwaAFAALFS---GQTVVLLPDVRfDADEVWRTIEREKVNVITIVGDamarpLLDALEARGPY---DLS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 326 SLHLSAGGGMPVQQVVAERWVKLTGQ-YLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPV-PSTeaKLVDDDDNEVPPG- 402
Cdd:PRK07798 297 SLFAIASGGALFSPSVKEALLELLPNvVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIgPRT--VVLDEDGNPVEPGs 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 403 -QPGELCVKGPqVMLGYWQRPDATDEIIK--NG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:PRK07798 375 gEIGWIARRGH-IPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAH 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 478 PGVQEVAAVGVPSGSSGEAVkIFVVKKDP--SLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:PRK07798 454 PDVADALVVGVPDERWGQEV-VAVVQLREgaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-549 |
5.00e-64 |
|
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: 215.85 E-value: 5.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 37 ADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYtPRE-LEH 115
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 116 QLNDSGAsaivivsnfahtlekvvdktavqHVILTRmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyr 195
Cdd:cd05930 79 ILEDSGA-----------------------KLVLTD-------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 196 mqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVVTALplyhIFALTINCLLFIEL 275
Cdd:cd05930 92 ---------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY-PLTPGDRVLQFTSF----SFDVSVWEIFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 276 GGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQqlDFSSLHLSAGGGMPVQQVVAERWVKL-TGQ 351
Cdd:cd05930 158 AGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELlPGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTECAPLVS---VNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEI 428
Cdd:cd05930 236 RLVNLYGPTEATVDATyyrVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 429 I------KNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV 501
Cdd:cd05930 316 FvpnpfgPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYV 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1728558706 502 V-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05930 396 VpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-551 |
7.25e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 218.26 E-value: 7.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 20 DRYQSLVDMFEQSVARYADQPAFVN-MGEvMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK07788 46 RRYGPFAGLVAHAARRAPDRAALIDeRGT-LTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 99 MIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRmGDQLSTAKGTVVNfvvkyikrlvpky 178
Cdd:PRK07788 124 ARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGN-PDDDEPSGSTDET------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 179 hLPDAISFRSAlhngyrmqyVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhPGKELVVTALP 258
Cdd:PRK07788 190 -LDDLIAGSST---------APLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLAGL-LSRVPF--RAGETTLLPAP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHIFALTiNCLLFIELGgqNLLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGM 335
Cdd:PRK07788 257 MFHATGWA-HLTLAMALG--STVVLRRRfDPEATLEDIAKHKATALVVVPVMLSRILDlgPEVLAKYDTSSLKIIFVSGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 336 PVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVM 415
Cdd:PRK07788 334 ALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 416 LGYwqrPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE 495
Cdd:PRK07788 414 EGY---TDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 496 AVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK07788 491 RLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
50-549 |
1.78e-63 |
|
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: 214.23 E-value: 1.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAsaivivs 129
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ-GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 nfahtlekvvdktavqHVILTrmgDQLSTAKGTvvnfvvkyikrlvpkyhlpDAISFRSALHNGYRMQYVKPELVPEDLA 209
Cdd:TIGR01923 73 ----------------QLLLT---DSLLEEKDF-------------------QADSLDRIEAAGRYETSLSASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVtALPLYHIFALTIncLLFIELGGQNLLITNPRDip 289
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDNWLL-SLPLYHISGLSI--LFRWLIEGATLRIVDKFN-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 290 GLVKELAKYPFTAITGVNTLFNALLNnkefQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTECAPLVSVN 369
Cdd:TIGR01923 188 QLLEMIANERVTHISLVPTQLNRLLD----EGGHNENLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 370 PYDIDYHSGSIGLPVPSTEAKLVDDDDNEVppgqpGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLR 449
Cdd:TIGR01923 263 TPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEA-VKIFVVKKDPSLTEesLVTFCRRQLTGYKVPK 528
Cdd:TIGR01923 338 VLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVpVAYIVSESDISQAK--LIAYLTEKLAKYKVPI 415
|
490 500
....*....|....*....|.
gi 1728558706 529 LVEFRDELPKSNVGKILRREL 549
Cdd:TIGR01923 416 AFEKLDELPYNASGKILRNQL 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-553 |
2.45e-63 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 211.57 E-value: 2.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE--QVNATYGPllhpgKELVVTALPLYHIFALTINCLLFIELGGQnLLI 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWmlALNSLFDP-----DDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 283 TNP---RDiPGLVKEL----AKYPFTAITGVNTLFNALLNNKEfqQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLE 355
Cdd:cd05944 75 AGPagyRN-PGLFDNFwklvERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 356 GYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDN-----EVPPGQPGELCVKGPQVMLGYWQRPDATDEIIK 430
Cdd:cd05944 152 GYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 431 NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV-VKKDPSLT 509
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1728558706 510 EESLVTFCRRQLTGY-KVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05944 312 EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-546 |
3.98e-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: 214.23 E-value: 3.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 vivsnfahtlekvvdktavqhviltrmgdqlstakgtvvnFVVKyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvP 205
Cdd:cd05914 84 ----------------------------------------FVSD-----------------------------------E 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygPLLHPGkELVVTALPLYHIFALTINCLLFIELGGQNLLITNP 285
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEV--VLLGKG-DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 286 RdiPGLVKELAKYPFTAITGVNTLF-----------------------NALLNNKEFQQLDFSSLHLSAGG--------G 334
Cdd:cd05914 166 P--SAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGnikefvigG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 335 MPVQQVVAERWVKLTGQYLlEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDDdnevPPGQPGELCVKGPQV 414
Cdd:cd05914 244 AKINPDVEEFLRTIGFPYT-IGYGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILV-SGFNVYPNEIEDVVMQHPGVQEvAAVGVPSGS 492
Cdd:cd05914 318 MKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEKK 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728558706 493 SGEAVKIF----------VVKKDPSLTEESLVTFcRRQLTGY-KVPKLVEFRDELPKSNVGKILR 546
Cdd:cd05914 397 LVALAYIDpdfldvkalkQRNIIDAIKWEVRDKV-NQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-549 |
5.63e-63 |
|
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: 214.68 E-value: 5.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNM--GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 101 VVNVNPLYTPRELEhQLNDSGASAIVIVSNFAhtleKVVDKTAVQHVILTRMGDQLSTAKGTVVNfvvkyikrlvpkyhl 180
Cdd:cd05923 80 PALINPRLKAAELA-ELIERGEMTAAVIAVDA----QVMDAIFQSGVRVLALSDLVGLGEPESAG--------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 181 pDAISFRSalhngyrmqyvkPElvPEDLAFLQYTGGTTGVAKGAMLTHRnmlANLEQV--NATYGPLLHPGKELVVTALP 258
Cdd:cd05923 140 -PLIEDPP------------RE--PEQPAFVFYTSGTTGLPKGAVIPQR---AAESRVlfMSTQAGLRHGRHNVVLGLMP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHI---FALTINCLLFielGGQNLLIT--NPRDIPGLVKELAkypFTAITGVNTLFNALLNNKEFQQLDFSSL-HLS-A 331
Cdd:cd05923 202 LYHVigfFAVLVAALAL---DGTYVVVEefDPADALKLIEQER---VTSLFATPTHLDALAAAAEFAGLKLSSLrHVTfA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 332 GGGMPvqQVVAERWVKLTGQYLLEGYGLTECAPLVsvnpYDIDYHSGSIGLPVPSTEAKLV---DDDDNEVPPGQPGELC 408
Cdd:cd05923 276 GATMP--DAVLERVNQHLPGEKVNIYGTTEAMNSL----YMRDARTGTEMRPGFFSEVRIVrigGSPDEALANGEEGELI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 409 VK--GPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAV 486
Cdd:cd05923 350 VAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 487 GVPSGSSGEAVKIFVVKKDPSLTEESLVTFCR-RQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05923 430 GVADERWGQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
50-550 |
1.42e-61 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 212.83 E-value: 1.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVvnvNPLYT---PRELEHQLNDSGASaiV 126
Cdd:PRK04319 75 TYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEafmEEAVRDRLEDSEAK--V 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 127 IVSNFAHTLEKVVDKT-AVQHVILTrmgDQLSTAKGTVVNFvvkyikrlvpkyhlpdaisfrsalhnGYRMQYVKPE--- 202
Cdd:PRK04319 149 LITTPALLERKPADDLpSLKHVLLV---GEDVEEGPGTLDF--------------------------NALMEQASDEfdi 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 203 --LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGKELVVTALP------LYHIFALTINCLLFIE 274
Cdd:PRK04319 200 ewTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHY--QTGKYVLDLHEDDVYWCTADPgwvtgtSYGIFAPWLNGATNVI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 275 LGGQnlliTNPRDIPGLvkeLAKYP----FTAITGVNTLFNAllNNKEFQQLDFSSLHLSAGGGMPVQ-QVVaeRW-VKL 348
Cdd:PRK04319 278 DGGR----FSPERWYRI---LEDYKvtvwYTAPTAIRMLMGA--GDDLVKKYDLSSLRHILSVGEPLNpEVV--RWgMKV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 349 TGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKG--PQVMLGYWQRPDATD 426
Cdd:PRK04319 347 FGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 EIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD- 505
Cdd:PRK04319 427 SYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPg 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1728558706 506 --PS--LTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK04319 507 yePSeeLKEE-IRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
47-552 |
9.13e-59 |
|
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: 204.24 E-value: 9.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 47 EVM-TFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05928 39 EVKwSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEKVVDKTAvqhviltrmgdQLSTakgtvvnfvvkyiKRLVPKYHLPDAISFRSAlhngyrMQYVKPELV- 204
Cdd:cd05928 119 VTSDELAPEVDSVASECP-----------SLKT-------------KLLVSEKSRDGWLNFKEL------LNEASTEHHc 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 ----PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYGPLLHPGKEL--------VVTALplYHIFALTIN-CLL 271
Cdd:cd05928 169 vetgSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGL-KVNGRYWLDLTASDIMwntsdtgwIKSAW--SSLFEPWIQgACV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELggqnllitNPR-DIPGLVKELAKYPFTAITGVNTLFNALLNNkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTG 350
Cdd:cd05928 246 FVHH--------LPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 351 QYLLEGYGLTECApLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVK-GPQ----VMLGYWQRPDAT 425
Cdd:cd05928 317 LDIYEGYGQTETG-LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 426 DEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV--- 502
Cdd:cd05928 396 AATIRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlap 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 503 ---KKDP-SLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:cd05928 476 qflSHDPeQLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-485 |
1.32e-58 |
|
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: 200.57 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVDKTAVQHVILTRMGDQLSTAKgtvvnfvvkyikrlvpkyhLPDAISfrsalhngyrmqyvkpelVPEDLA 209
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPP-------------------PPDAPS------------------GPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhpGKELVVTALPLYH-------IFAltinCLLFielGGQNLLI 282
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL----DPDDRVLQFASLSfdasveeIFG----ALLA---GATLVVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 283 TNP--RDIPGLVKEL-AKYPFTAITGVNTLFNALLnnkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ-YLLEGYG 358
Cdd:TIGR01733 193 PEDeeRDDAALLAALiAEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGaRLINLYG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 359 LTECAPLVSVNPYDIDYHSG----SIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE-IIKNG- 432
Cdd:TIGR01733 270 PTETTVWSTATLVDPDDAPRespvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErFVPDPf 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 433 -------WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAA 485
Cdd:TIGR01733 350 aggdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
19-551 |
3.30e-58 |
|
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: 203.11 E-value: 3.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 19 PDRYQSLVDMFEQSVARYADQPAFV---NMGE--VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:cd05970 13 PENFNFAYDVVDAMAKEYPDKLALVwcdDAGEerIFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSLLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNfaHTLEKVVDKTAVQHVILTRM---GDQLSTAkgtVVNFVvKY 170
Cdd:cd05970 92 LHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--DNIPEEIEKAAPECPSKPKLvwvGDPVPEG---WIDFR-KL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 171 IKRLVPKYHLPDAISFRSAlhngyrmqyvkpelvpEDLAFLQYTGGTTGVAKgaMLTHrnmlanleqvNATYgPLLHpgk 250
Cdd:cd05970 166 IKNASPDFERPTANSYPCG----------------EDILLVYFSSGTTGMPK--MVEH----------DFTY-PLGH--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 251 elVVTALPLYHI----FALTI------NCL---LFIE-LGGQNLLITN-PRDIP-GLVKELAKYPFTAITGVNTLFNALL 314
Cdd:cd05970 214 --IVTAKYWQNVreggLHLTVadtgwgKAVwgkIYGQwIAGAAVFVYDyDKFDPkALLEKLSKYGVTTFCAPPTIYRFLI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 315 NNKeFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYdIDYHSGSIGLPVPSTEAKLVDD 394
Cdd:cd05970 292 RED-LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW-MEPKPGSMGKPAPGYEIDLIDR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 395 DDNEVPPGQPGELCV---KGPQVML--GYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:cd05970 370 EGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 470 IEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-----KKDPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:cd05970 450 VESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
....*..
gi 1728558706 545 LRRELRD 551
Cdd:cd05970 529 RRVEIRE 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
201-551 |
4.00e-58 |
|
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: 201.07 E-value: 4.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 201 PELVPEDLA---FLQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLLHPGKELVVTAL---PLYHIfALTINCLLFIE 274
Cdd:cd05929 117 PETPIEDEAagwKMLYSGGTTGRPKGIK---RGLPGGPPDNDTLMAAALGFGPGADSVYLspaPLYHA-APFRWSMTALF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 275 LGGQNLLITN--PRDIPGLVKelaKYPFTAITGVNTLFNALLNNKEFQQ--LDFSSL----HlsAGGGMPVQqvVAERWV 346
Cdd:cd05929 193 MGGTLVLMEKfdPEEFLRLIE---RYRVTFAQFVPTMFVRLLKLPEAVRnaYDLSSLkrviH--AAAPCPPW--VKEQWI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 347 KLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPStEAKLVDDDDNEVPPGQPGELCVKGPQVMLgYWQRPDATD 426
Cdd:cd05929 266 DWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 E-IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV---- 501
Cdd:cd05929 344 AaRNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpap 423
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 502 -VKKDPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05929 424 gADAGTALAEE-LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-487 |
4.74e-58 |
|
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: 200.66 E-value: 4.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGmiVVNVnplytPR-------ELEHQLNDSGA 122
Cdd:cd17640 7 TYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALG--AVDV-----VRgsdssveELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 123 SAIVIvsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpE 202
Cdd:cd17640 79 VALVV--------------------------------------------------------------------------E 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 203 LVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllHPGKElVVTALPLYHIFALTinCLLFIELGGQNLLI 282
Cdd:cd17640 85 NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP--QPGDR-FLSILPIWHSYERS--AEYFIFACGCSQAY 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 283 TNPRDIPglvKELAKYPFTAITGVNTLFNALLNN--KEFQQLDFSS---LH-----------LSAGGGMPVQqvvAERWV 346
Cdd:cd17640 160 TSIRTLK---DDLKRVKPHYIVSVPRLWESLYSGiqKQVSKSSPIKqflFLfflsggifkfgISGGGALPPH---VDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 347 KLTGQYLLEGYGLTECAPLVSVNPYDIDYhSGSIGLPVPSTEAKLVDDDDNEV-PPGQPGELCVKGPQVMLGYWQRPDAT 425
Cdd:cd17640 234 EAIGIEVLNGYGLTETSPVVSARRLKCNV-RGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEAT 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 426 DEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:cd17640 313 SKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-549 |
7.03e-58 |
|
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: 200.89 E-value: 7.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRA-AGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYTPRELEHQLNDSGASAIVIvsnfAHTLEKVVDKTAVQHVILtrmgDQLSTAKGTVVNFVVKyikrlvpkyhlpdaisf 186
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLEVAVVID----EALDAGPAGNPAVPVS----------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 rsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvNATYGPLlHPGKELVVTALPLYHIFALT 266
Cdd:cd12117 135 ------------------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTL-GPDDRVLQTSPLAFDASTFE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 267 I-NCLLFielGGQnlLITNPRDIPGLVKELAKypFTAITGVNTLF--NALlnnkeFQQLD------FSSL-HLSAGG-GM 335
Cdd:cd12117 194 IwGALLN---GAR--LVLAPKGTLLDPDALGA--LIAEEGVTVLWltAAL-----FNQLAdedpecFAGLrELLTGGeVV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 336 PVQQV--VAERWVKLTgqyLLEGYGLTE---CAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVK 410
Cdd:cd12117 262 SPPHVrrVLAACPGLR---LVNGYGPTEnttFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 411 GPQVMLGYWQRPDATDE-IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEV 483
Cdd:cd12117 339 GDGLALGYLNRPALTAErFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREA 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 484 AAVGVPSGSSGEAVKIFVVkKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12117 419 VVVVREDAGGDKRLVAYVV-AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-549 |
1.96e-57 |
|
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: 199.48 E-value: 1.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIVIVsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyiKRLVPKYHLPD 182
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVP-------------------------------------------DRHAGFDHRAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISFRSALhngyrmqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHR----NMLANLEqvnatygpLLHPGKELV-VTAL 257
Cdd:cd05920 131 ARELAESI---------------PEVALFLLSGGTTGTPKLIPRTHNdyayNVRASAE--------VCGLDQDTVyLAVL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 258 PLYHIFALT----INCLLFielGGQNLLITNPRdiPGLVKEL-AKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:cd05920 188 PAAHNFPLAcpgvLGTLLA---GGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 333 GGMPVQQVVAERWVKLTGQYLLEGYGLTEcaPLVSV----NPYDIDYHSGsiGLPV-PSTEAKLVDDDDNEVPPGQPGEL 407
Cdd:cd05920 263 GGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYtrldDPDEVIIHTQ--GRPMsPDDEIRVVDEEGNPVPPGEEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 408 CVKGPQVMLGYWQRPDA-TDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAV 486
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHnARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 487 GVPSGSSGEAVKIFVVKKDPSLTEESLVTFCR-RQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05920 419 AMPDELLGERSCAFVVLRDPPPSAAQLRRFLReRGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
20-553 |
1.18e-56 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 205.54 E-value: 1.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 20 DRYQSLVDMFEQSVARYADQPAFVN-MGEVMTFRKLEERSRAFAAYLQQGLglKKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK08633 612 EALPPLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKREL--KDEENVGILLPPSVAGALANLALLLAG 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 99 MIVVNVNplYTPRE--LEHQLNDSGASAIVIVSNFahtLEKVVDKTAVQHVIL---TRMGDQLSTAKGTVVNFVVKYIKR 173
Cdd:PRK08633 690 KVPVNLN--YTASEaaLKSAIEQAQIKTVITSRKF---LEKLKNKGFDLELPEnvkVIYLEDLKAKISKVDKLTALLAAR 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 174 LVPKyhlpdaisfrSALHNGYRmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtygpLLHPGKE-L 252
Cdd:PRK08633 765 LLPA----------RLLKRLYG-----PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISD----VFNLRNDdV 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 253 VVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:PRK08633 826 ILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVA 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 333 GGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDI---DYHS------GSIGLPVPSTEAKLVDDDD-NEVPPG 402
Cdd:PRK08633 906 GAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVlaaDFKRqtgskeGSVGMPLPGVAVRIVDPETfEELPPG 985
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 403 QPGELCVKGPQVMLGYWQRPDATDEIIKN----GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-- 476
Cdd:PRK08633 986 EDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKal 1065
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 477 HPGVQEVAAVGVPSGSSGEavKIFVVKKDPSLTEESLvtfcRRQLTGYKVPKLVEFR-----DELPKSNVGKILRRELRD 551
Cdd:PRK08633 1066 GGEEVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEEL----KRAIKESGLPNLWKPSryfkvEALPLLGSGKLDLKGLKE 1139
|
..
gi 1728558706 552 EA 553
Cdd:PRK08633 1140 LA 1141
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
28-550 |
3.41e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 196.77 E-value: 3.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 28 MFEQSVARYA-DQPAFV--NMGEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:PRK13390 1 MYPGTHAQIApDRPAVIvaETGEQVSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NPLYTPRELEHQLNDSGASAIVIVSnfahTLEKVVDKTAVQHVILTRMGdqlstakGTVVNFVvkyikrlvpkyhlpdai 184
Cdd:PRK13390 80 NHHLTAPEADYIVGDSGARVLVASA----ALDGLAAKVGADLPLRLSFG-------GEIDGFG----------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 185 SFRSALHNGyrmqyvKPELVPEDL-AFLQYTGGTTGVAKGAM--LTHRNMLANLEQVNATYGPLLH-PGKELVVTALPLY 260
Cdd:PRK13390 132 SFEAALAGA------GPRLTEQPCgAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDiSESDIYYSSAPIY 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 261 HIFALTInCLLFIELGGqNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALL--NNKEFQQLDFSSLHLSAGGGMPVQ 338
Cdd:PRK13390 206 HAAPLRW-CSMVHALGG-TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 339 QVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTeAKLVDDDDNEVPPGQPGELCVKGPQVMLGY 418
Cdd:PRK13390 284 VDVKHAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 419 WQRPDATDEIIKNG---WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE 495
Cdd:PRK13390 363 LNDPEKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGE 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 496 AVKIFV-----VKKDPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK13390 443 QVKAVIqlvegIRGSDELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
14-558 |
5.27e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 196.89 E-value: 5.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 14 PTEINPDRYQSLVDmfeQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK06164 4 DAAPRADTLASLLD---AHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFaHTLEKVVDKTAVQHviltrmgDQLSTAKGTvvnFVVKYIKR 173
Cdd:PRK06164 80 CARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGF-KGIDFAAILAAVPP-------DALPPLRAI---AVVDDAAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 174 LVPKyHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQY-TGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkEL 252
Cdd:PRK06164 149 ATPA-PAPGARVQLFALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIARAYG--YDPG-AV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 253 VVTALPLYHIFALtiNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLnNKEFQQLDFSSLHLS-- 330
Cdd:PRK06164 225 LLAALPFCGVFGF--STLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRIL-DTAGERADFPSARLFgf 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 331 ---AGGGMPVQQVVAERWVKLTGQyllegYGLTECAPLVSVNPYDIDY---HSGSiGLPV-PSTEAKLVDDDDNEV-PPG 402
Cdd:PRK06164 302 asfAPALGELAALARARGVPLTGL-----YGSSEVQALVALQPATDPVsvrIEGG-GRPAsPEARVRARDPQDGALlPDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 403 QPGELCVKGPQVMLGYWQRPDAT-DEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQ 481
Cdd:PRK06164 376 ESGEIEIRAPSLMRGYLDNPDATaRALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 482 EVAAVGVPSGSSGEAVKiFVVKKD-PSLTEESLVTFCRRQLTGYKVPKLVEFRDELP---KSNVGKILRRELRDEARGKV 557
Cdd:PRK06164 456 AAQVVGATRDGKTVPVA-FVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLREMAQARL 534
|
.
gi 1728558706 558 D 558
Cdd:PRK06164 535 A 535
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
213-538 |
2.08e-55 |
|
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: 189.82 E-value: 2.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 213 YTGGTTGVAKGAMLTHRN------MLANLEQVNATYGPLlhpgkelvvTALPLYHIFALTINCLLFIeLGGQNLLI--TN 284
Cdd:cd17636 7 YTAAFSGRPNGALLSHQAllaqalVLAVLQAIDEGTVFL---------NSGPLFHIGTLMFTLATFH-AGGTNVFVrrVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLV-KELAKYPFTAITGVNTLFNAllnNKEFQqLDFSSLHLSAG--GGMPVQQVVAERWVKLTGqylleGYGLTE 361
Cdd:cd17636 77 AEEVLELIeAERCTHAFLLPPTIDQIVEL---NADGL-YDLSSLRSSPAapEWNDMATVDTSPWGRKPG-----GYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 362 CAPLVSVNPYDIDYHSGSiGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAV 441
Cdd:cd17636 148 VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 442 MDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVK-IFVVKKDPSLTEESLVTFCRRQ 520
Cdd:cd17636 227 REPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKaIVVLKPGASVTEAELIEHCRAR 306
|
330
....*....|....*...
gi 1728558706 521 LTGYKVPKLVEFRDELPK 538
Cdd:cd17636 307 IASYKKPKSVEFADALPR 324
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-555 |
3.61e-55 |
|
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: 201.24 E-value: 3.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 4 VWLNRYPADVPTEinpdryQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPN 83
Cdd:COG1020 463 AEWNATAAPYPAD------ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLER 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 84 LLQYPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGASAIVIVSNFAHTLekvvDKTAVQHVILtrmgDQLSTAKGT 162
Cdd:COG1020 536 SLEMVVALLAVLKAGAAYVPLDPAY-PAErLAYMLEDAGARLVLTQSALAARL----PELGVPVLAL----DALALAAEP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 163 VVNFVVkyikrlvpkyhlpdaisfrsalhngyrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:COG1020 607 ATNPPV---------------------------------PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 243 GplLHPG-KELVVTAL----PLYHIFAltinCLLFielGGQnLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALL 314
Cdd:COG1020 654 G--LGPGdRVLQFASLsfdaSVWEIFG----ALLS---GAT-LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 315 nnkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY-LLEGYGLTECAPLVS---VNPYDIDYHSGSIGLPVPSTEAK 390
Cdd:COG1020 724 ---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTETTVDSTyyeVTPPDADGGSVPIGRPIANTRVY 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 391 LVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE------IIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSG 462
Cdd:COG1020 801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 463 FNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFC-RRQLTGYKVPKLVEFRDELPKSNV 541
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGN 960
|
570
....*....|....
gi 1728558706 542 GKILRRELRDEARG 555
Cdd:COG1020 961 GKLDRLALPAPAAA 974
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
18-554 |
5.85e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 194.40 E-value: 5.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 18 NPDRYQSL--VDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGIL 95
Cdd:PRK08162 11 NAANYVPLtpLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 96 RAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDqlstakgtvvnfvvkyikrlv 175
Cdd:PRK08162 90 MAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDD--------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 176 PKY---HLPDAISFRSALHNGyrmqyvKPELV---PED----LAfLQYTGGTTGVAKGAMLTHR----NMLANleQVNAT 241
Cdd:PRK08162 149 PEYpggRFIGALDYEAFLASG------DPDFAwtlPADewdaIA-LNYTSGTTGNPKGVVYHHRgaylNALSN--ILAWG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 242 YGPllHPgkeLVVTALPLYHI----FALTINCllfieLGGQNLLItnpRDI-PGLVKEL-AKYPFTAITGVNTLFNALLN 315
Cdd:PRK08162 220 MPK--HP---VYLWTLPMFHCngwcFPWTVAA-----RAGTNVCL---RKVdPKLIFDLiREHGVTHYCGAPIVLSALIN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 316 NKEFQQLDFS-SLHLSAGGGMPVQQVVAErwVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSI----------GLPV 384
Cdd:PRK08162 287 APAEWRAGIDhPVHAMVAGAAPPAAVIAK--MEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLderaqlkarqGVRY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 385 PSTEAKLVDDDDN--EVP-PGQP-GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILV 460
Cdd:PRK08162 365 PLQEGVTVLDPDTmqPVPaDGETiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIIS 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 461 SGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEESLVTFCRRQLTGYKVPKLVEFrDELPKS 539
Cdd:PRK08162 445 GGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVeLKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKT 523
|
570
....*....|....*
gi 1728558706 540 NVGKILRRELRDEAR 554
Cdd:PRK08162 524 STGKIQKFVLREQAK 538
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
19-551 |
1.29e-54 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 193.05 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 19 PDRYQSLV-----------DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQY 87
Cdd:PRK13382 28 PDRYLRIVaamrregmgptSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQ-ALPIGEPRVVGIMCRNHRGF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 88 PVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQhvilTRMGDQLSTAKGTVVNFV 167
Cdd:PRK13382 107 VEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQA----TRIVAWTDEDHDLTVEVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 168 VkyikrlvpkyhlpdaisfrsALHNGYRmqyvkPELVPEDLAFLQYTGGTTGVAKGAMlthrnmlanlEQVNATYGPLLH 247
Cdd:PRK13382 183 I--------------------AAHAGQR-----PEPTGRKGRVILLTSGTTGTPKGAR----------RSGPGGIGTLKA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 248 -----PGK--ELVVTALPLYH-------IFALTINCLLfielggqnllITNPR-DIPGLVKELAKYPFTAITGVNTLFNA 312
Cdd:PRK13382 228 ildrtPWRaeEPTVIVAPMFHawgfsqlVLAASLACTI----------VTRRRfDPEATLDLIDRHRATGLAVVPVMFDR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 313 LLN--NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAK 390
Cdd:PRK13382 298 IMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 391 LVDDDDNEVPPGQPGELCVKGPQVMLGYwqRPDATDEIIkNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
Cdd:PRK13382 378 ILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH-DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 471 EDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK13382 455 EKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
..
gi 1728558706 550 RD 551
Cdd:PRK13382 535 QA 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
33-549 |
5.00e-53 |
|
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: 186.68 E-value: 5.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPlYTPRE 112
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSPAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 113 lehqlndsgasaivivsnfahtlekvvdktavqhviltRMGDQLSTAKGTVVnfvvkyikrlvpkyhlpdaisfrsalhn 192
Cdd:cd05945 79 --------------------------------------RIREILDAAKPALL---------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 193 gyrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpLLHPGKELVVTA-----LPLYHIFAlti 267
Cdd:cd05945 93 ---------IADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDF--PLGPGDVFLNQApfsfdLSVMDLYP--- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 nCLLfieLGGQnlLITNPRDIPG----LVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLS--AGGGMPVQQvv 341
Cdd:cd05945 159 -ALA---SGAT--LVPVPRDATAdpkqLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFlfCGEVLPHKT-- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 342 AERWVKLT-GQYLLEGYGLTECAplVSVNPYDID------YHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQV 414
Cdd:cd05945 231 ARALQQRFpDARIYNTYGPTEAT--VAVTYIEVTpevldgYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDATDE----IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPS 490
Cdd:cd05945 309 SKGYLNNPEKTAAaffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 491 GSSGEAVKIFVVKKDPS---LTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05945 389 GEKVTELIAFVVPKPGAeagLTKA-IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-551 |
3.31e-52 |
|
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: 180.99 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLhPGKELVvtALPLYHI--FALTINCLLfielGGQNLLITN 284
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGG-GDSWLL--SLPLYHVggLAILVRSLL----AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDipGLVKELAKYPFTAITGVNT-LFNALLNNKEFQQLDfsSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTECA 363
Cdd:cd17630 74 RNQ--ALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 364 PLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDddnevppgqpGELCVKGPQVMLGYWqRPDATDEIIKNGWLHTGDIAVMD 443
Cdd:cd17630 149 SQVATKRPD-GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVkIFVVKKDPSLTEESLVTFCRRQLTG 523
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLAR 295
|
330 340
....*....|....*....|....*...
gi 1728558706 524 YKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-549 |
7.57e-52 |
|
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: 184.40 E-value: 7.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 26 VDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVN 105
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 106 PLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDqlstakgtvvnfvvkyikrlvpkyHLPDais 185
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPA------------------------TPPL--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 186 frsalhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVVTALPlyhiFAL 265
Cdd:cd17646 133 ---------------VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY-PLGPGDRVLQKTPLS----FDV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 266 TINCLLFIELGGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDfsSLHLSAGGGMPVQQVVA 342
Cdd:cd17646 193 SVWELFWPLVAGARLVVARPgghRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 343 ERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS--IGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQ 420
Cdd:cd17646 271 ARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 421 RPDATDEIIKNGWL-------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSS 493
Cdd:cd17646 351 RPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAG 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 494 GEAVKIFVVKKD--PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17646 431 AARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
50-551 |
8.53e-52 |
|
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: 185.56 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDsgasaiviVS 129
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRK--------LR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEkvvdktavQHVILTRmgdqlstakgtvvnfvvkyiKRLVPKY--------HLPDAISFRSALHNGYRmQYVKP 201
Cdd:cd05906 112 HIWQLLG--------SPVVLTD--------------------AELVAEFagletlsgLPGIRVLSIEELLDTAA-DHDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG-----------PLLHpgkelvVTALPLYHIFAltincl 270
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGltpqdvflnwvPLDH------VGGLVELHLRA------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 271 lfIELGGQ------NLLITNPRDIPGLVKelaKYPFTAITGVNTLFnALLNNK----EFQQLDFSSLHLSAGGGMPVQQV 340
Cdd:cd05906 231 --VYLGCQqvhvptEEILADPLRWLDLID---RYRVTITWAPNFAF-ALLNDLleeiEDGTWDLSSLRYLVNAGEAVVAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 341 VAERWVKLTGQYLLE------GYGLTE-CAPLVSVNPYDIDYHSG-----SIGLPVPSTEAKLVDDDDNEVPPGQPGELC 408
Cdd:cd05906 305 TIRRLLRLLEPYGLPpdairpAFGMTEtCSGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 409 VKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDeEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQE--VAA 485
Cdd:cd05906 385 VRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAA 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1728558706 486 VGV--PSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLT---GYKVPKLVEF-RDELPKSNVGKILRRELRD 551
Cdd:cd05906 464 FAVrdPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPLpKEEIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-549 |
1.15e-50 |
|
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: 180.95 E-value: 1.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYtPRE-LEHQ 116
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 117 LNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAkgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrm 196
Cdd:cd12116 80 LEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTP------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 197 qyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTALPLYHIFALTincLLFIELG 276
Cdd:cd12116 123 ------VSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLG--LGPGDRLLAVTTYAFDISLLE---LLLPLLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNkEFQQLDfsSLHLSAGGgMPVQQVVAERWVKLTGQyL 353
Cdd:cd12116 192 GARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDA-GWQGRA--GLTALCGG-EALPPDLAARLLSRVGS-L 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 354 LEGYGLTE-----CAPLVSVNPYDIDyhsgsIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE- 427
Cdd:cd12116 267 WNLYGPTEttiwsTAARVTAAAGPIP-----IGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAEr 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 428 -----IIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIF 500
Cdd:cd12116 342 fvpdpFAGPGsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYV 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1728558706 501 VVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12116 422 VLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-550 |
1.72e-49 |
|
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: 178.31 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 29 FEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLY 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLR-ARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 109 TPRELEHQLNDSGASAIVivsnfahTLEKVVDKTAVQHVILTRMgDQLSTAKGTVVNfvvkyikrlvpkyhlPDaisfrs 188
Cdd:cd17651 80 PAERLAFMLADAGPVLVL-------THPALAGELAVELVAVTLL-DQPGAAAGADAE---------------PD------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 189 alhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQVNATYGPLlHPGKELVVTALPLYHIFALTIN 268
Cdd:cd17651 131 ------------PALDADDLAYVIYTSGSTGRPKGVVMPHR-SLANLVAWQARASSL-GPGARTLQFAGLGFDVSVQEIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 269 CLLfieLGGQNLLITNPR---DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSL-HLSAGG-GMPVQQVVAE 343
Cdd:cd17651 197 STL---CAGATLVLPPEEvrtDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALrYLLTGGeQLVLTEDLRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 344 RWVKLTGQYLLEGYGLTEcAPLVS--VNPYDIDYH--SGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYW 419
Cdd:cd17651 274 FCAGLPGLRLHNHYGPTE-THVVTalSLPGDPAAWpaPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 420 QRPDATDE-IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGS 492
Cdd:cd17651 353 NRPELTAErFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 493 SGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17651 433 GEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-551 |
2.49e-49 |
|
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: 176.35 E-value: 2.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQ-LGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYTPRELEHQLNDSGASAIVIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTDS-------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 rsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTALPLYHIFALT 266
Cdd:cd17653 104 ------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLD--VGPGSRVAQVLSIAFDACIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 267 I-NCLLFielgGQNLLITNPRDipglvkelakyPF-TAITGVNTL-----FNALLNNKEFQQLDFSSLhlsagGGMPVQQ 339
Cdd:cd17653 164 IfSTLCN----GGTLVLADPSD-----------PFaHVARTVDALmstpsILSTLSPQDFPNLKTIFL-----GGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 340 VVAERWVKltGQYLLEGYGLTECAPLVSVNPYDIDYHSgSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYW 419
Cdd:cd17653 224 SLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 420 QRPDATDEIIK-----NGWLH--TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HPGVQEVAAVgvpsg 491
Cdd:cd17653 301 GNPALTASKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI----- 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 492 SSGEAVKIFVVKKdpSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17653 376 VVNGRLVAFVTPE--TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-483 |
1.63e-48 |
|
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: 176.64 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFA-AYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLY---TPRELEHQLNDSGASA 124
Cdd:cd05927 6 ISYKEVAERADNIGsALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 125 IVIVSNFA-HTLEKVVDktavqhviltrMGDQlstAKGTVVnfvvkyikrlVPKyhlpdaisfrsalhngyrmqyvkpel 203
Cdd:cd05927 83 VFCDAGVKvYSLEEFEK-----------LGKK---NKVPPP----------PPK-------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 vPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELV-VTALPLYHIF-ALTINCLLFIelGGQnll 281
Cdd:cd05927 113 -PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyISYLPLAHIFeRVVEALFLYH--GAK--- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 282 ITNPR-DIPGLVKELAKYPFTAITGV----------------------NTLFNALLNNKE-------------FQQLDFS 325
Cdd:cd05927 187 IGFYSgDIRLLLDDIKALKPTVFPGVprvlnriydkifnkvqakgplkRKLFNFALNYKLaelrsgvvraspfWDKLVFN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 326 SLHLSAG--------GGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVN-PYDIDYhsGSIGLPVPSTEAKLVDddd 396
Cdd:cd05927 267 KIKQALGgnvrlmltGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTlPGDTSV--GHVGGPLPCAEVKLVD--- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 397 neVP--------PGQPGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVY 466
Cdd:cd05927 342 --VPemnydakdPNPRGEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVA 419
|
490
....*....|....*..
gi 1728558706 467 PNEIEDVVMQHPGVQEV 483
Cdd:cd05927 420 PEKIENIYARSPFVAQI 436
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
30-550 |
2.89e-48 |
|
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: 177.30 E-value: 2.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 30 EQSVARYADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:cd05968 68 DKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NPLYTPRELEHQLNDSGASAIVIVSNFAH-----TLEKVVDKTA-----VQHVILTRMGDQLSTAkgTVVNFVvkyikrl 174
Cdd:cd05968 147 FSGFGKEAAATRLQDAEAKALITADGFTRrgrevNLKEEADKACaqcptVEKVVVVRHLGNDFTP--AKGRDL------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 vpKYHLPDAISFRSAlhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlanleqvnatygpllhPGKelvv 254
Cdd:cd05968 218 --SYDEEKETAGDGA-----------ERTESEDPLMIIYTSGTTGKPKGTVHVHAGF----------------PLK---- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 255 TALPLYHIFALTINCLLF-----------------IELGGQNLLITNPRDIPG---LVKELAKYPFTAITGVNTLFNALL 314
Cdd:cd05968 265 AAQDMYFQFDLKPGDLLTwftdlgwmmgpwlifggLILGATMVLYDGAPDHPKadrLWRMVEDHEITHLGLSPTLIRALK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 315 NNKE--FQQLDFSSLHLSAGGGMPVQqvvAERWvkltgQYLLEGYGLTECaPLvsvnpydIDYHSG-------------- 378
Cdd:cd05968 345 PRGDapVNAHDLSSLRVLGSTGEPWN---PEPW-----NWLFETVGKGRN-PI-------INYSGGteisggilgnvlik 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 379 -----SIGLPVPSTEAKLVDDDDNEVPPgQPGELCVKGPQVML--GYWQRPDATDEI----IKNGWLHtGDIAVMDEEGF 447
Cdd:cd05968 409 pikpsSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWPGMtrGFWRDEDRYLETywsrFDNVWVH-GDFAYYDEEGY 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-----PSLTEEsLVTFCRRQLT 522
Cdd:cd05968 487 FYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEALAEE-LMERVADELG 565
|
570 580
....*....|....*....|....*...
gi 1728558706 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05968 566 KPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-547 |
3.73e-48 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 175.46 E-value: 3.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAFVNMGE--VMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 102 VNVNPLYTPRELEHQLNDSGASAIVIVSNFAHtleKVVDKTAVQHVILTRMGDQLSTAKGTvvnfvvkyikrlvPKYHLP 181
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPH---DRAEPTTRWWPLTVNVGGDSGPSGGT-------------LSVHLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 182 DAI--SFRSALHNGYRmqyvkpelvPEDlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVVTALPL 259
Cdd:PRK05852 160 AATepTPATSTPEGLR---------PDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR--LSPR-DATVAVMPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 260 YHIFALTINCLLFIELGGQNLLITNPR-DIPGLVKELAKYPFTAITGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMP 336
Cdd:PRK05852 227 YHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLEraATEPSGRKPAALRFIRSCSAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 337 VQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHS----GSIGLPVPSTEA--KLVDDDDNEVPPGQPGELCVK 410
Cdd:PRK05852 307 LTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvVSTGLVGRSTGAqiRIVGSDGLPLPAGAVGEVWLR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 411 GPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPS 490
Cdd:PRK05852 387 GTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPD 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 491 GSSGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRR 547
Cdd:PRK05852 467 QLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
1.08e-47 |
|
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: 171.93 E-value: 1.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLYT---PRELEHQLNDSGASAI 125
Cdd:cd05973 1 LTFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEkvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvp 205
Cdd:cd05973 77 VTDAANRHKLD--------------------------------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHPGKELVVTALP--LYHIFALTINCLLfieLGGQNLLIT 283
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAVDLRPEDSFWNAADPgwAYGLYYAITGPLA---LGHPTILLE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPRDIPGLVKELAKYPFTAITGVNTLFNALL-NNKEFQQLDFSSLHLSAGGGMPVQQVVAeRWVKLT-GQYLLEGYGLTE 361
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTAYRLLMaAGAEVPARPKGRLRRVSSAGEPLTPEVI-RWFDAAlGVPIHDHYGQTE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 362 CAPLVSVNPYDID-YHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVML----GYWQRPDATdeiIKNGWLHT 436
Cdd:cd05973 242 LGMVLANHHALEHpVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPA---IDGGYYLT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 437 GDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-----KKDPSLTEE 511
Cdd:cd05973 319 GDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPALADE 398
|
490 500 510
....*....|....*....|....*....|....*....
gi 1728558706 512 sLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05973 399 -LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
27-549 |
1.38e-45 |
|
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: 166.34 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYTPRELEHQLNDSGASaivivsnfahtlekvvdktavqhVILTRmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd12115 82 AYPPERLRFILEDAQAR-----------------------LVLTD----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 rsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllhPGKEL--VVTA------LP 258
Cdd:cd12115 104 ------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAF-----SAEELagVLAStsicfdLS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHIFAlTINCllfielGGQNLLITNPRDIPGLVkelAKYPFTAITGVNTLFNALLNNKEFQQlDFSSLHLsAGGGMPvQ 338
Cdd:cd12115 161 VFELFG-PLAT------GGKVVLADNVLALPDLP---AAAEVTLINTVPSAAAELLRHDALPA-SVRVVNL-AGEPLP-R 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 339 QVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYH-SGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLG 417
Cdd:cd12115 228 DLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASgEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDE-IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPS 490
Cdd:cd12115 308 YLGRPGLTAErFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGD 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 491 GSSGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12115 388 AAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
28-549 |
2.27e-44 |
|
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: 164.04 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 28 MFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDSGASAIVivsnfahTLEKVVDKTA-VQHVILTrmgDQLSTAKGTVVNFvvkyikrlvpkyhlpdaisf 186
Cdd:cd17655 81 YPEERIQYILEDSGADILL-------TQSHLQPPIAfIGLIDLL---DEDTIYHEESENL-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 187 rsalhngyrmqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHPGKELVVTALPLYHiFALT 266
Cdd:cd17655 131 -------------EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI----YQGEHLRVALFASIS-FDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 267 INCLLFIELGGQNLLITnPR----DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLhLSAGGGMPvqQVVA 342
Cdd:cd17655 193 VTEIFASLLSGNTLYIV-RKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL-IVGGEALS--TELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 343 ERWVKLTGQ--YLLEGYGLTE---CAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLG 417
Cdd:cd17655 269 KKIIELFGTnpTITNAYGPTEttvDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDE-IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGVPS 490
Cdd:cd17655 349 YLNRPELTAEkFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE-AVVIARK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 491 GSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17655 428 DEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
50-545 |
2.98e-44 |
|
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: 165.44 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:cd17634 86 SYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAH-----TLEKVVDK------TAVQHVI-LTRMGDQLSTAKGTVVNfvvkyikrlvpkYHlpDAISFRSALHNGYRMQ 197
Cdd:cd17634 165 GGVRagrsvPLKKNVDDalnpnvTSVEHVIvLKRTGSDIDWQEGRDLW------------WR--DLIAKASPEHQPEAMN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtYGPLLHPGkELVVTALPL-------YHIFALTIncl 270
Cdd:cd17634 231 -------AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMK-YVFDYGPG-DIYWCTADVgwvtghsYLLYGPLA--- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 271 lfieLGGQNLLITNPRDIPG---LVKELAKYPFTAITGVNTLFNALL--NNKEFQQLDFSSLHLSAGGGMPVQQVVAERW 345
Cdd:cd17634 299 ----CGATTLLYEGVPNWPTparMWQVVDKHGVNILYTAPTAIRALMaaGDDAIEGTDRSSLRILGSVGEPINPEAYEWY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 346 VKLTGQY---LLEGYGLTECA-PLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKG--PQVMLGYW 419
Cdd:cd17634 375 WKKIGKEkcpVVDTWWQTETGgFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDpwPGQTRTLF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 420 QRPDATDEI----IKNGWLHtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE 495
Cdd:cd17634 455 GDHERFEQTyfstFKGMYFS-GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQ 533
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1728558706 496 AVKIFVVKK-----DPSLTEEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:cd17634 534 APYAYVVLNhgvepSPELYAE-LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
38-550 |
1.16e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 162.26 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLglKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKE--SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVIvsnfahtlekvvdktavqhviLTRMGDQLSTAKGTVVNfvVKYIKRLVPKYhLPDAISFRSALHNGYRMQ 197
Cdd:PRK07638 94 AISNADMIVT---------------------ERYKLNDLPDEEGRVIE--IDEWKRMIEKY-LPTYAPIENVQNAPFYMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 YvkpelvpedlaflqyTGGTTGVAKGAMLTHRNMLANLeQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFielgG 277
Cdd:PRK07638 150 F---------------TSGSTGKPKAFLRAQQSWLHSF-DCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYV----G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 QNLLITnPRDIPGLVKE-LAKYPFTAITGVNTLFNALLNNKEFqqLDFSSLHLSAGGGMPVQQV--VAERWVKLTgqyLL 354
Cdd:PRK07638 210 QTVHLM-RKFIPNQVLDkLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGAKWEAEAKekIKNIFPYAK---LY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 355 EGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWL 434
Cdd:PRK07638 284 EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 435 HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEavkIFVVKKDPSLTEESLV 514
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE---KPVAIIKGSATKQQLK 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 1728558706 515 TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07638 441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-546 |
1.27e-43 |
|
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: 157.95 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 213 YTGGTTGVAKGAMLTHRNMLANLEqVNATygpLLHPGKELVVTAL-PLYHifALTINCLLFIELGGQNLLITNPRDIPGL 291
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFV-CNED---LFNISGEDAILAPgPLSH--SLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 292 VKELAKYPFTAITGVNTLFNALLNNkEFQQLDFSSLhLSAGGGMP--VQQVVAERWVKLTgqyLLEGYGLTEcAPLVSVN 369
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFesTKKKLKNIFPKAN---LIEFYGTSE-LSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 370 PYDIDYHSGSIGLPVPSTEAKLVDDDDNEVppgqpGELCVKGPQVMLGYWQrpdaTDEIIKNGWLHTGDIAVMDEEGFLR 449
Cdd:cd17633 155 FNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVR----GGFSNPDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVkIFVVKKDpSLTEESLVTFCRRQLTGYKVPKL 529
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*..
gi 1728558706 530 VEFRDELPKSNVGKILR 546
Cdd:cd17633 304 IIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-549 |
1.43e-43 |
|
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: 160.94 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLR-AEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIvivsnfahtlekvvdktavqhviLTRmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd17643 81 ADSGPSLL-----------------------LTD---------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY------------------------GPLLHpGKELV 253
Cdd:cd17643 92 -------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgfneddvwtlfhsyafdfsvweiwGALLH-GGRLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 254 VtalPLYHIfALTincllfielggqnllitnPRDIPGLVKElakypfTAITGVN---TLFNALLNNKEFQQLDFSSLHLS 330
Cdd:cd17643 164 V---VPYEV-ARS------------------PEDFARLLRD------EGVTVLNqtpSAFYQLVEAADRDGRDPLALRYV 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 331 AGGGMPVQQVVAERWVK---LTGQYLLEGYGLTECAPLVS---VNPYDIDYHSGS-IGLPVPSTEAKLVDDDDNEVPPGQ 403
Cdd:cd17643 216 IFGGEALEAAMLRPWAGrfgLDRPQLVNMYGITETTVHVTfrpLDAADLPAAAASpIGRPLPGLRVYVLDADGRPVPPGV 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 404 PGELCVKGPQVMLGYWQRPDATDE-IIKNGW-------LHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:cd17643 296 VGELYVSGAGVARGYLGRPELTAErFVANPFggpgsrmYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALA 375
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 476 QHPGVQEvAAVGVPSGSSGEA--VKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17643 376 THPSVRD-AAVIVREDEPGDTrlVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
46-553 |
2.68e-43 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 162.66 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:PLN02860 30 NRRRTGHEFVDGVLSLAAGLLR-LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVML 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEKVvDKTAVQHVILTRMGDQLSTAKGTVVNFVVK--YIKRLVPKYHLPDaisfrsalhngyrmqyvkPEL 203
Cdd:PLN02860 109 VTDETCSSWYEEL-QNDRLPSLMWQVFLESPSSSVFIFLNSFLTteMLKQRALGTTELD------------------YAW 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNM----LANLEQVNatYGP---LLHpgkelvvTAlPLYHIFALTiNCLLFIELG 276
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAIVG--YGEddvYLH-------TA-PLCHIGGLS-SALAMLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLItnPR-DIPGLVKELAKYPFTAITGVNTLFNALL--NNKEFQQLDFSSLH--LSAGGGMPVQQVVAERWVkLTGQ 351
Cdd:PLN02860 239 ACHVLL--PKfDAKAALQAIKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRkiLNGGGSLSSRLLPDAKKL-FPNA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTE-CAPLVSVNPYDID---------------------YHSGSIGLPVPSTEAKLVDDDDNEVppgqpGELCV 409
Cdd:PLN02860 316 KLFSAYGMTEaCSSLTFMTLHDPTlespkqtlqtvnqtksssvhqPQGVCVGKPAPHVELKIGLDESSRV-----GRILT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 410 KGPQVMLGYWQRPDATDEIIKN-GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PLN02860 391 RGPHVMLGYWGQNSETASVLSNdGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 489 PSGSSGEAVKIFV---------------VKKDPSLTEESLVTFCRRQ-LTGYKVPKL-VEFRDELPKSNVGKILRRELRD 551
Cdd:PLN02860 471 PDSRLTEMVVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREKnLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
..
gi 1728558706 552 EA 553
Cdd:PLN02860 551 EV 552
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-552 |
1.29e-42 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 160.30 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:PRK06018 41 TYAQIHDRALKVSQALD-RDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVDKTAvqhviltrmgdqlstakgTVVNFVVKYIKRLVPKYHLPDAISFRSAL--HNGYrmqyVKPELVPED 207
Cdd:PRK06018 120 TFVPILEKIADKLP------------------SVERYVVLTDAAHMPQTTLKNAVAYEEWIaeADGD----FAWKTFDEN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 208 LAF-LQYTGGTTGVAKGAMLTHR-NMLANLEQVNAtyGPLLHPGKELVVTALPLYHIFA--LTINCllfiELGGQNLLIT 283
Cdd:PRK06018 178 TAAgMCYTSGTTGDPKGVLYSHRsNVLHALMANNG--DALGTSAADTMLPVVPLFHANSwgIAFSA----PSMGTKLVMP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPRDIPGLVKEL---AKYPFTAitGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLT 360
Cdd:PRK06018 252 GAKLDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 361 ECAPLVSVN---------PYD--IDyHSGSIGLPVPSTEAKLVDDDDNEVP-PGQ-PGELCVKGPQVMLGYWQrpdATDE 427
Cdd:PRK06018 329 EMSPLGTLAalkppfsklPGDarLD-VLQKQGYPPFGVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYR---VDGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 428 II-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE-AVKIFVVKKD 505
Cdd:PRK06018 405 ILdDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErPLLIVQLKPG 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1728558706 506 PSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06018 485 ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
50-557 |
3.02e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 159.10 E-value: 3.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:PRK07008 41 TYRDCERRAKQLAQALA-ALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVvdktavqhviltrmGDQLSTAKGTVVnfvvkyikrLVPKYHLP-DAISFRS--ALHNGYRMQYVKPELVPE 206
Cdd:PRK07008 120 TFLPLVDAL--------------APQCPNVKGWVA---------MTDAAHLPaGSTPLLCyeTLVGAQDGDYDWPRFDEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNmlanleQVNATYGPLLhP------GKELVVTALPLYHIFALTINclLFIELGGQNL 280
Cdd:PRK07008 177 QASSLCYTSGTTGNPKGALYSHRS------TVLHAYGAAL-PdamglsARDAVLPVVPMFHVNAWGLP--YSAPLTGAKL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 281 LITNPrDIPGL-VKEL---AKYPFTAitGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEG 356
Cdd:PRK07008 248 VLPGP-DLDGKsLYELieaERVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 357 YGLTECAPLVSVN---------PYDIDYHS-GSIGLPVPSTEAKLVDDDDNEVP-PGQP-GELCVKGPQVMLGYWQRpda 424
Cdd:PRK07008 325 WGMTEMSPLGTLCklkwkhsqlPLDEQRKLlEKQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG--- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 425 TDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKK 504
Cdd:PRK07008 402 DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKR 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 505 -DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKV 557
Cdd:PRK07008 482 pGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRDYV 535
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
6-473 |
3.76e-42 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 160.65 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 6 LNRYPaDVPtEInpdryQSLVDMFEQSVARYADQPAFVN-------MGEV--MTFRKLEERSRAFAAYLQQgLGLKKGDR 76
Cdd:PLN02736 34 VSRFP-DHP-EI-----GTLHDNFVYAVETFRDYKYLGTrirvdgtVGEYkwMTYGEAGTARTAIGSGLVQ-HGIPKGAC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 77 VALMMPNLLQYPVALFGILRAGMIVVnvnPLYtprelehqlnDS-GASAIVIVSNFAhTLEKVVDKTAVQHVILTRMGdQ 155
Cdd:PLN02736 106 VGLYFINRPEWLIVDHACSAYSYVSV---PLY----------DTlGPDAVKFIVNHA-EVAAIFCVPQTLNTLLSCLS-E 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 156 LSTAKGTVVnfvVKYIKRLVPKyhLPDAISFR----SALHNGYRMQ---YVKPElvPEDLAFLQYTGGTTGVAKGAMLTH 228
Cdd:PLN02736 171 IPSVRLIVV---VGGADEPLPS--LPSGTGVEivtySKLLAQGRSSpqpFRPPK--PEDVATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 229 RNMLANLeqVNATYGPLLHPGkELVVTALPLYHIFAlTINCLLFIELG-------GQNLLITNprDIPGL-------VKE 294
Cdd:PLN02736 244 GNLIANV--AGSSLSTKFYPS-DVHISYLPLAHIYE-RVNQIVMLHYGvavgfyqGDNLKLMD--DLAALrptifcsVPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 295 LAKYPFTAIT-GVNT-------LFNALLNNKE------------FQQLDFSSLHLSAGGGM--------PVQQVVAERWV 346
Cdd:PLN02736 318 LYNRIYDGITnAVKEsgglkerLFNAAYNAKKqalengknpspmWDRLVFNKIKAKLGGRVrfmssgasPLSPDVMEFLR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 347 KLTGQYLLEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVD-------DDDNEVPPGqpgELCVKGPQVMLGYW 419
Cdd:PLN02736 398 ICFGGRVLEGYGMTETSCVISGMDEG-DNLSGHVGSPNPACEVKLVDvpemnytSEDQPYPRG---EICVRGPIIFKGYY 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 420 QRPDATDEIIKN-GWLHTGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDV 473
Cdd:PLN02736 474 KDEVQTREVIDEdGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-546 |
6.30e-42 |
|
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: 153.96 E-value: 6.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQvnatygpLLHPGKELVV-----TALPLYHIFAL--TINCLLF---IEL 275
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVgdvtyLPLPATHIGGLwwILTCLIHgglCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 276 GGQNLLITNprdipgLVKELAKYPFTAITGVNTLFNALLN-----NKEFQQLDFsslhLSAGGGMPVQQVVAE-RWVKLT 349
Cdd:cd17635 74 GGENTTYKS------LFKILTTNAVTTTCLVPTLLSKLVSelksaNATVPSLRL----IGYGGSRAIAADVRFiEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 350 GqyLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEII 429
Cdd:cd17635 144 N--TAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVK---KDP 506
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1728558706 507 SLTEESLVTFcRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17635 302 NAIRALKHTI-RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-549 |
6.97e-42 |
|
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: 157.05 E-value: 6.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLStakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPP---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHPGKELVVTA-------LPLYHIFALTincl 270
Cdd:cd12114 121 ---VDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF----AVGPDDRVLAlsslsfdLSVYDIFGAL---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 271 lfiELGGQNLLITNPRDI-PGLVKELA-KYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MPVQQvvAERWV 346
Cdd:cd12114 190 ---SAGATLVLPDEARRRdPAHWAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDL--PARLR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 347 KLTGQYLLEGYG-LTECA------PLVSVNPYDidyhsGSI--GLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLG 417
Cdd:cd12114 265 ALAPDARLISLGgATEASiwsiyhPIDEVPPDW-----RSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDE---IIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGs 492
Cdd:cd12114 340 YLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP- 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 493 SGEAVKIFVV--KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12114 419 GGKRLAAFVVpdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-554 |
2.38e-41 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 156.93 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 12 DVPTeiNPDRYQSLVDMF--EQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYL-QQGLGLkkGDRVALMMPNLLQYP 88
Cdd:PLN02479 9 DLPK--NAANYTALTPLWflERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALaKRSIGP--GSTVAVIAPNIPAMY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 89 VALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVV------DKTAVQHVILTRMGDQLSTAKGT 162
Cdd:PLN02479 85 EAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALkilaekKKSSFKPPLLIVIGDPTCDPKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 163 vvnfvvkyikrlvpKYHLPD-AISFRSALHNGyrmqyvKPELV---PED----LAfLQYTGGTTGVAKGAMLTHRNMLan 234
Cdd:PLN02479 165 --------------QYALGKgAIEYEKFLETG------DPEFAwkpPADewqsIA-LGYTSGTTASPKGVVLHHRGAY-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 235 leqVNATYGPLLHPGKELVVT--ALPLYH------IFALTINCllfielgGQNLLItnpRDIP--GLVKELAKYPFTAIT 304
Cdd:PLN02479 222 ---LMALSNALIWGMNEGAVYlwTLPMFHcngwcfTWTLAALC-------GTNICL---RQVTakAIYSAIANYGVTHFC 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 305 GVNTLFNALLNN-KEFQQLDFSSL-HLSAGGGMPVQQVVAERWVKltGQYLLEGYGLTECAPLVSVNPYDIDYHSgsigL 382
Cdd:PLN02479 289 AAPVVLNTIVNApKSETILPLPRVvHVMTAGAAPPPSVLFAMSEK--GFRVTHTYGLSETYGPSTVCAWKPEWDS----L 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 383 PvPSTEAKL----------------VDDDDNEVPPGQP---GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMD 443
Cdd:PLN02479 363 P-PEEQARLnarqgvryiglegldvVDTKTMKPVPADGktmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 444 EEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKK------DPSLTEESLVTFC 517
Cdd:PLN02479 442 PDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKpgvdksDEAALAEDIMKFC 521
|
570 580 590
....*....|....*....|....*....|....*..
gi 1728558706 518 RRQLTGYKVPKLVEFrDELPKSNVGKILRRELRDEAR 554
Cdd:PLN02479 522 RERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAK 557
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-553 |
5.65e-41 |
|
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: 154.62 E-value: 5.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 27 DMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYtPRE-LEHQLNDSGASaIVIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdais 185
Cdd:cd05918 82 SH-PLQrLQEILQDTGAK-VVLTSS------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 186 frsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQvnatYGPLLHPGKELVVTA-------LP 258
Cdd:cd05918 105 -------------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALA----HGRALGLTSESRVLQfasytfdVS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 LYHIF-ALTINCLLFI--ELGGQNllitnprDIPGLVKELakypftaitGVNTLF-----NALLNNKefqqlDFSSLHLS 330
Cdd:cd05918 162 ILEIFtTLAAGGCLCIpsEEDRLN-------DLAGFINRL---------RVTWAFltpsvARLLDPE-----DVPSLRTL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 331 AGGGMPVQQVVAERWVKLTGqyLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTeAKLVDDDDNE--VPPGQPGELC 408
Cdd:cd05918 221 VLGGEALTQSDVDTWADRVR--LINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHDrlVPIGAVGELL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 409 VKGPQVMLGYWQRPDATDEI-IKN-GWLH------------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:cd05918 298 IEGPILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 475 MQHPGVQEVAAVGV-----------------PSGSSGEAVKIFVVKKDPSLTEESLVT----FCRRQLTGYKVPKLVEFR 533
Cdd:cd05918 378 RQSLPGAKEVVVEVvkpkdgssspqlvafvvLDGSSSGSGDGDSLFLEPSDEFRALVAelrsKLRQRLPSYMVPSVFLPL 457
|
570 580
....*....|....*....|
gi 1728558706 534 DELPKSNVGKILRRELRDEA 553
Cdd:cd05918 458 SHLPLTASGKIDRRALRELA 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-544 |
1.58e-40 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 157.43 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQGLGLkkGDRVALMMPNLLQYPVALFGILRAGMIVVnvnplytprelehQLNDSGASAI 125
Cdd:PRK06814 656 NGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPA-------------MINFSAGIAN 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEKVVdkTAVQHVILTRMGDqLSTAKGTVVNFVvkYIKRLVPKYHLPDAISfrsALHNGYRMQYVKPELVP 205
Cdd:PRK06814 721 ILSACKAAQVKTVL--TSRAFIEKARLGP-LIEALEFGIRII--YLEDVRAQIGLADKIK---GLLAGRFPLVYFCNRDP 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVVTALPLYHIFALTINCLLFIELGGQNLLITNP 285
Cdd:PRK06814 793 DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--FSPE-DKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSP 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 286 ---RDIPGLVKELAKypfTAITGVNTLFNALLNNKefQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEC 362
Cdd:PRK06814 870 lhyRIIPELIYDTNA---TILFGTDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTET 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 363 APLVSVN-PydIDYHSGSIGLPVPSTEAKLvddddnEVPPG--QPGELCVKGPQVMLGYWqRPDA--TDEIIKNGWLHTG 437
Cdd:PRK06814 945 APVIALNtP--MHNKAGTVGRLLPGIEYRL------EPVPGidEGGRLFVRGPNVMLGYL-RAENpgVLEPPADGWYDTG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 438 DIAVMDEEGFLRIVDRKK-------DMILVSGFNVYPNEIEdvvmqhPGVQEvAAVGVPSGSSGEavKIFVVKKDPSLTE 510
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKrfakiagEMISLAAVEELAAELW------PDALH-AAVSIPDARKGE--RIILLTTASDATR 1086
|
490 500 510
....*....|....*....|....*....|....*
gi 1728558706 511 ESLVTFCR-RQLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PRK06814 1087 AAFLAHAKaAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
24-552 |
4.46e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 154.50 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPA--FVNM-----GEV--MTFRKLEERSRAFAAYLQQGLglKKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAyrFLDFsterdGVArdLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 95 LRAGMIVVnvnPLYTPRELEHqlndsgasaivivsnfAHTLEKVVDKtAVQHVILTRMGdqlsTAKGtVVNFVvkyikRL 174
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDD-CTPSAILTTTD----SAEG-VRKFF-----RA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 VPKYHLPDAISFrSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV-NATYGPLLHPGkelv 253
Cdd:PRK07769 150 RPAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQViDALEGQEGDRG---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 254 VTALPLYHIFAL-TInclLFIELGGQNLLITNPRDI---PG-LVKELAKYPftaiTGVNTLFNALLN-----------NK 317
Cdd:PRK07769 225 VSWLPFFHDMGLiTV---LLPALLGHYITFMSPAAFvrrPGrWIRELARKP----GGTGGTFSAAPNfafehaaarglPK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 318 EFQQ-LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTECAPLVSVNPYD-------IDYHSGSIG-- 381
Cdd:PRK07769 298 DGEPpLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVSTTPMDeeptviyVDRDELNAGrf 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 382 LPVPSTE-----------------AKLVD-DDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKN------------ 431
Cdd:PRK07769 378 VEVPADApnavaqvsagkvgvsewAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshae 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 432 ------GWLHTGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-----HPGVqeVAAVGVPSGSSGEAV--- 497
Cdd:PRK07769 458 gapddaLWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYTAQEatkalRTGY--VAAFSVPANQLPQVVfdd 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 498 KIFVVKKDPSLTEESLVTFCRRQLTGYK---------------VPKLVEFRDEL-------PKSNVGKILRRELRDE 552
Cdd:PRK07769 535 SHAGLKFDPEDTSEQLVIVAERAPGAHKldpqpiaddiraaiaVRHGVTVRDVLlvpagsiPRTSSGKIARRACRAA 611
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
211-557 |
7.45e-40 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 152.87 E-value: 7.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 211 LQYTGGTTGVAKGAMLTHRNmlANLEQVNATYGPLLHPGKELVVTaLPLYHIFALTINCLLFIElGGQNLLITNPrDIPG 290
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWT-LPMFHCNGWTFTWGTAAR-GGTSVCMRHV-TAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 291 LVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSS-LHLSAGGGMPVQQVVAErwVKLTGQYLLEGYGLTECAPLVSVN 369
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGSPPPAALVKK--VQRLGFQVMHAYGLTEATGPVLFC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 370 PYDIDYHSgsigLPvPSTEAKL-------------VDDDDNEVPPGQP------GELCVKGPQVMLGYWQRPDATDEIIK 430
Cdd:PLN03102 344 EWQDEWNR----LP-ENQQMELkarqgvsilgladVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAFK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 431 NGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKK------ 504
Cdd:PLN03102 419 HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgettk 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 505 ----DPSLTEE-SLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKV 557
Cdd:PLN03102 499 edrvDKLVTRErDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLV 556
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-558 |
1.44e-39 |
|
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: 152.72 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAF------VNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd05966 63 LKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKS-LGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 107 LYTPRELEHQLNDSGASAIVIVSNF-----AHTLEKVVDK-----TAVQHVI-LTRMGDQLSTAKGtvVNFVVKYIKRLV 175
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGGyrggkVIPLKEIVDEalekcPSVEKVLvVKRTGGEVPMTEG--RDLWWHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 176 PKYHLPDAISfrsalhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKG-----------AMLTHRNML-----------A 233
Cdd:cd05966 220 SPECEPEWMD-------------------SEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVFdyhpddiywctA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 234 NLEQVNA----TYGPLLHPGKELVVTALPLYHIFALTINcllFIELGGQNLLITNPRDIPGLVKELAKYPftaitgvntl 309
Cdd:cd05966 281 DIGWITGhsyiVYGPLANGATTVMFEGTPTYPDPGRYWD---IVEKHKVTIFYTAPTAIRALMKFGDEWV---------- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 310 fnallnnkefQQLDFSSLHLSAGGGMPVQ----------------QVVAERWVKLTGQYLLegygltecAPLvsvnPYDI 373
Cdd:cd05966 348 ----------KKHDLSSLRVLGSVGEPINpeawmwyyevigkercPIVDTWWQTETGGIMI--------TPL----PGAT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 374 DYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGP-QVML------------GYWQRpdatdeiiKNGWLHTGDIA 440
Cdd:cd05966 406 PLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwPGMArtiygdheryedTYFSK--------FPGYYFTGDGA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 441 VMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD-----PSLTEEsLVT 515
Cdd:cd05966 478 RRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepsDELRKE-LRK 556
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1728558706 516 FCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKVD 558
Cdd:cd05966 557 HVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAAGEEE 599
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-556 |
1.93e-39 |
|
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: 152.47 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGaSAIVIVS 129
Cdd:cd05967 84 TYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAK-PKLIVTA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVD-KTAVQHVIltrmgdQLSTAKGTVVNFVVKYIKRLVPKYHLPDaISFRSALHNGYRMQYVKPElvPEDL 208
Cdd:cd05967 162 SCGIEPGKVVPyKPLLDKAL------ELSGHKPHHVLVLNRPQVPADLTKPGRD-LDWSELLAKAEPVDCVPVA--ATDP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 AFLQYTGGTTGVAKG--------AMLTHRNMlANLEQVNA-------------------TYGPLLHPGKELVVTALPLYH 261
Cdd:cd05967 233 LYILYTSGTTGKPKGvvrdngghAVALNWSM-RNIYGIKPgdvwwaasdvgwvvghsyiVYGPLLHGATTVLYEGKPVGT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 262 ifaltincllfielggqnllitnPrDIPGLVKELAKYPFTAITGVNTLFNAL----LNNKEFQQLDFSSL-HLSAGGgmp 336
Cdd:cd05967 312 -----------------------P-DPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLrTLFLAG--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 337 vqqvvaER-------WV-KLTGQYLLEGYGLTECAPLVSVNPYDIDYHS---GSIGLPVPSTEAKLVDDDDNEVPPGQPG 405
Cdd:cd05967 365 ------ERldpptleWAeNTLGVPVIDHWWQTETGWPITANPVGLEPLPikaGSPGKPVPGYQVQVLDEDGEPVGPNELG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 406 ELCVKGP---QVMLGYWQRPDATDEIIKN---GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPG 479
Cdd:cd05967 439 NIVIKLPlppGCLLTLWKNDERFKKLYLSkfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPA 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 480 VQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFC----RRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:cd05967 519 VAECAVVGVRDELKGQVPLGLVVlKEGVKITAEELEKELvalvREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIAD 598
|
..
gi 1728558706 555 GK 556
Cdd:cd05967 599 GE 600
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
35-501 |
2.05e-38 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 149.00 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 35 RYADQPAFV--------------------NMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK09192 16 RYADFPTLVealdyaalgeagmnfydrrgQLEEALPYQTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 95 LRAGMIVVnvnPLYTP-----RE-----LEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHViltrmgdqlstakGTVV 164
Cdd:PRK09192 95 QYAGLVPV---PLPLPmgfggREsyiaqLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHV-------------LSHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 165 NFvvkyikrlvpkyHLPDAIsfRSALhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYGP 244
Cdd:PRK09192 159 WF------------KALPEA--DVAL----------PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL-RAISHDGL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 245 LLHPGkELVVTALPLYHIFALtINCLLFIeLGGQ---NLLITNprdipglvkELAKYPF---------TAITGVNTLFNA 312
Cdd:PRK09192 214 KVRPG-DRCVSWLPFYHDMGL-VGFLLTP-VATQlsvDYLPTR---------DFARRPLqwldlisrnRGTISYSPPFGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 313 LL-----NNKEFQQLDFSSLHLSAGGG----MPVQQVVAERW--VKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSI- 380
Cdd:PRK09192 282 ELcarrvNSKDLAELDLSCWRVAGIGAdmirPDVLHQFAEAFapAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVd 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 381 --------------------------GLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWL 434
Cdd:PRK09192 362 rdrleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWL 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 435 HTGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQ--EVAAVGVPSGsSGEAVKIFV 501
Cdd:PRK09192 442 DTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLV 508
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
28-549 |
2.09e-38 |
|
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: 146.55 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 28 MFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDSGASaiVIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfr 187
Cdd:cd17645 82 YPGERIAYMLADSSAK--ILLTN--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 188 salhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHPGKELVVTALPlYHIFALTI 267
Cdd:cd17645 103 -----------------PDDLAYVIYTSGSTGLPKGVMIEHHN-LVNLCEWHRPYFGVTPADKSLVYASFS-FDASAWEI 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 NCLLFIelgGQNLLITnPRDIPGLVKELAKYPFTaiTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAErwvk 347
Cdd:cd17645 164 FPHLTA---GAALHVV-PSERRLDLDALNDYFNQ--EGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK---- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 ltGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE 427
Cdd:cd17645 234 --GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAE 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 428 -IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIF 500
Cdd:cd17645 312 kFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAY 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1728558706 501 VVKKDpSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17645 392 VTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-487 |
2.70e-38 |
|
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: 147.62 E-value: 2.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVivs 129
Cdd:cd05932 8 TWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 nfahtLEKVVDKTAVQHVILTRMgdqlstakgtvvnfvvkyIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLA 209
Cdd:cd05932 84 -----VGKLDDWKAMAPGVPEGL------------------ISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVVTALPLYHIFALTincllFIELGG--QNLLITNPRD 287
Cdd:cd05932 141 TLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGT---EENDRMLSYLPLAHVTERV-----FVEGGSlyGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 288 IPGLVKELAKYPFTAITGVN---TLF----------------------NALLNNKEFQQLDFSSLHLSAGGGMPVQQVVA 342
Cdd:cd05932 213 LDTFVEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkipvvNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 343 ErWVKLTGQYLLEGYGLTE-CAplVSVNPYDIDYHSGSIGLPVPSTEAKLVDDddnevppgqpGELCVKGPQVMLGYWQR 421
Cdd:cd05932 293 E-WYRSLGLNILEAYGMTEnFA--YSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKD 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 422 PDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:cd05932 360 PEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
17-553 |
3.63e-38 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 148.48 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 17 INPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAA-RGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 97 AGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLsTAKGTVVNFvvkyikrlvp 176
Cdd:PRK08279 110 LGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTL-DDPEGYEDL---------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 177 kyhlpDAISFRSALHNgyrmQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPLLHPGKELVV-T 255
Cdd:PRK08279 179 -----AAAAAGAPTTN----PASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAM----GGFGGLLRLTPDDVLyC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 256 ALPLYHIFALTInCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGM 335
Cdd:PRK08279 246 CLPLYHNTGGTV-AWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGNGL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 336 PvqqvvAERWVKLTGQY----LLEGYGLTECaplvSVNPYDIDYHSGSIGLpVPS--------------TEAKLVDDDDN 397
Cdd:PRK08279 325 R-----PDIWDEFQQRFgiprILEFYAASEG----NVGFINVFNFDGTVGR-VPLwlahpyaivkydvdTGEPVRDADGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 398 --EVPPGQPGELC--VKGPQVMLGYWQrPDATDE-IIKNG------WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVY 466
Cdd:PRK08279 395 ciKVKPGEVGLLIgrITDRGPFDGYTD-PEASEKkILRDVfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 467 PNEIEDVVMQHPGVQEVAAVGVP-SGSSGEA--VKIfVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVEvPGTDGRAgmAAI-VLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFK 552
|
570
....*....|
gi 1728558706 544 ILRRELRDEA 553
Cdd:PRK08279 553 YRKVDLRKEG 562
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
24-548 |
4.16e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 147.78 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAFVNM---------GEVMTFRKLEERSRAFAAYLQQgLGlKKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIdyeqdpagvAETLTWSQLYRRTLNVAEELRR-HG-STGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 95 LRAGMIVVnvnPLYTPRELEHqlnDSGASAIVivsnfahtlekvVDKTAVqhVILTRmgdqlSTAKGTVVNFVVKYIKRL 174
Cdd:PRK05850 80 LQAGLIAV---PLSVPQGGAH---DERVSAVL------------RDTSPS--VVLTT-----SAVVDDVTEYVAPQPGQS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 VPKYHLPDAISFRSALhngyrmqyvKPELVPEDL---AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpLLHPGKE 251
Cdd:PRK05850 135 APPVIEVDLLDLDSPR---------GSDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY--FGDTGGV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 252 L-----VVTALPLYHIFALTINCLLFIeLGGQNLLITNP--------RdipgLVKELAKYP--FTAitGVNTLFNalLNN 316
Cdd:PRK05850 204 PppdttVVSWLPFYHDMGLVLGVCAPI-LGGCPAVLTSPvaflqrpaR----WMQLLASNPhaFSA--APNFAFE--LAV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 317 KEFQQLDFSSLHLSA-----GGGMPVQQVVAERWVKLTGQYLLE------GYGLTECAPLVSVNPY-------DIDYHSG 378
Cdd:PRK05850 275 RKTSDDDMAGLDLGGvlgiiSGSERVHPATLKRFADRFAPFNLRetairpSYGLAEATVYVATREPgqppesvRFDYEKL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 379 SIGLPVP----------------STEAKLVDDDDN-EVPPGQPGELCVKGPQVMLGYWQRPDATDEII------------ 429
Cdd:PRK05850 355 SAGHAKRcetgggtplvsygsprSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtp 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 KNGWLHTGDIAVMDeEGFLRIVDRKKDMILVSGFNVYPNEIEDVvmqhpgVQE-----VAAVGVPSGSSGEAVKIFVVKK 504
Cdd:PRK05850 435 EGPWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYPDDIEAT------IQEitggrVAAISVPDDGTEKLVAIIELKK 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 505 DPSLTEESLVTFC--RRQLT-------GYKVPKLVEF-RDELPKSNVGKILRRE 548
Cdd:PRK05850 508 RGDSDEEAMDRLRtvKREVTsaiskshGLSVADLVLVaPGSIPITTSGKIRRAA 561
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-549 |
5.90e-38 |
|
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: 145.09 E-value: 5.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGAsaivivsnfahtlekvvdktavqHVILTrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd17652 81 ADARP-----------------------ALLLT----------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLlHPGKELVVTALPLYHIFALTInCLLFieLGG 277
Cdd:cd17652 91 ------TPDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDV-GPGSRVLQFASPSFDASVWEL-LMAL--LAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 QNLLITNPRDI---PGLVKELAKYPFTAITGVNTLFNALlnnKEFQQLDFSSLhLSAGGGMPVQqvVAERWVKltGQYLL 354
Cdd:cd17652 160 ATLVLAPAEELlpgEPLADLLREHRITHVTLPPAALAAL---PPDDLPDLRTL-VVAGEACPAE--LVDRWAP--GRRMI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 355 EGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE-IIKN-- 431
Cdd:cd17652 232 NAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErFVADpf 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 432 ----GWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGVPSGSSGEA--VKIFVVKK 504
Cdd:cd17652 312 gapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKrlVAYVVPAP 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1728558706 505 DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17652 391 GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
47-558 |
6.83e-38 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 147.24 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 47 EVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIV 126
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 127 IVSNFAHTLEKVVDKT-AVQHVILTRMGDQLSTAKgtvvnfvvkyikrlvpkyHLPDAISFRS--ALHNGYRMQYVKPEL 203
Cdd:PRK05620 117 ADPRLAEQLGEILKECpCVRAVVFIGPSDADSAAA------------------HMPEGIKVYSyeALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVVTALPLYHIFALTINCLLFieLGGQNLLIT 283
Cdd:PRK05620 179 DETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHG-ESFLCCVPIYHVLSWGVPLAAF--MSGTPLVFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPR-DIPGLVKELA-KYPFTAiTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE 361
Cdd:PRK05620 256 GPDlSAPTLAKIIAtAMPRVA-HGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 362 CAPL--VSVNPydidyhSGSIG------------LPVpSTEAKLVDD-------DDNEvppgqpGELCVKGPQVMLGYWQ 420
Cdd:PRK05620 335 TSPVgtVARPP------SGVSGearwayrvsqgrFPA-SLEYRIVNDgqvmestDRNE------GEIQVRGNWVTASYYH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 421 RP-----------------DATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEV 483
Cdd:PRK05620 402 SPteegggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVEC 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 484 AAVGVPSGSSGE---AVKIFVVKKDPSL-TEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE-ARGKVD 558
Cdd:PRK05620 482 AVIGYPDDKWGErplAVTVLAPGIEPTReTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHlADGDFE 561
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-549 |
4.89e-37 |
|
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: 143.38 E-value: 4.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASaiVIVSNFAHTlekvvdktavqhviltrmgDQLSTAKGTVvnfvvkyikrlvpkyHLPDAISFRSALHNgyrmq 197
Cdd:cd17656 82 LDSGVR--VVLTQRHLK-------------------SKLSFNKSTI---------------LLEDPSISQEDTSN----- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMlANLEQVNATYGPLLHPGKELVVTALPL---YH-IFAltinCLLFi 273
Cdd:cd17656 121 -IDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM-VNLLHFEREKTNINFSDKVLQFATCSFdvcYQeIFS----TLLS- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 274 elGGQNLLITNP--RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSL-HLSAGGGM-----PVQQVVAERW 345
Cdd:cd17656 194 --GGTLYIIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVkHIITAGEQlvitnEFKEMLHEHN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 346 VKLTGQYlleGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDAT 425
Cdd:cd17656 272 VHLHNHY---GPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELT 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 426 -DEIIKNGW------LHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGVPSGSSGEAVK 498
Cdd:cd17656 349 aEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEKYL 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 499 IFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17656 428 CAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
32-556 |
4.96e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 145.94 E-value: 4.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 32 SVARYADQPAFVnMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPR 111
Cdd:PRK06060 15 SEAGWYDRPAFY-AADVVTHGQIHDGAARLGEVLRN-RGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 112 ELEHQLNDSgASAIVIVSNfahtleKVVDKTAVQHVIltRMGDQLSTAKgtvvnfvvkyikRLVPKYHLPdaisfrsalh 191
Cdd:PRK06060 93 DHALAARNT-EPALVVTSD------ALRDRFQPSRVA--EAAELMSEAA------------RVAPGGYEP---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 192 ngyrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV--NATYgplLHPgKELVVTALPLYHIFALTINC 269
Cdd:PRK06060 142 -----------MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrKALR---LTP-EDTGLCSARMYFAYGLGNSV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 270 LLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQldFSSLHLSAGGGMPVQQVVAERWVKLT 349
Cdd:PRK06060 207 WFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDS--FRSLRCVVSAGEALELGLAERLMEFF 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 350 GQY-LLEGYGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDA--TD 426
Cdd:PRK06060 285 GGIpILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSpvAN 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 427 EiiknGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP 506
Cdd:PRK06060 364 E----GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 507 SLTEESLVTFCRR----QLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK 556
Cdd:PRK06060 440 ATIDGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
49-458 |
5.63e-37 |
|
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: 143.51 E-value: 5.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVnplY-TPRE--LEHQLNDSGASAI 125
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVE-LGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV---YaTLGEdaLIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvP 205
Cdd:cd17639 82 FTDGK--------------------------------------------------------------------------P 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVVTALPLYHIFALTI-NCLLFIelGG------- 277
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAeNVCLYR--GGtigygsp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 QNLLITNPRDIPGLVKELAKYPFTAITGV-------------------NTLFNALLNNKEFQQLD-----------FSSL 327
Cdd:cd17639 165 RTLTDKSKRGCKGDLTEFKPTLMVGVPAIwdtirkgvlaklnpmgglkRTLFWTAYQSKLKALKEgpgtplldelvFKKV 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 328 H----------LSAGGGMPVQqvvAERWVKLTGQYLLEGYGLTE-CAPLVSVNPYDIDYhsGSIGLPVPSTEAKLVDDDD 396
Cdd:cd17639 245 RaalggrlrymLSGGAPLSAD---TQEFLNIVLCPVIQGYGLTEtCAGGTVQDPGDLET--GRVGPPLPCCEIKLVDWEE 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 397 ----NEVPPGQpGELCVKGPQVMLGYWQRPDATDEIIK-NGWLHTGDIAVMDEEGFLRIVDRKKDMI 458
Cdd:cd17639 320 ggysTDKPPPR-GEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
205-543 |
1.07e-35 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 142.16 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN--ATYGPllhpgKELVVTALPLYHIFALTINCLLFIELGGQNLLI 282
Cdd:PRK08043 364 PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKtiADFTP-----NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLY 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 283 TNP---RDIPGLVKELAkypFTAITGVNTLfnaLLNNKEFQQ-LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYG 358
Cdd:PRK08043 439 PSPlhyRIVPELVYDRN---CTVLFGTSTF---LGNYARFANpYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 359 LTECAPLVSVN-PydIDYHSGSIGLPVPSTEAKLVddddnEVPP-GQPGELCVKGPQVMLGY--------WQRPDATDE- 427
Cdd:PRK08043 513 VTECAPVVSINvP--MAAKPGTVGRILPGMDARLL-----SVPGiEQGGRLQLKGPNIMNGYlrvekpgvLEVPTAENAr 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 428 -IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVkkDP 506
Cdd:PRK08043 586 gEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DS 663
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1728558706 507 SLTEESLVTFCRR----QLTgykVPKLVEFRDELPKSNVGK 543
Cdd:PRK08043 664 ELTREKLQQYAREhgvpELA---VPRDIRYLKQLPLLGSGK 701
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
47-487 |
1.40e-35 |
|
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: 140.96 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 47 EVMTFRKLEERSRAFA-AYLQqgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASaI 125
Cdd:cd05933 7 HTLTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNfAHTLEKVvdkTAVQhviltrmgDQLSTAKGtvvnfVVKYikRLVPKYHLPDAISFR-----------SALHNgy 194
Cdd:cd05933 84 LVVEN-QKQLQKI---LQIQ--------DKLPHLKA-----IIQY--KEPLKEKEPNLYSWDefmelgrsipdEQLDA-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 195 RMQYVKPElvpeDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHP-GKELVVTALPLYHIFALTINCLLFI 273
Cdd:cd05933 143 IISSQKPN----QCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvGQESVVSYLPLSHIAAQILDIWLPI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 274 ELGGQnLLITNPRDIPG-LVKELAKYPFTAITGV---------------------------------------------- 306
Cdd:cd05933 219 KVGGQ-VYFAQPDALKGtLVKTLREVRPTAFMGVprvwekiqekmkavgaksgtlkrkiaswakgvgletnlklmggesp 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 307 ----NTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQyLLEGYGLTECAPLVSVNpYDIDYHSGSIGL 382
Cdd:cd05933 298 splfYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIP-IMELYGMSETSGPHTIS-NPQAYRLLSCGK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 383 PVPSTEAKLVDDDDNevppGQpGELCVKGPQVMLGYWQRPDATDEIIK-NGWLHTGDIAVMDEEGFLRIVDRKKDMILVS 461
Cdd:cd05933 376 ALPGCKTKIHNPDAD----GI-GEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITA 450
|
490 500
....*....|....*....|....*...
gi 1728558706 462 -GFNVYPNEIEDVV-MQHPGVQEVAAVG 487
Cdd:cd05933 451 gGENVPPVPIEDAVkKELPIISNAMLIG 478
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-549 |
3.25e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 142.22 E-value: 3.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 14 PTEINPDRYQSLvdmFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK12467 506 ATEYAPDCVHQL---IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLI-AAGVGPDVLVGIAVERSIEMVVGLLA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 94 ILRAGMIVVNVNPLYtPRE-LEHQLNDSGASAIVIVSnfaHTLEKVVDKTAVQHVILTRMGDQLSTAKGtvvnfvvkyik 172
Cdd:PRK12467 582 VLKAGGAYVPLDPEY-PQDrLAYMLDDSGVRLLLTQS---HLLAQLPVPAGLRSLCLDEPADLLCGYSG----------- 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 173 rlvpkyHLPDaisfrsalhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHPGKEL 252
Cdd:PRK12467 647 ------HNPE------------------VALDPDNLAYVIYTSGSTGQPKGVAISHGA-LANYVCVIAERLQLAADDSML 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 253 VVTAlPLYHIFALtincLLFIELG-GQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLdfSSLH 328
Cdd:PRK12467 702 MVST-FAFDLGVT----ELFGALAsGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQR 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 329 LSAGGGMPVQQVVAERWVKLT-GQYLLEGYGLTECAPLVSVNPY---DIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQP 404
Cdd:PRK12467 775 ALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYELsdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVV 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 405 GELCVKGPQVMLGYWQRPDAT------DEIIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK12467 855 GELYIGGAGLARGYHRRPALTaerfvpDPFGADGgrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLA 934
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 477 HPGVQEvAAVGVPSGSSGEAVKIFVVKK------DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12467 935 QPGVRE-AVVLAQPGDAGLQLVAYLVPAavadgaEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
3.45e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.02 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 7 NRYPADVPTEinpdryQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQ 86
Cdd:PRK12316 4541 NRTDAGYPAT------RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIA-RGVGPEVLVGIAMERSAE 4613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 87 YPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGASAIVIVSnfaHTLEKVVDKTAVQHVILTRMGDQlstakgtvvn 165
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEY-PRErLAYMMEDSGAALLLTQS---HLLQRLPIPDGLASLALDRDEDW---------- 4679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 166 fvvkyikrlvpkyhlpdaisfrsalhNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpL 245
Cdd:PRK12316 4680 --------------------------EGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE-L 4732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 246 LHPGKELVVTALPlyhiFALTINCLLFIELGGQNLLITNPR--DIPGLVKELAKYPFTAITGVNTLFNALLNNKEfQQLD 323
Cdd:PRK12316 4733 TPDDRVLQFMSFS----FDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGE 4807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 324 FSSLHLSAGGGMPVQQVVAER-WVKLTGQYLLEGYGLTECAPLVS---VNPYDIDYHSG-SIGLPVPSTEAKLVDDDDNE 398
Cdd:PRK12316 4808 PPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLlwkARDGDACGAAYmPIGTPLGNRSGYVLDGQLNP 4887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 399 VPPGQPGELCVKGPQVMLGYWQRPDATDEII-------KNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
Cdd:PRK12316 4888 LPVGVAGELYLGGEGVARGYLERPALTAERFvpdpfgaPGGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEI 4967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 471 EDVVMQHPGVQEVAAVGVPsGSSGEAVKIFVVKKDPSLTE---------ESLVTFCRRQLTGYKVPKLVEFRDELPKSNV 541
Cdd:PRK12316 4968 EARLREHPAVREAVVIAQE-GAVGKQLVGYVVPQDPALADadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPN 5046
|
....*...
gi 1728558706 542 GKILRREL 549
Cdd:PRK12316 5047 GKLDRKAL 5054
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-543 |
1.22e-34 |
|
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: 134.05 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLaFLQYTGGTTGVAKGAMLTH---RNML---ANLEQVNATYGPLLHPGKE-----LVVTALPLYHifALTINCLLFI 273
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQediFRMLmggADFGTGEFTPSEDAHKAAAaaagtVMFPAPPLMH--GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 274 ELGGQNLLITNPR-DIPGLVKELAKYPFTAITGVNT-----LFNALLNNKEFqqlDFSSLHLSAGGGMPVQQVVAERWVK 347
Cdd:cd05924 80 LLGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVGDamarpLIDALRDAGPY---DLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 LTGQ-YLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTeaKLVDDDDNEVPPGQPGE--LCVKGpQVMLGYWQRPDA 424
Cdd:cd05924 157 LVPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPPGSGGVgwIARRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 425 TDEIIK--NG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVkIF 500
Cdd:cd05924 234 TAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV-VA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1728558706 501 VVKKDP--SLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:cd05924 313 VVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
47-487 |
2.21e-34 |
|
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: 137.17 E-value: 2.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 47 EVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLlqyPVALFGILRAGMIVVNVNPLYT---PRELEHQLNDSGAS 123
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 124 AiVIVSNfahtlEKVVDKtavqhviLTRMGDQLSTakgtvVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPEL 203
Cdd:cd17641 86 V-VIAED-----EEQVDK-------LLEIADRIPS-----VRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 V--------PEDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYGPLlHPGKElVVTALPLYHI--FALTI------ 267
Cdd:cd17641 148 YerevaagkGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPL-GPGDE-YVSVLPLPWIgeQMYSVgqalvc 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 -NCLLFIELG----------GQNLLITNPRDIPGLVKEL-------------------------------AKYPFTAITG 305
Cdd:cd17641 225 gFIVNFPEEPetmmedlreiGPTFVLLPPRVWEGIAADVrarmmdatpfkrfmfelgmklglraldrgkrGRPVSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 306 VNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAeRWVKLTGQYLLEGYGLTECAPLVSVNP-YDIDYHSgsIGLPV 384
Cdd:cd17641 305 ASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRdGDVDPDT--VGVPF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 385 PSTEAKLvdddDNEvppgqpGELCVKGPQVMLGYWQRPDATDE-IIKNGWLHTGDIAVMDEEGFLRIVDRKKD-MILVSG 462
Cdd:cd17641 382 PGTEVRI----DEV------GEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSDG 451
|
490 500
....*....|....*....|....*
gi 1728558706 463 FNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
2.27e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 7 NRYPADVPTEinpdryQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQ 86
Cdd:PRK12316 501 NATAAEYPLQ------RGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 87 YPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASaiVIVSNfahtlekvvdktavqhvilTRMGDQLSTAKGtvvnf 166
Cdd:PRK12316 574 MVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ--LLLSQ-------------------SHLGRKLPLAAG----- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 167 vvkyIKRLvpkyhlpdAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLL 246
Cdd:PRK12316 628 ----VQVL--------DLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGV 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 247 HPGKeLVVTALPlyhiFALTINCLLFIELGGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLD 323
Cdd:PRK12316 696 GDTV-LQKTPFS----FDVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCT 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 324 FSSLHLSAGGGMP---VQQVVAERWVklTGQYLLegYGLTECAPLVSVNPY-DIDYHSGSIGLPVPSTEAKLVDDDDNEV 399
Cdd:PRK12316 771 SLRRIVCSGEALPadaQEQVFAKLPQ--AGLYNL--YGPTEAAIDVTHWTCvEEGGDSVPIGRPIANLACYILDANLEPV 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 400 PPGQPGELCVKGPQVMLGYWQRPDATDE-----IIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIED 472
Cdd:PRK12316 847 PVGVLGELYLAGRGLARGYHGRPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 926
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 473 VVMQHPGVQEVAAVGVpsgsSGEAVKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 927 RLLEHPWVREAAVLAV----DGKQLVGYVVLESEGgDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
49-509 |
4.69e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 135.80 E-value: 4.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAiVIV 128
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDA-FIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SNFAHTLEKVvdktavqhviltrmgdqLSTAKGTVVNFVVkyikrlVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDL 208
Cdd:PRK09274 120 IPKAHLARRL-----------------FGWGKPSVRRLVT------VGGRLLWGGTTLATLLRDGAAAPFPMADLAPDDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVVtaLPLYHIFALTincllfieLGGQNLL------- 281
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYG-IEPGEIDLPT--FPLFALFGPA--------LGMTSVIpdmdptr 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 282 -IT-NPRDIpglVKELAKYpftaitGVNTLFN--ALLNN----KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKL--TGQ 351
Cdd:PRK09274 246 pATvDPAKL---FAAIERY------GVTNLFGspALLERlgryGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlpPDA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTECAPLVSVNPYDI--------DYHSGS-IGLPVPSTEAKLVD---------DDDNEVPPGQPGELCVKGPQ 413
Cdd:PRK09274 317 EILTPYGATEALPISSIESREIlfatraatDNGAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 414 VMLGYWQRPDATDEI-IKNG----WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PRK09274 397 VTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGV 476
|
490 500
....*....|....*....|.
gi 1728558706 489 PSGssGEAVKIFVVKKDPSLT 509
Cdd:PRK09274 477 GVP--GAQRPVLCVELEPGVA 495
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
205-555 |
5.37e-34 |
|
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: 134.92 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV-NATYGPLlhpgKELVVTALPLYHIFALtINCLLFIELGGQNLLIT 283
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIlNSTEWKT----KDRILSWMPLTHDMGL-IAFHLAPLIAGMNQYLM 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPRDI---PGL-VKELAKYPFTAITGVN---TLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY---- 352
Cdd:cd05908 180 PTRLFirrPILwLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYglkr 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 --LLEGYGLTECAPLVSVNPYDIDY------HSG---------------------SIGLPVPSTEAKLVDDDDNEVPPGQ 403
Cdd:cd05908 260 naILPVYGLAEASVGASLPKAQSPFktitlgRRHvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 404 PGELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMdEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQ- 481
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVEl 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 482 -EVAAVGV-PSGSSGEAVKIFVVKKDpslTEESLVTFCRR------QLTGYKVPKLVEFRdELPKSNVGKILRRELRDEA 553
Cdd:cd05908 419 gRVVACGVnNSNTRNEEIFCFIEHRK---SEDDFYPLGKKikkhlnKRGGWQINEVLPIR-RIPKTTSGKVKRYELAQRY 494
|
..
gi 1728558706 554 RG 555
Cdd:cd05908 495 QS 496
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-550 |
6.28e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 137.99 E-value: 6.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGE------VMTFRKLEERSRAFAAYLQQGLGLkkGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK05691 9 LTLVQALQRRAAQTPDRLALRFLADdpgegvVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 97 AGMIVVnvnPLYTPRELEHQLNDSGASAIvivsnfAHTLEKVVDKTAVQHVILTRMgDQLSTAKgtvvnfvvkyikrlVP 176
Cdd:PRK05691 87 AGVIAV---PAYPPESARRHHQERLLSII------ADAEPRLLLTVADLRDSLLQM-EELAAAN--------------AP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 177 KYHLPDAISfrSALHNGYRmqyvKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVVTA 256
Cdd:PRK05691 143 ELLCVDTLD--PALAEAWQ----EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP-DDVIVSW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 257 LPLYHIFALtINCLLFIELGGQNLLITNPRDIPG----LVKELAKYPFTaITG----VNTLFNALLNNKEFQQLDFSSLH 328
Cdd:PRK05691 216 LPLYHDMGL-IGGLLQPIFSGVPCVLMSPAYFLErplrWLEAISEYGGT-ISGgpdfAYRLCSERVSESALERLDLSRWR 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 329 LSAGGGMPVQQVVAERWVK------LTGQYLLEGYGLTECAPLVS-------VNPYDIDYHS----------GSI----G 381
Cdd:PRK05691 294 VAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSggrrgqgIPALELDAEAlarnraepgtGSVlmscG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 382 LPVPSTEAKLVDDDDNEV-PPGQPGELCVKGPQVMLGYWQRPDATDEIIKN----GWLHTGDIAVMdEEGFLRIVDRKKD 456
Cdd:PRK05691 374 RSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEhdgrTWLRTGDLGFL-RDGELFVTGRLKD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 457 MILVSGFNVYPNEIEDVVMQHPGV---QEVAAVGVP-SGSSGEAVKIFVVKK-DPSLTEESLVTFCRRQLTG--YKVPKL 529
Cdd:PRK05691 453 MLIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNhQGEEGIGIAAEISRSvQKILPPQALIKSIRQAVAEacQEAPSV 532
|
570 580
....*....|....*....|...
gi 1728558706 530 VEFRD--ELPKSNVGKILRRELR 550
Cdd:PRK05691 533 VLLLNpgALPKTSSGKLQRSACR 555
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-550 |
1.77e-33 |
|
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: 132.88 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGAsaivivsnfahtlekvvdktavqHVILTRMGDQLstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd17649 81 EDSGA-----------------------GLLLTHHPRQL----------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvpedlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELvvtaLPLYHI-FALTINCLLFIELG 276
Cdd:cd17649 97 -----------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG--LTPGDRE----LQFASFnFDGAHEQLLPPLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLI------TNPRDIPGLVKELAkypfTAITGVNT--LFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKl 348
Cdd:cd17649 160 GACVVLrpdelwASADELAEMVRELG----VTVLDLPPayLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLK- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 349 TGQYLLEGYGLTEC--APLVSVNPYDIDYHSGS--IGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDA 424
Cdd:cd17649 235 APVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPEL 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 425 TDE-IIKNG-------WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEA 496
Cdd:cd17649 315 TAErFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 497 VKIFVVKKDPSLTE--ESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17649 395 VAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-549 |
5.57e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 130.54 E-value: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 211 LQYTGGTTGVAKgamlTHRNMLANLEQVNATYGPLLH-PGKELVVTALPLYHIFALTINCLLFIELGGQNLLIT--NPRD 287
Cdd:PRK08308 106 LQYSSGTTGEPK----LIRRSWTEIDREIEAYNEALNcEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITnkNPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 288 IpglVKELAKYPFTAITGVNTLFNAL--LNNKEFQqldFSSLHLSaGGGMPvqqvvaERW---VKLTGQYLLEGYGLTEc 362
Cdd:PRK08308 182 A---LNILRNTPQHILYAVPLMLHILgrLLPGTFQ---FHAVMTS-GTPLP------EAWfykLRERTTYMMQQYGCSE- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 363 APLVSVNPyDIDYHsGSIGLPVPSTEAKLVDDddnevpPGQPGELCVKgpqvmlgywqrpDATDEIikngwlHTGDIAVM 442
Cdd:PRK08308 248 AGCVSICP-DMKSH-LDLGNPLPHVSVSAGSD------ENAPEEIVVK------------MGDKEI------FTKDLGYK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 443 DEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVkKDPSLTEESLVTFCRRQLT 522
Cdd:PRK08308 302 SERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-SHEEIDPVQLREWCIQHLA 380
|
330 340
....*....|....*....|....*..
gi 1728558706 523 GYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK08308 381 PYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
200-555 |
6.60e-33 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 132.44 E-value: 6.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 200 KPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLA--------NLEQVNATYGpllhpgkELVVTALPLYHIFAL--TINC 269
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilqkeGLNWVTWVVG-------ETTYSPLPATHIGGLwwILTC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 270 LLFielGGqnLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpvQQVVAE--RWVK 347
Cdd:PRK05857 236 LMH---GG--LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAAdvRFIE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 LTGQYLLEGYGLTE------CAPLVSVNPYDIDyhSGSIGLPVPSTEAKLVDDD--DNEVPPGQP----GELCVKGPQVM 415
Cdd:PRK05857 308 ATGVRTAQVYGLSEtgctalCLPTDDGSIVKIE--AGAVGRPYPGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANM 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 416 LGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGE 495
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 496 AVKIFVVKK---DPSLTEE---SLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARG 555
Cdd:PRK05857 466 LVGLAVVASaelDESAARAlkhTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-549 |
7.83e-33 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 134.40 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHviltrmgDQLSTAkgtvvnfvvkyikrlvpkyhlPD 182
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCY-------NAPLAP---------------------QG 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISFRSALhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPgKELVVTALP---- 258
Cdd:PRK10252 589 AAPLQLSQ--------------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYP--LTA-DDVVLQKTPcsfd 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 259 --LYHIFaltincLLFIelGGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLS--- 330
Cdd:PRK10252 652 vsVWEFF------WPFI--AGAKLVMAEPeahRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRqvf 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 331 -AGGGMPVQQVvaERWVKLTGQYLLEGYGLTECAPLVSVNP---YDIDYHSGS---IGLPVPSTEAKLVDDDDNEVPPGQ 403
Cdd:PRK10252 724 cSGEALPADLC--REWQQLTGAPLHNLYGPTEAAVDVSWYPafgEELAAVRGSsvpIGYPVWNTGLRILDARMRPVPPGV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 404 PGELCVKGPQVMLGYWQRPDATDE-IIKNGWL------HTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK10252 802 AGDLYLTGIQLAQGYLGRPDLTASrFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQA 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 477 HPGVQEVAAVGV-------PSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK10252 882 LPDVEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
23-550 |
8.65e-33 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 132.04 E-value: 8.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVAryADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGmiVV 102
Cdd:PRK10946 25 LPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLG--VA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEhqLN---DSGASAIVIVSNfAHTL--------EKVVDKTAVQHVILtrMGDQLSTAkgtvvnfvvkyi 171
Cdd:PRK10946 100 PVNALFSHQRSE--LNayaSQIEPALLIADR-QHALfsdddflnTLVAEHSSLRVVLL--LNDDGEHS------------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 172 krlvpkyhLPDAISfRSALHngyrmqyVKPELVPED-LAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGK 250
Cdd:PRK10946 163 --------LDDAIN-HPAED-------FTATPSPADeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICG--FTPQT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 251 ELVVtALPLYHIFALTI-NCLLFIELGGQNLLITNPRdiPGLVKEL-AKYPFTAIT----GVNTLFNALLNNKEFQQLdf 324
Cdd:PRK10946 225 RYLC-ALPAAHNYPMSSpGALGVFLAGGTVVLAPDPS--ATLCFPLiEKHQVNVTAlvppAVSLWLQAIAEGGSRAQL-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 325 SSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEcaPLVSVNPYDID----YHSGsiGLPV-PSTEAKLVDDDDNEV 399
Cdd:PRK10946 300 ASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE--GLVNYTRLDDSderiFTTQ--GRPMsPDDEVWVADADGNPL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 400 PPGQPGELCVKGPQVMLGYWQRPD----ATDEiikNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK10946 376 PQGEVGRLMTRGPYTFRGYYKSPQhnasAFDA---NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 476 QHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPsLTEESLVTFCRRQ-LTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK10946 453 RHPAVIHAALVSMEDELMGEKSCAFLVVKEP-LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
28-549 |
7.27e-32 |
|
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: 128.32 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 28 MFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDSGASaivivsnfahtlekvvdktavqhVILTRmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfr 187
Cdd:cd17644 84 YPQERLTYILEDAQIS-----------------------VLLTQ------------------------------------ 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 188 salhngyrmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVVTALPlyhiFALTI 267
Cdd:cd17644 105 -----------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG-ITSSDRVLQFASIA----FDVAA 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 NCLLFIELGGQNL-LITNP--RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDF-SSLHLSAGGGMPVQQVVAE 343
Cdd:cd17644 163 EEIYVTLLSGATLvLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 344 RWVKLTGQY--LLEGYGLTECAPLVSV----NPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLG 417
Cdd:cd17644 243 QWQKNVGNFiqLINVYGPTEATIAATVcrltQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDE-IIKNGWLH--------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGV 488
Cdd:cd17644 323 YLNRPELTAEkFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT-AVVIV 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728558706 489 PSGSSGEA--VKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17644 402 REDQPGNKrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
1.44e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.85 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 7 NRYPADVPTEInpdryqSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQ 86
Cdd:PRK12316 1993 DRTPEAYPRGP------GVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFE 2065
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 87 YPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGASAIVIVSnfaHTLEKVVDKTAVQHVILTRMGDqlstakgtvvn 165
Cdd:PRK12316 2066 LVVALLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLLTQR---HLLERLPLPAGVARLPLDRDAE----------- 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 166 fvvkyikrlvpkyhLPDAISFRSAlhngyrmqyvkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpl 245
Cdd:PRK12316 2131 --------------WADYPDTAPA-----------VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE-- 2183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 246 LHPGK-ELVVTALPlyhiFALTINCLLFIELGGQNLLITNP--RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQ-- 320
Cdd:PRK12316 2184 LSPADcELQFMSFS----FDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgr 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 321 QLDFSSLHLsagGGMPVQQVVAER-WVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS----IGLPVPSTEAKLVDDD 395
Cdd:PRK12316 2260 PPAVRVYCF---GGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNRRAYILDAD 2336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 396 DNEVPPGQPGELCVKGPQVMLGYWQRPDATDEII-------KNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYP 467
Cdd:PRK12316 2337 LNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsaSGERLYrTGDLARYRADGVVEYLGRIDHQVKIRGFRIEL 2416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 468 NEIEDVVMQHPGVQEvAAVGVPSGSSGEAVKIFVVKKDP-SLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:PRK12316 2417 GEIEARLQAHPAVRE-AVVVAQDGASGKQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDR 2495
|
...
gi 1728558706 547 REL 549
Cdd:PRK12316 2496 KAL 2498
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-549 |
2.57e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 130.28 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 5 WlNRYPADVPTEinpdryQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNL 84
Cdd:PRK12467 1563 W-NATHTGYPLA------RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIA-LGVGPEVLVGIAVERS 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSnfaHTLEKVVDKTAVQHVILTRMGDQLStakgtvv 164
Cdd:PRK12467 1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS---HLQARLPLPDGLRSLVLDQEDDWLE------- 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 165 nfvvkyikrlvpkyhlpdaisfrsalhnGYRMqyVKPELV--PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:PRK12467 1705 ----------------------------GYSD--SNPAVNlaPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 243 GplLHPGKelvvtALPLYHIFALTINCLLFIE--LGGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNNK 317
Cdd:PRK12467 1755 Q--LSAAD-----VVLQFTSFAFDVSVWELFWplINGARLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMD 1827
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 318 EFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS----IGLPVPSTEAKLVD 393
Cdd:PRK12467 1828 EQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILD 1907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 394 DDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDE-IIKN------GWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNV 465
Cdd:PRK12467 1908 ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErFVADpfgtvgSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRI 1987
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 466 YPNEIEDVVMQHPGVQEvAAVGVPSGSSGEAVKIFVVKKDPSLTEESL-VTFCRRQLTG--------YKVPKLVEFRDEL 536
Cdd:PRK12467 1988 ELGEIEARLREQGGVRE-AVVIAQDGANGKQLVAYVVPTDPGLVDDDEaQVALRAILKNhlkaslpeYMVPAHLVFLARM 2066
|
570
....*....|...
gi 1728558706 537 PKSNVGKILRREL 549
Cdd:PRK12467 2067 PLTPNGKLDRKAL 2079
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
201-548 |
3.73e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 127.42 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 201 PELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTALPLYH----IFALTINcllfIELG 276
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVETDVMVSWLPLFHdmgmVGFLTVP----MYFG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLITnPRDI---PGLVKEL-AKYPFTAITGVN---TLFNALLNNK-EFQQLDFSSLHLSAGGGMPVQQVVAERWV-- 346
Cdd:PRK07768 221 AELVKVT-PMDFlrdPLLWAELiSKYRGTMTAAPNfayALLARRLRRQaKPGAFDLSSLRFALNGAEPIDPADVEDLLda 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 347 ----KLTGQYLLEGYGLTECAPLVSVNPYD----IDY---------------HSG------SIGLPVPSTEAKLVDDDDN 397
Cdd:PRK07768 300 garfGLRPEAILPAYGMAEATLAVSFSPCGaglvVDEvdadllaalrravpaTKGntrrlaTLGPPLPGLEVRVVDEDGQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 398 EVPPGQPGELCVKGPQVMLGYwQRPD----ATDEiikNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PRK07768 380 VLPPRGVGVIELRGESVTPGY-LTMDgfipAQDA---DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERA 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 474 VMQHPGVQE--VAAVGVPSGSSGEAVKIFVVKKDPSltEESLVTFCRRQLTgYKVPKLVEFRDE---------LPKSNVG 542
Cdd:PRK07768 456 AARVEGVRPgnAVAVRLDAGHSREGFAVAVESNAFE--DPAEVRRIRHQVA-HEVVAEVGVRPRnvvvlgpgsIPKTPSG 532
|
....*.
gi 1728558706 543 KiLRRE 548
Cdd:PRK07768 533 K-LRRA 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-551 |
3.75e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.51 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 14 PTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYL-QQGLGlkkGDR-VALMMPNLLQYPVAL 91
Cdd:PRK12467 3086 ATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLiAIGVG---PDVlVGVAVERSVEMIVAL 3162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 92 FGILRAGMIVVNVNPLYtPRE-LEHQLNDSGASaiVIVSNfAHTLEKVVDKTAVQHVILtrmgDQLSTakgtvvnfvvky 170
Cdd:PRK12467 3163 LAVLKAGGAYVPLDPEY-PRErLAYMIEDSGVK--LLLTQ-AHLLEQLPAPAGDTALTL----DRLDL------------ 3222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 171 ikrlvpkyhlpdaisfrsalhNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHrNMLANLEQVNATYGPLLHPGK 250
Cdd:PRK12467 3223 ---------------------NGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRH-GALANHLCWIAEAYELDANDR 3280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 251 ELVVTALPlyhiFALTINCLLFIELGGQNLLIT--NPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLH 328
Cdd:PRK12467 3281 VLLFMSFS----FDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCASLDIY 3356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 329 LSAGGGMPVQQVvAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS----IGLPVPSTEAKLVDDDDNEVPPGQP 404
Cdd:PRK12467 3357 VFGGEAVPPAAF-EQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDGQLNPVPVGVA 3435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 405 GELCVKGPQVMLGYWQRPDATDE-------IIKNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK12467 3436 GELYIGGVGLARGYHQRPSLTAErfvadpfSGSGGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQ 3515
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 477 HPGVQEVAAVGVPsGSSGEAVKIFVVKKDPSLT-EESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK12467 3516 HPSVREAVVLARD-GAGGKQLVAYVVPADPQGDwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPD 3590
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
24-552 |
3.69e-30 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 124.85 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAF-------VNMGEV--MTFRKLEERSRAFAAYLQQGLGlkKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYryldhshSAAGCAveLTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 95 LRAGMIVVnvnPLYTPRELEHqlndsgasaivivsnfAHTLEKVVdKTAVQHVILTRmgdqlSTAKGTVVNFVVKYIKRL 174
Cdd:PRK12476 113 IKAGTIAV---PLFAPELPGH----------------AERLDTAL-RDAEPTVVLTT-----TAAAEAVEGFLRNLPRLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 VPKYHLPDAISFRSAlhngyrMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKElVV 254
Cdd:PRK12476 168 RPRVIAIDAIPDSAG------ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSID-LLDRNTH-GV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 255 TALPLYHIFALTIncLLFIELGGQNLLITNP----RDIPGLVKELAK---------------YPFTAITGVNtlfnalln 315
Cdd:PRK12476 240 SWLPLYHDMGLSM--IGFPAVYGGHSTLMSPtafvRRPQRWIKALSEgsrtgrvvtaapnfaYEWAAQRGLP-------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 316 nKEFQQLDFSSLHLsAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTECAPLVS---------------------- 367
Cdd:PRK12476 310 -AEGDDIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPrtafkpSYGIAEATLFVAtiapdaepsvvyldreqlgagr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 368 VNPYDIDYHSG----SIGLPVPSTEAKLVDDD-DNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKN----------- 431
Cdd:PRK12476 388 AVRVAADAPNAvahvSCGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 432 --------GWLHTGDIAV-MDEEgfLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HPGVQE--VAAVGVPSGSSGEAVKI 499
Cdd:PRK12476 468 adgaaddgTWLRTGDLGVyLDGE--LYITGRIADLIVIDGRNHYPQDIEATVAEaSPMVRRgyVTAFTVPAEDNERLVIV 545
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 500 F-----VVKKDPSLTEESL-VTFCRRQLTGYKVPKLVEfRDELPKSNVGKILRRELRDE 552
Cdd:PRK12476 546 AeraagTSRADPAPAIDAIrAAVSRRHGLAVADVRLVP-AGAIPRTTSGKLARRACRAQ 603
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-553 |
4.07e-30 |
|
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: 122.95 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIViv 128
Cdd:cd05910 3 LSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 snfahtlekvvdktavqhviltrmgdqlstakGtvvnfvvkyikrlVPKYHLPDAISFrsalhngyrmqyvkpelvpedl 208
Cdd:cd05910 80 --------------------------------G-------------IPKADEPAAILF---------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 aflqyTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllHPGkELVVTALPLYHIFALTINCLLFI-ELGGQNLLITNPRD 287
Cdd:cd05910 93 -----TSGSTGTPKGVVYRHGTFAAQIDALRQLYGI--RPG-EVDLATFPLFALFGPALGLTSVIpDMDPTRPARADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 288 ipgLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLH--LSAGGgmPVQQVVAERWVKLT--GQYLLEGYGLTECA 363
Cdd:cd05910 165 ---LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGA--PVPIALAARLRKMLsdEAEILTPYGATEAL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 364 PLVSVNPYDI--------DYHSGS-IGLPVPSTEAKLVD---------DDDNEVPPGQPGELCVKGPQVMLGYWQRPDAT 425
Cdd:cd05910 240 PVSSIGSRELlatttaatSGGAGTcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 426 ------DEiiKNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVpsGSSGEAVK 498
Cdd:cd05910 320 alakidDN--SEGFWHrMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQLP 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 499 IFVVKKDPSLTEES------LVTFCRRQLTGYKVPKLVeFRDELP---KSNvGKILRRELRDEA 553
Cdd:cd05910 396 VLCVEPLPGTITPRarleqeLRALAKDYPHTQRIGRFL-IHPSFPvdiRHN-AKIFREKLAVWA 457
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-549 |
7.83e-29 |
|
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: 119.11 E-value: 7.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVIVsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd17650 81 EDSGAKLLLTQ--------------------------------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFielGG 277
Cdd:cd17650 92 -------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLN---GG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 QnlLITNPRDI----PGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpvqQVVAERWVK------ 347
Cdd:cd17650 162 T--LVICPDEVkldpAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS----DGCKAQDFKtlaarf 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 348 LTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS----IGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPD 423
Cdd:cd17650 236 GQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 424 ATDE-IIKNGW------LHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGVPSGSSGEA 496
Cdd:cd17650 316 LTAErFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1728558706 497 VKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17650 395 RLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-553 |
8.04e-29 |
|
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: 119.38 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKS-LGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIvsnfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvp 205
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 eDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnatYGPLLHPGKELVVTALPLYHIFALTInCLLFIELGGQNLLITNP 285
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALIV-GWSACLASGATLVIRKK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 286 RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvqqvvAERWVKLTGQY----LLEGYGLTE 361
Cdd:cd05940 157 FSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLR-----PDIWEEFKERFgvprIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 362 CaplvSVNPYDIDYHSGSIG----LPVPSTEAKLVD-DDDN------------EVPPGQPGELC--VKGPQVMLGYWQRP 422
Cdd:cd05940 232 G----NSGFINFFGKPGAIGrnpsLLRKVAPLALVKyDLESgepirdaegrciKVPRGEPGLLIsrINPLEPFDGYTDPA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 423 DATDEIIKN------GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVP-SGSSGE 495
Cdd:cd05940 308 ATEKKILRDvfkkgdAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDGR 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 496 A-VKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05940 388 AgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
1.03e-28 |
|
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: 118.82 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLnDSGASAIVIV 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SNFAHTlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpelvpEDL 208
Cdd:cd05974 79 DENTHA-----------------------------------------------------------------------DDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 209 AFLQYTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLHPGKELVVTALPLYHIFALTinCLLFIELGGQNLLITN-PR- 286
Cdd:cd05974 88 MLLYFTSGTTSKPKLVEHTHRSYPVG--HLSTMYWIGLKPGDVHWNISSPGWAKHAWS--CFFAPWNAGATVFLFNyARf 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 287 DIPGLVKELAKYPFTAITGVNTLFNALLnnkefqQLDFSSLHLS----AGGGMPVQQVVAERWVKLTGQYLLEGYGLTEC 362
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLI------QQDLASFDVKlrevVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 363 APLVSVNPYDIdYHSGSIGLPVPSTEAKLVDDDDNevpPGQPGELCV-----KGPQVMLGYWQRPDATDEIIKNGWLHTG 437
Cdd:cd05974 238 TALVGNSPGQP-VKAGSMGRPLPGYRVALLDPDGA---PATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 438 DIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-----KKDPSlTEES 512
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPE-TALE 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 1728558706 513 LVTFCRRQLTGYKVPKLVEFRdELPKSNVGKILRRELR 550
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
49-455 |
1.84e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 120.08 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIV 128
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAE-LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SNFAHTLEKVVDKTAVQHVILTRMGDqlstakgtvvnfvvkyikrlvpkyhLPDA--------ISFRSALHNGYRMQYVK 200
Cdd:PTZ00216 201 GKNVPNLLRLMKSGGMPNTTIIYLDS-------------------------LPASvdtegcrlVAWTDVVAKGHSAGSHH 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 201 PELVPE---DLAFLQYTGGTTGVAKGAMLTHRNMLANL----EQVNATYGPLlHPGkELVVTALPLYHIFALTI-NCLL- 271
Cdd:PTZ00216 256 PLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGIlaleDRLNDLIGPP-EED-ETYCSYLPLAHIMEFGVtNIFLa 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 ---FIELGgqnllitNPRDIPGLVK----ELAKYPFTAITGVNTLFN------------------------------ALL 314
Cdd:PTZ00216 334 rgaLIGFG-------SPRTLTDTFArphgDLTEFRPVFLIGVPRIFDtikkaveaklppvgslkrrvfdhayqsrlrALK 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 315 NNKE---FQQLDFS--------SLHLSAGGGMPVQQVVAErWVKLTGQYLLEGYGLTECaplVSVNPYDI--DYHSGSIG 381
Cdd:PTZ00216 407 EGKDtpyWNEKVFSapravlggRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTET---VCCGGIQRtgDLEPNAVG 482
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 382 LPVPSTEAKLVDDDD---NEVPpgQP-GELCVKGPQVMLGYWQRPDATDEII-KNGWLHTGDIAVMDEEGFLRIVDRKK 455
Cdd:PTZ00216 483 QLLKGVEMKLLDTEEykhTDTP--EPrGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-553 |
2.17e-28 |
|
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: 118.30 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQA-QGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VivsnfahtlekvvdktavqhvilTRMGDQLSTAKGTvvnfvvkyikrlvpkyHLP--DAISFRSALhngyrmqyvkpel 203
Cdd:cd05939 80 I-----------------------FNLLDPLLTQSST----------------EPPsqDDVNFRDKL------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 vpedlaFLQYTGGTTGVAKGAMLTHRNMLanLEQVNATYGPLLHPgKELVVTALPLYHIFALTI---NCLLFielgGQNL 280
Cdd:cd05939 108 ------FYIYTSGTTGLPKAAVIVHSRYY--RIAAGAYYAFGMRP-EDVVYDCLPLYHSAGGIMgvgQALLH----GSTV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 281 LITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvQQVvaerWVKLTGQY----LLEG 356
Cdd:cd05939 175 VIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR-PQI----WEQFVRRFgipqIGEF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 357 YGLTECaplvSVNPYDIDYHSGSIGLpVPSTEAKL-------VDDDDNE---------VP--PGQPGELCVKGPQ----- 413
Cdd:cd05939 250 YGATEG----NSSLVNIDNHVGACGF-NSRILPSVypirlikVDEDTGElirdsdglcIPcqPGEPGLLVGKIIQndplr 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 414 VMLGYWQRPDATDEIIKNGWLH------TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:cd05939 325 RFDGYVNEGATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYG 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 488 VP-SGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05939 405 VEvPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
33-555 |
3.14e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 119.09 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 33 VARYADQPAFVNMGE------VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMI--VVNV 104
Cdd:PRK00174 77 LKTRGDKVAIIWEGDdpgdsrKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsVVFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 105 NplYTPRELEHQLNDSGASAIVIVSNF-----AHTLEKVVDK-----TAVQHVI-LTRMGDQLSTAKGtvvnfvvkyikR 173
Cdd:PRK00174 156 G--FSAEALADRIIDAGAKLVITADEGvrggkPIPLKANVDEalancPSVEKVIvVRRTGGDVDWVEG-----------R 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 174 LVpKYHlpDAISFRSAlhngyrmqYVKPELVP-EDLAFLQYTGGTTGVAKG-----------AMLTHRNML--------- 232
Cdd:PRK00174 223 DL-WWH--ELVAGASD--------ECEPEPMDaEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVFdykdgdvyw 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 233 --ANLEQVNA----TYGPLLHPGKELVVTALPLY-------HIfaltincllfIELGGQNLLITNPRDIPGLVKELAKYP 299
Cdd:PRK00174 292 ctADVGWVTGhsyiVYGPLANGATTLMFEGVPNYpdpgrfwEV----------IDKHKVTIFYTAPTAIRALMKEGDEHP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 300 ftaitgvntlfnallnnkefQQLDFSSLHLSAGGGMPV--------QQVV-AER-------WVKLTGQYLLegygltecA 363
Cdd:PRK00174 362 --------------------KKYDLSSLRLLGSVGEPInpeawewyYKVVgGERcpivdtwWQTETGGIMI--------T 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 364 PLvsvnPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKG--PQVMLGYWQRPD-------ATdeiIKNGWL 434
Cdd:PRK00174 414 PL----PGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHErfvktyfST---FKGMYF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 435 hTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKD---PS--LT 509
Cdd:PRK00174 487 -TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGgeePSdeLR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1728558706 510 EEsLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARG 555
Cdd:PRK00174 566 KE-LRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAEG 610
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-553 |
5.03e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 117.86 E-value: 5.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTvvnfvvkyikrlvpkyhlpdAISFRSALhngyrmq 197
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDA--------------------EPPFRVAD------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQYTGGTTGVAKGAMLTHR------NMLAnleqvnATYGplLHPGkELVVTALPLYHIFALtINCLL 271
Cdd:PRK07867 151 -------PDDLFMLIFTSGTSGDPKAVRCTHRkvasagVMLA------QRFG--LGPD-DVCYVSMPLFHSNAV-MAGWA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEfqQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ 351
Cdd:PRK07867 214 VALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPE--RPDDADNPLRIVYGNEGAPGDIARFARRFGC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 352 YLLEGYGLTECAPLVSVNPydiDYHSGSIGLPVPSTeaKLVD-DDDNEVPPGQP------------GELC-VKGPQVMLG 417
Cdd:PRK07867 292 VVVDGFGSTEGGVAITRTP---DTPPGALGPLPPGV--AIVDpDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAV 497
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 498 KIFVV-KKDPSLTEESLVTFCRRQ--LTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK07867 447 MAALVlAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEG 505
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
5.30e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.06 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 7 NRYPADVPTEINPDRyqslvdMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQ 86
Cdd:PRK12316 3047 NATAAEYPLERGVHR------LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLE 3119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 87 YPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFahtleKVVDKTAVQHVILTRMGDQLSTAKGTVvnf 166
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHL-----RLPLAQGVQVLDLDRGDENYAEANPAI--- 3191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 167 vvkyikrlvpkyhlpdaisfrsalhngyrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplL 246
Cdd:PRK12316 3192 -----------------------------------RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG--L 3234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 247 HPGKELVVTALPLYHIFALTINCLLfieLGGQNLLITNPR---DIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLD 323
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPL---MSGARVVLAGPEdwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 324 FSSLHLSAGGGMPVQqvVAERWVklTGQYLLEGYGLTECAPLVSVNPYDIDYHSGS-IGLPVPSTEAKLVDDDDNEVPPG 402
Cdd:PRK12316 3312 SLKRIVCGGEALPAD--LQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVG 3387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 403 QPGELCVKGPQVMLGYWQRPDATDE------IIKNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK12316 3388 ALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGERLYrTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1728558706 476 QHPGVQEVAAVGVpsgsSGEAVKIFVVKKDPSLT-EESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 3468 EHPWVREAVVLAV----DGRQLVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-550 |
9.42e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 114.37 E-value: 9.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 175 VPKYHLPDAISFRSALHNGyrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnATYGPLLHPGKELVv 254
Cdd:PRK07824 12 VPAQDERRAALLRDALRVG--------EPIDDDVALVVATSGTTGTPKGAMLTAAALTASAD---ATHDRLGGPGQWLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 255 tALPLYHIFALTIncLLFIELGGQNLLIT------NPRDIPGLVKELA---KYpfTAITGVNtLFNALLNNKEFQQL-DF 324
Cdd:PRK07824 80 -ALPAHHIAGLQV--LVRSVIAGSEPVELdvsagfDPTALPRAVAELGggrRY--TSLVPMQ-LAKALDDPAATAALaEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 325 SSLhLSAGGGMPVQqvVAERWVKLtGQYLLEGYGLTE-CAPLVsvnpYDidyhsgsiGLPVPSTEAKLVDdddnevppgq 403
Cdd:PRK07824 154 DAV-LVGGGPAPAP--VLDAAAAA-GINVVRTYGMSEtSGGCV----YD--------GVPLDGVRVRVED---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 404 pGELCVKGPQVMLGYwQRPDATDEIIKNGWLHTGDIAVMDEeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEV 483
Cdd:PRK07824 208 -GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1728558706 484 AAVGVPSGSSGEAVKIFVVKK-DPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07824 285 AVFGLPDDRLGQRVVAAVVGDgGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
32-549 |
2.29e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 115.86 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 32 SVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGlGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPR 111
Cdd:PRK13383 44 TAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 112 ELEHQLNDSGASAIVIVSNFAhtlekvvdktavqhviltrmgDQLSTAKgtvvnfvvkyikrlvpkyhlpDAISFRSALH 191
Cdd:PRK13383 123 ALAAALRAHHISTVVADNEFA---------------------ERIAGAD---------------------DAVAVIDPAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 192 NGYRMQYVKPELVPEDLAFLqYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVtALPLYHIFALTInCLL 271
Cdd:PRK13383 161 AGAEESGGRPAVAAPGRIVL-LTSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISV-AMPMFHGLGLGM-LML 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELGGqNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLT 349
Cdd:PRK13383 238 TIALGG-TVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 350 GQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYwqrPDATDEII 429
Cdd:PRK13383 317 GDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPS-L 508
Cdd:PRK13383 394 VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSgV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1728558706 509 TEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK13383 474 DAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-550 |
3.52e-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: 115.22 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVS 129
Cdd:cd05915 26 TYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVDktavqhvILTRMGDQLSTAKgtvvnfvvkyikrlvpKYHlpdaiSFRSALHNGY-RMQYVKPelVPE-D 207
Cdd:cd05915 105 NLLPLVEAIRG-------ELKTVQHFVVMDE----------------KAP-----EGYLAYEEALgEEADPVR--VPErA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTaLPLYHIFALtinCLLFI--ELGGQNLLITNP 285
Cdd:cd05915 155 ACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPV-VPMFHVNAW---CLPYAatLVGAKQVLPGPR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 286 RDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFS-SLHLSAGGGMPVQqvVAERWVKLTGQYLLEGYGLTECAP 364
Cdd:cd05915 231 LDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtLRRLVVGGSAAPR--SLIARFERMGVEVRQGYGLTETSP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 365 LVSVNPYDIDYHS----------GSIGLPVPSTEAKLVDDDDNEVPpgQPGE----LCVKGPQVMLGYWQRPDATDEI-I 429
Cdd:cd05915 309 VVVQNFVKSHLESlseeekltlkAKTGLPIPLVRLRVADEEGRPVP--KDGKalgeVQLKGPWITGGYYGNEEATRSAlT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 430 KNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLT 509
Cdd:cd05915 387 PDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPT 466
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1728558706 510 EESLVTFCRRQLTGYK-VPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05915 467 PEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-549 |
2.56e-26 |
|
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: 111.72 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 118 NDSGASaiVIVSNfahtlekvvdktavqhviltrmgdqlstakgtvvnfvvkyikrlvpkyhlpdaisfrsalhngyrmq 197
Cdd:cd17648 82 EDTGAR--VVITN------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 198 yvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKElVVTALPLYhIFALTINCLLFIELGG 277
Cdd:cd17648 93 -------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDE-AVLFFSNY-VFDFFVEQMTLALLNG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 278 QNLLITNPR---DIPGLVKELAKYPFTAITGVNTLFnallnnkefQQLDFSSL-HL----SAGggmpvQQVVAERWVKLT 349
Cdd:cd17648 163 QKLVVPPDEmrfDPDRFYAYINREKVTYLSGTPSVL---------QQYDLARLpHLkrvdAAG-----EEFTAPVFEKLR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 350 GQY---LLEGYGLTECAPLVSVNPYDIDYH-SGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDAT 425
Cdd:cd17648 229 SRFaglIINAYGPTETTVTNHKRFFPGDQRfDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELT 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 426 DEII--------------KNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVG--V 488
Cdd:cd17648 309 AERFlpnpfqteqerargRNARLYkTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeD 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 489 PSGSSGEAVKIFV---VKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17648 389 ASQAQSRIQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
69-452 |
2.94e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 113.22 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 69 LGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH----QLNDSGASAIVIVSN---FAHTLEkVVDK 141
Cdd:PRK12582 100 LGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHaklkHLFDLVKPRVVFAQSgapFARALA-ALDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 142 TAVQHVILTRMGDQLST------AKGTVVNFVVKYIKRLVPkyhlpDAIsfrsalhngyrmqyvkpelvpedlAFLQYTG 215
Cdd:PRK12582 179 LDVTVVHVTGPGEGIASiafadlAATPPTAAVAAAIAAITP-----DTV------------------------AKYLFTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 216 GTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTALPLYHIFALTI--NCLLFielGGQNLLITNPRDIPGLVK 293
Cdd:PRK12582 230 GSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNAnfNGLLW---GGGTLYIDDGKPLPGMFE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 294 ELAK--------YPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW----VKLTGQY--LLEGYGL 359
Cdd:PRK12582 307 ETIRnlreisptVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMqalaVRTTGHRipFYTGYGA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 360 TECAPlVSVNPYDIDYHSGSIGLPVPSTEAKLvddddneVPPGQPGELCVKGPQVMLGYWQRPDATDeiikngwlhtgdi 439
Cdd:PRK12582 387 TETAP-TTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTA------------- 445
|
410
....*....|...
gi 1728558706 440 AVMDEEGFLRIVD 452
Cdd:PRK12582 446 AAFDEEGFYRLGD 458
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-458 |
7.72e-26 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 112.13 E-value: 7.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 2 KKVWLNRYPADVPTE----INPDRYQSLVD-----------MFEQSVARYADQP----------AFVNMGEVMTFRKLE- 55
Cdd:PLN02387 22 KKGKKRGVPVDVGGEpgyaIRNARFPELVEtpwegattlaaLFEQSCKKYSDKRllgtrklisrEFETSSDGRKFEKLHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 56 ------------ERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAS 123
Cdd:PLN02387 102 geyewitygqvfERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 124 AIVIVSNfahTLEKVVDktavqhviltrMGDQLSTAKGtvvnfvVKYIKRLVPKYHLPDA-------ISFRSALHNGyRM 196
Cdd:PLN02387 181 TVICDSK---QLKKLID-----------ISSQLETVKR------VIYMDDEGVDSDSSLSgssnwtvSSFSEVEKLG-KE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 197 QYVKPEL-VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLLHPgKELVVTALPLYHIFALTINCLLF--- 272
Cdd:PLN02387 240 NPVDPDLpSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGV-MTVVPKLGK-NDVYLAYLPLAHILELAAESVMAavg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 273 -----------------IELG--------GQNLLITNP------RDipGLVKE------LAKYPF--------TAITGV- 306
Cdd:PLN02387 318 aaigygspltltdtsnkIKKGtkgdasalKPTLMTAVPaildrvRD--GVRKKvdakggLAKKLFdiaykrrlAAIEGSw 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 307 -------NTLFNALLnNKEFQQLDFSSLHLSAGGGMPVQQvVAERWVKLT-GQYLLEGYGLTECAPLVSVNPYDiDYHSG 378
Cdd:PLN02387 396 fgawgleKLLWDALV-FKKIRAVLGGRIRFMLSGGAPLSG-DTQRFINIClGAPIGQGYGLTETCAGATFSEWD-DTSVG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 379 SIGLPVPSTEAKLVDDD-------DNEVPpgqPGELCVKGPQVMLGYWQRPDATDEIIK---NG--WLHTGDIAVMDEEG 446
Cdd:PLN02387 473 RVGPPLPCCYVKLVSWEeggylisDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKvdeRGmrWFYTGDIGQFHPDG 549
|
570
....*....|..
gi 1728558706 447 FLRIVDRKKDMI 458
Cdd:PLN02387 550 CLEIIDRKKDIV 561
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
205-452 |
1.62e-25 |
|
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: 110.60 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVVTALPLYHIFALTINCLLFIELGGqNLLITN 284
Cdd:cd05921 164 PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTY-PFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGG-TLYIDD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLVKELAK--------YPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW----VKLTGQY 352
Cdd:cd05921 242 GKPMPGGFEETLRnlreisptVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLqalaVATVGER 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 --LLEGYGLTECAPLvSVNPYDIDYHSGSIGLPVPSTEAKLVddddnevPPGQPGELCVKGPQVMLGYWQRPDATdeiik 430
Cdd:cd05921 322 ipMMAGLGATETAPT-ATFTHWPTERSGLIGLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYWRQPELT----- 388
|
250 260
....*....|....*....|..
gi 1728558706 431 ngwlhtgdIAVMDEEGFLRIVD 452
Cdd:cd05921 389 --------AQAFDEEGFYCLGD 402
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
205-452 |
2.54e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 110.35 E-value: 2.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVVTALPLYHIFALTINCLLFIELGGqNLLITN 284
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGG-TLYIDD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLVKE----LAKYPFTAITGVNTLFNALLN----NKEFQQLDFSSLHLS--AGGGMPvqQVVAERWVKLTGQYLL 354
Cdd:PRK08180 286 GKPTPGGFDEtlrnLREISPTVYFNVPKGWEMLVPalerDAALRRRFFSRLKLLfyAGAALS--QDVWDRLDRVAEATCG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 355 E------GYGLTECAPLVSVNPYDIDyHSGSIGLPVPSTEAKLVDDDDNEvppgqpgELCVKGPQVMLGYWQRPDATDEi 428
Cdd:PRK08180 364 ErirmmtGLGMTETAPSATFTTGPLS-RAGNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPGYWRAPELTAE- 434
|
250 260
....*....|....*....|....
gi 1728558706 429 ikngwlhtgdiaVMDEEGFLRIVD 452
Cdd:PRK08180 435 ------------AFDEEGYYRSGD 446
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
2.94e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 111.41 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 103 NVNPLYTPRELEHQLNDSGASAIVIVSnfaHTLEKVVDKTAVQHVILtrmgDQLstakgtvvnfvvkyikrlvpkyHLPD 182
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQS---HLLERLPQAEGVSAIAL----DSL----------------------HLDS 1260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 183 AISFRSALHngyrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTAlPLYhi 262
Cdd:PRK05691 1261 WPSQAPGLH-----------LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDSDVLMQKA-PIS-- 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 263 FALTI-NCLLFIeLGGQNLLITNP---RDIPGLVKELAKYPFTAITGVNTLFNALLNnkEFQQLDFSSLHLSAGGGMPVQ 338
Cdd:PRK05691 1325 FDVSVwECFWPL-ITGCRLVLAGPgehRDPQRIAELVQQYGVTTLHFVPPLLQLFID--EPLAAACTSLRRLFSGGEALP 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 339 QVVAERWVKLTGQYLLEG-YGLTECAplVSVNPYDIDYHSGS---IGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQV 414
Cdd:PRK05691 1402 AELRNRVLQRLPQVQLHNrYGPTETA--INVTHWQCQAEDGErspIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGL 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRPDAT------DEIIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAV 486
Cdd:PRK05691 1480 ARGYLGRPALTaerfvpDPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAV 1558
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1728558706 487 GVPSGSSG-EAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 1559 LVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
205-549 |
2.12e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 108.72 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLAN-LEQVnatygPLLHPGKELVVtALPLYHIFALTINCLLFIELGGQNLLIT 283
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNqLSKV-----PYLALSEADVI-AQTASQSFDISVWQFLAAPLFGARVEIV 3941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 nPRDIP----GLVKELAKYPFTAITGVNTLFNALLNNKEfQQLDFSSLHLSAGGGMPVQqvVAERWVKLTGQY-LLEGYG 358
Cdd:PRK05691 3942 -PNAIAhdpqGLLAHVQAQGITVLESVPSLIQGMLAEDR-QALDGLRWMLPTGEAMPPE--LARQWLQRYPQIgLVNAYG 4017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 359 LTECAPLVSVNPYDIDYHSGS---IGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEI-IKNGW- 433
Cdd:PRK05691 4018 PAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAfVPHPFg 4097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 434 ------LHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEvAAVGVPSGSSGEAVKIFVVKKDPS 507
Cdd:PRK05691 4098 apgerlYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTV 4176
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1728558706 508 LTEESLVTFCRRQLTG----YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 4177 LAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
353-553 |
2.26e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.03 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 LLEGYGLTECAPLVSVNPydiDYHSGSIGLPVPSTEakLVDDDD-NEVPPGQ-------------PGELCVK-GPQVMLG 417
Cdd:PRK13388 291 VEDGYGSSEGAVIVVREP---GTPPGSIGRGAPGVA--IYNPETlTECAVARfdahgallnadeaIGELVNTaGAGFFEG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 418 YWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAV 497
Cdd:PRK13388 366 YYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQV 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 498 KIFVVKKDP-SLTEESLVTFCRRQ--LTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK13388 446 MAALVLRDGaTFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-536 |
3.42e-24 |
|
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: 106.22 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 46 GEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 VIVSNFAHTLEKVVDKtavqhviLTRMGDQLSTAKGTVvnfvvkyikrlvpkyHLPDAISFRSALhngyrmQYVKPELVP 205
Cdd:cd05938 83 VVAPELQEAVEEVLPA-------LRADGVSVWYLSHTS---------------NTEGVISLLDKV------DAASDEPVP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 206 EDL---------AFLQYTGGTTGVAKGAMLTHRNMLanleQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFIELG 276
Cdd:cd05938 135 ASLrahvtikspALYIYTSGTTGLPKAARISHLRVL----QCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 277 GQNLLITnprdipglvK--------ELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpVQQVVAERWVKL 348
Cdd:cd05938 211 ATCVLKP---------KfsasqfwdDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNG--LRADVWREFLRR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 349 TGQ-YLLEGYGLTE-----------CAPLVSVN-------PYD-IDYHsgsiglpvPSTEAKLVDDDDN--EVPPGQPGE 406
Cdd:cd05938 280 FGPiRIREFYGSTEgnigffnytgkIGAVGRVSylykllfPFElIKFD--------VEKEEPVRDAQGFciPVAKGEPGL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 407 LCVKGPQV--MLGYWQRPDATD-----EIIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:cd05938 352 LVAKITQQspFLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLL 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 478 PGVQEVAAVGVP-SGSSGEAVKIFVVKKDP-SLTEESLVTFCRRQLTGYKVPKLVEFRDEL 536
Cdd:cd05938 432 DFLQEVNVYGVTvPGHEGRIGMAAVKLKPGhEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
197-510 |
3.56e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 107.03 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 197 QYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLA-------NLEQVNATYGPllhpgKELVVTALPLYHIFALTIN- 268
Cdd:PLN02614 214 QYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTliagvirLLKSANAALTV-----KDVYLSYLPLAHIFDRVIEe 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 269 CllFIELGGQ--------NLLITN------------PRDI----PGLVKELA--------------KYPFTAI------T 304
Cdd:PLN02614 289 C--FIQHGAAigfwrgdvKLLIEDlgelkptifcavPRVLdrvySGLQKKLSdggflkkfvfdsafSYKFGNMkkgqshV 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 305 GVNTLFNALLNNKEFQQLDfSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE-CAPLVSVNPYDIDYhSGSIGLP 383
Cdd:PLN02614 367 EASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDM-LGTVGPP 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 384 VPSTEAKL--VDDDDNEVPPGQP-GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMI-L 459
Cdd:PLN02614 445 VPNVDIRLesVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkL 524
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1728558706 460 VSGFNVYPNEIEDVVMQhpgVQEVAAVGVpSGSSGEAVKIFVVKKDPSLTE 510
Cdd:PLN02614 525 SQGEYVAVENIENIYGE---VQAVDSVWV-YGNSFESFLVAIANPNQQILE 571
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
5.56e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYL-QQGLGLKKgdRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALrERGVGPQV--RVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 102 VNVNPLYTPRELEHQLNDSGASAIVivsnfahtlekvvdktaVQHVILTRMGDqlstakgtvvnfvvkyIKRLVPKYHLP 181
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLL-----------------SDRALFEALGE----------------LPAGVARWCLE 2312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 182 DaisfRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKelvvTALPLYH 261
Cdd:PRK05691 2313 D----DAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG--MRADD----CELHFYS 2382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 262 I-FALTINCLLFIELGGQNLLIT-----NPRDIPGLVKELAkypfTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGm 335
Cdd:PRK05691 2383 InFDAASERLLVPLLCGARVVLRaqgqwGAEEICQLIREQQ----VSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGG- 2457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 336 pvQQVVAERWVKLTG----QYLLEGYGLTECA--PLVSVNPYDIDYHSGS--IGLPVPSTEAKLVDDDDNEVPPGQPGEL 407
Cdd:PRK05691 2458 --EALTGEHLQRIRQafapQLFFNAYGPTETVvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGEL 2535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 408 CVKGPQVMLGYWQRPDATDE-------IIKNGWLH-TGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPG 479
Cdd:PRK05691 2536 YVGGAGLAQGYHDRPGLTAErfvadpfAADGGRLYrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPA 2615
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 480 VQE--VAAVGVPsgsSGEAVKIFVVKKDPSLTE-------ESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 2616 VREavVLALDTP---SGKQLAGYLVSAVAGQDDeaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
357-551 |
3.88e-22 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 99.30 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 357 YGLTECAPLVSVNPYDiDYHSGSIGLPVPSTEAKLvddddnEVPPGQPGELCVKGPQVMLGYWqrPDATDeiiKNGWLHT 436
Cdd:PRK07445 261 YGMTETASQIATLKPD-DFLAGNNSSGQVLPHAQI------TIPANQTGNITIQAQSLALGYY--PQILD---SQGIFET 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 437 GDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTF 516
Cdd:PRK07445 329 DDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTA 408
|
170 180 190
....*....|....*....|....*....|....*...
gi 1728558706 517 CRRQLTGYKVPK---LVEfrdELPKSNVGKILRRELRD 551
Cdd:PRK07445 409 IKDQLSPFKQPKhwiPVP---QLPRNPQGKINRQQLQQ 443
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
74-499 |
1.64e-21 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 97.96 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 74 GDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGasaivivsnfahtlekvvdktaVQHVILTRmg 153
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVG----------------------VTHVLTSK-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 154 dQLSTAKGTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELV---------PEDLAFLQYTGGTTGVAKGA 224
Cdd:PRK06334 123 -QLMQHLAQTHGEDAEYPFSLIYMEEVRKELSFWEKCRIGIYMSIPFEWLMrwfgvsdkdPEDVAVILFTSGTEKLPKGV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 225 MLTHRNMLANLEQVNATYGPLlhpGKELVVTALPLYHIFALTiNCLLFIELGGQNLLIT-NPRDIPGLVKELAKYPFTAI 303
Cdd:PRK06334 202 PLTHANLLANQRACLKFFSPK---EDDVMMSFLPPFHAYGFN-SCTLFPLLSGVPVVFAyNPLYPKKIVEMIDEAKVTFL 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 304 TGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLL-EGYGLTECAPLVSVNPYDIDYHSGSIGL 382
Cdd:PRK06334 278 GSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLrQGYGTTECSPVITINTVNSPKHESCVGM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 383 PVPSTEAKLVDDDDN-EVPPGQPGELCVKGPQVMLGYWQRpDATDEIIKNG---WLHTGDIAVMDEEGFLRIVDRKKDMI 458
Cdd:PRK06334 358 PIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGE-DFGQGFVELGgetWYVTGDLGYVDRHGELFLKGRLSRFV 436
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1728558706 459 LVSGFNVYPNEIEDVVMQHPGVQEVAAVG--VPSGSSGEAVKI 499
Cdd:PRK06334 437 KIGAEMVSLEALESILMEGFGQNAADHAGplVVCGLPGEKVRL 479
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
205-487 |
1.90e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 98.35 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY----GPLLHpgKELVVTALPLYHIFALTINCLLF-------- 272
Cdd:PLN02430 219 PLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMeqfeDKMTH--DDVYLSFLPLAHILDRMIEEYFFrkgasvgy 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 273 ------------IELGgQNLLITNPRDIPGLVKELAKypftAITGVNTL----FNALLN------NKEFQQLDFS----- 325
Cdd:PLN02430 297 yhgdlnalrddlMELK-PTLLAGVPRVFERIHEGIQK----ALQELNPRrrliFNALYKyklawmNRGYSHKKASpmadf 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 326 ------------SLHLSAGGGMPVQQVVaERWVKLTG-QYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLv 392
Cdd:PLN02430 372 lafrkvkaklggRLRLLISGGAPLSTEI-EEFLRVTScAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRL- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 393 ddddNEVPP------GQP--GELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS-GF 463
Cdd:PLN02430 450 ----EEVPEmgydplGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGE 525
|
330 340
....*....|....*....|....
gi 1728558706 464 NVYPNEIEDVVMQHPGVQEVAAVG 487
Cdd:PLN02430 526 YVALEYLENVYGQNPIVEDIWVYG 549
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
34-556 |
6.81e-21 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 96.56 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 34 ARYADQPAFV------NMGEVMTFRKLEERSRAFAAYLQqGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:PRK10524 64 AKRPEQLALIavstetDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 108 YTPRELEHQLNDsgASAIVIVSNFAHTLE-KVVD-KTAVQHVIltrmgdQLSTAKGTVVNFVVKYI--KRLVPKYHLpDA 183
Cdd:PRK10524 143 FASHSLAARIDD--AKPVLIVSADAGSRGgKVVPyKPLLDEAI------ALAQHKPRHVLLVDRGLapMARVAGRDV-DY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 184 ISFRsALHNGYRmqyVKPELVPE-DLAFLQYTGGTTGVAKGAmltHRN-------MLANLEQVNAT-------------- 241
Cdd:PRK10524 214 ATLR-AQHLGAR---VPVEWLESnEPSYILYTSGTTGKPKGV---QRDtggyavaLATSMDTIFGGkagetffcasdigw 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 242 --------YGPLLHPGKELVVTALPLyhifaltincllfielggqnllitnpRDIPGLVKEL-AKYpftaitGVNTLFNA 312
Cdd:PRK10524 287 vvghsyivYAPLLAGMATIMYEGLPT--------------------------RPDAGIWWRIvEKY------KVNRMFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 313 -----LLNNKEFQQL---DFSSLHLSAGGGMPVQQVVAeRWVKLT-GQYLLEGYGLTECA-PLVSVNP--YDIDYHSGSI 380
Cdd:PRK10524 335 ptairVLKKQDPALLrkhDLSSLRALFLAGEPLDEPTA-SWISEAlGVPVIDNYWQTETGwPILAIARgvEDRPTRLGSP 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 381 GLPVPSTEAKLVDDDDNE-VPPGQPGELCVKGP---QVMLGYWqRPDatDEIIKNGWLH-------TGDIAVMDEEGFLR 449
Cdd:PRK10524 414 GVPMYGYNVKLLNEVTGEpCGPNEKGVLVIEGPlppGCMQTVW-GDD--DRFVKTYWSLfgrqvysTFDWGIRDADGYYF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTF---------CRRQ 520
Cdd:PRK10524 491 ILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLalekeimalVDSQ 570
|
570 580 590
....*....|....*....|....*....|....*.
gi 1728558706 521 LTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK 556
Cdd:PRK10524 571 LGAVARPARVWFVSALPKTRSGKLLRRAIQAIAEGR 606
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
469-543 |
3.45e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 84.52 E-value: 3.45e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 469 EIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
205-550 |
3.87e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 93.68 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTALPLYHIFALTIncLLFIELGGQNLLITn 284
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG--LDAATDVGCSWLPLYHDMGLAF--LLTAALAGAPLWLA- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 prdiPglVKELAKYPF-----------TAITGVNTLFNALLN-NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY 352
Cdd:PRK05851 226 ----P--TTAFSASPFrwlswlsdsraTLTAAPNFAYNLIGKyARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPF 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 ------LLEGYGLTE--CAPLVSVnP------YDIDYHSGS-------IGLPVPSTEAKLV-DDDDNEVPPGQPGELCVK 410
Cdd:PRK05851 300 gfdagaAAPSYGLAEstCAVTVPV-PgiglrvDEVTTDDGSgarrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIR 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 411 GPQVMLGYW-QRPDATDEiikngWLHTGDIAVMDEEGfLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQE--VAAVG 487
Cdd:PRK05851 379 GASMMSGYLgQAPIDPDD-----WFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREgaVVAVG 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 488 VPSGS--SGEAVKIFVVKKDPSLTEESLVTFCRRQlTGYkVPKLVEFRD--ELPKSNVGKILRRELR 550
Cdd:PRK05851 453 TGEGSarPGLVIAAEFRGPDEAGARSEVVQRVASE-CGV-VPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
35-560 |
8.92e-20 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 92.24 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 35 RYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELE 114
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQ-QGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 115 HQLNDSGAsaivivsNFAHTLEKVVDKTAVQHViltrmgdqlstakgtvvnfvvkyikrLVPKYHLPDAISFRsalhngy 194
Cdd:PRK09029 94 ELLPSLTL-------DFALVLEGENTFSALTSL--------------------------HLQLVEGAHAVAWQ------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 195 rmqyvkpelvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA--TYGP----LLhpgkelvvtALPLYHIFALTI- 267
Cdd:PRK09029 134 ----------PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSlmPFTAqdswLL---------SLPLFHVSGQGIv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 268 -NCLLfielGGQNLLITNPRDIpglvkelakypFTAITG------VNTLFNALLNNKefqQLDFSSLHLSAGGGM-PV-- 337
Cdd:PRK09029 195 wRWLY----AGATLVVRDKQPL-----------EQALAGcthaslVPTQLWRLLDNR---SEPLSLKAVLLGGAAiPVel 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 -QQVVA---ERWVkltgqylleGYGLTECAPLVSVNPydIDYHSGsIGLPVPSTEAKLVDDddnevppgqpgELCVKGPQ 413
Cdd:PRK09029 257 tEQAEQqgiRCWC---------GYGLTEMASTVCAKR--ADGLAG-VGSPLPGREVKLVDG-----------EIWLRGAS 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 414 VMLGYWQ----RPdATDEiikNGWLHTGDIAVMDEeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVP 489
Cdd:PRK09029 314 LALGYWRqgqlVP-LVND---EGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1728558706 490 SGSSGE---AvkifVVKKDPSLTEESLVTFCRRQLTGYKVPklVEF---RDELPKSNVgKILRRELRDEARGKVDNK 560
Cdd:PRK09029 389 DAEFGQrpvA----VVESDSEAAVVNLAEWLQDKLARFQQP--VAYyllPPELKNGGI-KISRQALKEWVAQQLGNN 458
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-558 |
1.83e-19 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 92.27 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSgASAIVIV 128
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC-KPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SNFAHTLEKVVDKTAVQHVILTRmgdqlSTAKGTVVNFVVKY-----IKRLVPKYHLPDAISFRSALHNgYRMQYVKPEL 203
Cdd:PLN02654 199 CNAVKRGPKTINLKDIVDAALDE-----SAKNGVSVGICLTYenqlaMKREDTKWQEGRDVWWQDVVPN-YPTKCEVEWV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNML----------------------ANLEQVNA----TYGPLLHPGKELVVTAL 257
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMvytattfkyafdykptdvywctADCGWITGhsyvTYGPMLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 258 PLYhifaltincllfielggqnllitnPRdiPGLVKELA-KYPFTAITGVNTLFNALLNNKEFQQLDFS--SLHLSAGGG 334
Cdd:PLN02654 353 PNY------------------------PD--SGRCWDIVdKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 335 MPVQ--------QVVAER--------WVKLTGQYLLegygltecAPLVSVNPYDidyhSGSIGLPVPSTEAKLVDDDDNE 398
Cdd:PLN02654 407 EPINpsawrwffNVVGDSrcpisdtwWQTETGGFMI--------TPLPGAWPQK----PGSATFPFFGVQPVIVDEKGKE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 399 VPPGQPGELCVKGP-----QVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PLN02654 475 IEGECSGYLCVKKSwpgafRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 474 VMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEE---SLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PLN02654 555 LVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGvPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
....*....
gi 1728558706 550 RDEARGKVD 558
Cdd:PLN02654 635 RKIASRQLD 643
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-485 |
8.19e-19 |
|
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: 89.71 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEhqlndsgasaiVIVS 129
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG-----------FLLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 130 NFAHTLEKVVDKTAVQHVILTRmgdqLSTAKGTVVNfvvkyiKRLVPKYHLPDAISFRSALHNgyRMQYVKPELVPEDLA 209
Cdd:cd05905 85 TCKVRVALTVEACLKGLPKKLL----KSKTAAEIAK------KKGWPKILDFVKIPKSKRSKL--KKWGPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 210 FLQYTGGTTGVAKGAMLTHRNMLA---NLEQVNATYgpllhpGKELVVTALPLYHIFALTINCLLFIELGGQNLLI---- 282
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAhcrALKEACELY------ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIppel 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 283 --TNPrdiPGLVKELAKYP-FTAITGVNTLFNALLN---NKEFQQL---DFSSLH-LSAGGGMPVQQVVAERWVKLTGQy 352
Cdd:cd05905 227 mkTNP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDlssTLASLKNrdvNLSSLRmCMVPCENRPRISSCDSFLKLFQT- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 llEGYGLTECAPLVS--VNPYD--------------IDYHSGSIGLPVPSTEAK---LVDDDDNEVPP------------ 401
Cdd:cd05905 303 --LGLSPRAVSTEFGtrVNPFIcwqgtsgpepsrvyLDMRALRHGVVRLDERDKpnsLPLQDSGKVLPgaqvaivnpetk 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 402 -----GQPGELCVKGPQVMLGYWQRPDATDE-------------IIKNGWLHTGDI----------AVMDEEGFLRIVDR 453
Cdd:cd05905 381 glckdGEIGEIWVNSPANASGYFLLDGETNDtfkvfpstrlstgITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGS 460
|
490 500 510
....*....|....*....|....*....|...
gi 1728558706 454 KKDMILVSGFNVYPNEIEDVVMQ-HPGVQEVAA 485
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRvHPYRGRCAV 493
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
207-511 |
1.57e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 89.13 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnleQVNATYGPLLHPGK-----ELVVTALPLYHIFALTINCLLFIELGGQNLL 281
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIA---EVLSTDHLLKVTDRvateeDSYFSYLPLAHVYDQVIETYCISKGASIGFW 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 282 ITNPRDIPGLVKELAKYPFTAI--------TGVN-----------TLFNALLNNK---------------EFQQLDFSSL 327
Cdd:PLN02861 298 QGDIRYLMEDVQALKPTIFCGVprvydriyTGIMqkissggmlrkKLFDFAYNYKlgnlrkglkqeeaspRLDRLVFDKI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 328 --------HLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE-CAPLVS--VNPYDIdyhSGSIGLPVPSTEAKLVD--- 393
Cdd:PLN02861 378 keglggrvRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTsiANVFSM---VGTVGVPMTTIEARLESvpe 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 394 ---DDDNEVPPGqpgELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS-GFNVYPNE 469
Cdd:PLN02861 455 mgyDALSDVPRG---EICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVEN 531
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1728558706 470 IEDVVMQHPgvqEVAAVGVpSGSSGEAVKIFVVKKDPSLTEE 511
Cdd:PLN02861 532 LENTYSRCP---LIASIWV-YGNSFESFLVAVVVPDRQALED 569
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
205-552 |
3.57e-18 |
|
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: 87.49 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYgplLHPGKEL-VVTALPLYHIFALTInCLLFIELGGQNLLIT 283
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVT-SNLLSHD---LNLKNGDrTYTCMPLYHGTAAFL-GACNCLMSGGTLALS 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 284 NPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGM--PVQQVVAERW-VKLTGQYllegYGLT 360
Cdd:cd05937 161 RKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLrpDIWERFRERFnVPEIGEF----YAAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 361 EcAPLVSVNPYDIDYHSGSIGL--------------PV---PSTEAKLVDDDDN---EVPPGQPGELCVKGPQVML---- 416
Cdd:cd05937 237 E-GVFALTNHNVGDFGAGAIGHhglirrwkfenqvvLVkmdPETDDPIRDPKTGfcvRAPVGEPGEMLGRVPFKNReafq 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 417 GYWQRPDATD-----EIIKNG--WLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVP 489
Cdd:cd05937 316 GYLHNEDATEsklvrDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVK 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728558706 490 ----SGSSGEA-VKIFVVKKDPS-LTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:cd05937 396 vpghDGRAGCAaITLEESSAVPTeFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
23-555 |
1.29e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.72 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 23 QSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQglgLKKGDRVALMM-----PNLLqypVALFGILRA 97
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDS---LKLPDKSPIIVfghmsPEML---ATFLGAVKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 98 GMIVVNVNpLYTPRELEHQLNDSGASAIVIvsnfaHTLEKVVDKTAVQHVILTRMGDQLstAKGTVVNFvvkyikrlvpk 177
Cdd:PRK04813 76 GHAYIPVD-VSSPAERIEMIIEVAKPSLII-----ATEELPLEILGIPVITLDELKDIF--ATGNPYDF----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 178 yhlpdaisfrsalhngyrMQYVKPElvpeDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhpGKELVVTAL 257
Cdd:PRK04813 137 ------------------DHAVKGD----DNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL----PEGPQFLNQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 258 PLYHiFALTI----NCLLfieLGGQ-NLL----ITNPRDipgLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSL- 327
Cdd:PRK04813 191 APYS-FDLSVmdlyPTLA---SGGTlVALpkdmTANFKQ---LFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLt 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 328 H-LSAGGGMPVQqvvaerwvklTGQYLLE---------GYGLTECAplVSVNPYDI------DYHSGSIGLPVPSTEAKL 391
Cdd:PRK04813 264 HfLFCGEELPHK----------TAKKLLErfpsatiynTYGPTEAT--VAVTSIEItdemldQYKRLPIGYAKPDSPLLI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 392 VDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIK--NGW--LHTGDIAVMDEeGFLRIVDRKKDMILVSGFNVYP 467
Cdd:PRK04813 332 IDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFtfDGQpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIEL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 468 NEIEDVVMQHPGVQEvaAVGVPSGSSGEAVKI--FVVKKDPSLTEEslvtfcrRQLTG------------YKVPKLVEFR 533
Cdd:PRK04813 411 EEIEQNLRQSSYVES--AVVVPYNKDHKVQYLiaYVVPKEEDFERE-------FELTKaikkelkerlmeYMIPRKFIYR 481
|
570 580
....*....|....*....|..
gi 1728558706 534 DELPKSNVGKILRRELRDEARG 555
Cdd:PRK04813 482 DSLPLTPNGKIDRKALIEEVNK 503
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
24-461 |
1.50e-17 |
|
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: 85.97 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 24 SLVDMFEQSVARYADQPAF------VNMGEV--------------MTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPN 83
Cdd:cd17632 23 RLAQIIATVMTGYADRPALgqrateLVTDPAtgrttlrllprfetITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 84 LLQYPVALFGILRAGMIVVnvnPLYT---PRELEHQLNDSGASAI-VIVSNFAHTLEKVVDKTAVQHVI-------LTRM 152
Cdd:cd17632 103 SPDYATVDLALTRLGAVSV---PLQAgasAAQLAPILAETEPRLLaVSAEHLDLAVEAVLEGGTPPRLVvfdhrpeVDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 153 GDQLSTAKGtvvnfvvkyikRLVPKyhlPDAISFRSALHNGYRMQYVKPELVPED----LAFLQYTGGTTGVAKGAMLTH 228
Cdd:cd17632 180 RAALESARE-----------RLAAV---GIPVTTLTLIAVRGRDLPPAPLFRPEPdddpLALLIYTSGSTGTPKGAMYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 229 RNMLANLEQVNATYGPllHPGKELVVTALPLYHIfaltincllfielGGQNLLITnprdipGLVKELAKYpFTAITGVNT 308
Cdd:cd17632 246 RLVATFWLKVSSIQDI--RPPASITLNFMPMSHI-------------AGRISLYG------TLARGGTAY-FAAASDMST 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 309 LFN--ALLNNKE-----------FQQLDFSSLHLSAGGGMPV---QQVVAE-RWVKLTGQY------------------- 352
Cdd:cd17632 304 LFDdlALVRPTElflvprvcdmlFQRYQAELDRRSVAGADAEtlaERVKAElRERVLGGRLlaavcgsaplsaemkafme 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 ------LLEGYGLTEcAPLVSVNpydidyhsGSIGLPvPSTEAKLVDdddneVP---------PGQPGELCVKGPQVMLG 417
Cdd:cd17632 384 slldldLHDGYGSTE-AGAVILD--------GVIVRP-PVLDYKLVD-----VPelgyfrtdrPHPRGELLVKTDTLFPG 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1728558706 418 YWQRPDATDEII-KNGWLHTGDIavMDEEGFLRI--VDRKKDMILVS 461
Cdd:cd17632 449 YYKRPEVTAEVFdEDGFYRTGDV--MAELGPDRLvyVDRRNNVLKLS 493
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
205-461 |
1.78e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 79.76 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANL-----EQVNATYGPLLHpgkelvVTALPLYHIFALTINCLLFIeLGGQn 279
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTH------LSYLPISHIYERVIAYLSFM-LGGT- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 280 LLITNpRDIPGLVKELAKYPFTAITGVNTLFNALLNN-----------------------KEFQQLDFSSL-----HLSA 331
Cdd:PTZ00342 375 INIWS-KDINYFSKDIYNSKGNILAGVPKVFNRIYTNimteinnlpplkrflvkkilslrKSNNNGGFSKFlegitHISS 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 332 ---------------GGGMPVQQVVAERWVKLTGQYLlEGYGLTECAPLVSVNPYDiDYHSGSIGLPV-PSTEAKLVD-- 393
Cdd:PTZ00342 454 kikdkvnpnlevilnGGGKLSPKIAEELSVLLNVNYY-QGYGLTETTGPIFVQHAD-DNNTESIGGPIsPNTKYKVRTwe 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 394 -DDDNEVPPgqPGELCVKGPQVMLGYWQRPDATDE-IIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVS 461
Cdd:PTZ00342 532 tYKATDTLP--KGELLIKSDSIFSGYFLEKEQTKNaFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
49-546 |
7.35e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 77.47 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLnDSGASAIVIV 128
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRI-ETITPKLIIT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 129 SNFAHTLEKVVD-----KTAVQ-------HVILTRMGDQLSTAKgtvvnfvVKYIKRLVPkyhLPDAISFRSALhNGYRM 196
Cdd:PTZ00237 171 TNYGILNDEIITftpnlKEAIElstfkpsNVITLFRNDITSESD-------LKKIETIPT---IPNTLSWYDEI-KKIKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 197 QYVKP--ELVPEDLA---FLQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLLHPGKELVVtaLPLYHIFALTINCLL 271
Cdd:PTZ00237 240 NNQSPfyEYVPVESShplYILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVV--FSHSSIGWVSFHGFL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 272 FIELGGQNLL------ITNPRDIP-GLVKELAKYPFT-AITGVNTLFNALLNNKEFQQL----DFSSLHLSAGGGMPVQQ 339
Cdd:PTZ00237 315 YGSLSLGNTFvmfeggIIKNKHIEdDLWNTIEKHKVThTLTLPKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIEE 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 340 VVAERWVKLTGQYLLEGYGLTE--CAPLVSVNPYDIDYHSgsIGLPVPSTEAKLVDDDDNEVPPGQPGELCVK---GPQV 414
Cdd:PTZ00237 395 SIPEYIENKLKIKSSRGYGQTEigITYLYCYGHINIPYNA--TGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSF 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 415 MLGYWQRpdatDEIIKN------GWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGV 488
Cdd:PTZ00237 473 ATTFYKN----DEKFKQlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1728558706 489 PSGSSGEA-VKIFVVKKDPSLTEESLVTF-------CRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:PTZ00237 549 YDPDCYNVpIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-561 |
1.36e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.75 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 50 TFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPlytprelehqlnDSGASAI---- 125
Cdd:cd05943 100 TWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSP------------DFGVPGVldrf 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 ------VIVSNFAHTLE-KVVDKTA-VQHVIltrmgDQLSTAKGTVvnfVVKYikrlVPKYHLPDAISFRSALH-NGYRM 196
Cdd:cd05943 167 gqiepkVLFAVDAYTYNgKRHDVREkVAELV-----KGLPSLLAVV---VVPY----TVAAGQPDLSKIAKALTlEDFLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 197 QYVKPELVPEDLAF-----LQYTGGTTGVAKGAMLTHRNMLanLEQVNATygpLLH----PGKEL---VVTALPLYH--I 262
Cdd:cd05943 235 TGAAGELEFEPLPFdhplyILYSSGTTGLPKCIVHGAGGTL--LQHLKEH---ILHcdlrPGDRLfyyTTCGWMMWNwlV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 263 FALTINCLLFIELGgqNLLITNPRDIPGLVKELAkypfTAITGVNTLFNALLNNKEFQQ---LDFSSLH--LSAGGGMPV 337
Cdd:cd05943 310 SGLAVGATIVLYDG--SPFYPDTNALWDLADEEG----ITVFGTSAKYLDALEKAGLKPaetHDLSSLRtiLSTGSPLKP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 338 QQVvaeRWV--KLTGQYLLEGY-GLTE-CAPLVSVNPyDIDYHSGSIGLPVPSTEAKLVDDDDNEVpPGQPGEL-CVKG- 411
Cdd:cd05943 384 ESF---DYVydHIKPDVLLASIsGGTDiISCFVGGNP-LLPVYRGEIQCRGLGMAVEAFDEEGKPV-WGEKGELvCTKPf 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 412 PQVMLGYWQRPDATD------EIIKNGWLHtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAA 485
Cdd:cd05943 459 PSMPVGFWNDPDGSRyraayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 486 VGVPSGSSGEAVKIFVVKKDPSLTEESLV----TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGK-VDNK 560
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDDELRkrirSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKKIIAGRpVKNA 617
|
.
gi 1728558706 561 A 561
Cdd:cd05943 618 G 618
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
320-480 |
9.18e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.85 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 320 QQLDFSSLHLSAG--GGMPV----QQVVAERW-VKLtgqylLEGYGLTECAPLVSvnpYDIDYHSGsigLPVPS----TE 388
Cdd:COG1541 196 EGIDPRDLSLKKGifGGEPWseemRKEIEERWgIKA-----YDIYGLTEVGPGVA---YECEAQDG---LHIWEdhflVE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 389 akLVDDDDNE-VPPGQPGELCV----KGPQVMLGYwqrpdatdeiikngwlHTGDIAVMDEEG---------FLRIVDRK 454
Cdd:COG1541 265 --IIDPETGEpVPEGEEGELVVttltKEAMPLIRY----------------RTGDLTRLLPEPcpcgrthprIGRILGRA 326
|
170 180
....*....|....*....|....*.
gi 1728558706 455 KDMILVSGFNVYPNEIEDVVMQHPGV 480
Cdd:COG1541 327 DDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
37-228 |
2.64e-08 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 56.73 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 37 ADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQQgLGLKKGDRVALMMPNLlqyPVALFGILRA---GMIVVNVNPly 108
Cdd:PRK03584 98 DDRPAIIFRGEdgprrELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNI---PETVVAMLATaslGAIWSSCSP-- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 109 tprelehqlnDSGASAIV-----------IVSNFAHTLEKVVDKTAVqhviLTRMGDQLSTAKGTVvnfVVKYIKRLVPK 177
Cdd:PRK03584 172 ----------DFGVQGVLdrfgqiepkvlIAVDGYRYGGKAFDRRAK----VAELRAALPSLEHVV---VVPYLGPAAAA 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1728558706 178 YHLPDAISFRSALHNgyrmqYVKPELVPEDLAF-----LQYTGGTTGVAK-------GAMLTH 228
Cdd:PRK03584 235 AALPGALLWEDFLAP-----AEAAELEFEPVPFdhplwILYSSGTTGLPKcivhghgGILLEH 292
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
49-552 |
3.31e-08 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 56.63 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 49 MTFRKLEERSRAfAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAI--- 125
Cdd:PLN03052 209 MTLSELRSQVSR-VANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 126 -VIV-SNFAHTL-EKVVDKTAVQHVILTRMGDQLSTakgTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGyrmqyvkpe 202
Cdd:PLN03052 288 dVIVrGGKSIPLySRVVEAKAPKAIVLPADGKSVRV---KLREGDMSWDDFLARANGLRRPDEYKAVEQPV--------- 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 203 lvpEDLAFLQYTGGTTGVAKGAMLTHRNML-------ANLE-QVNATY----------GPLLHPGKELVVTALPLYHIFA 264
Cdd:PLN03052 356 ---EAFTNILFSSGTTGEPKAIPWTQLTPLraaadawAHLDiRKGDIVcwptnlgwmmGPWLVYASLLNGATLALYNGSP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 265 LTINCLLFIELGGQNLLITnprdIPGLVKelakypftaiTGVNTlfNALLNnkefqqLDFSSLHL--SAGGGMPVQQVVa 342
Cdd:PLN03052 433 LGRGFAKFVQDAKVTMLGT----VPSIVK----------TWKNT--NCMAG------LDWSSIRCfgSTGEASSVDDYL- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 343 erWVKLTGQY--LLEGYGLTECAPlvsvnpydiDYHSGSIGLP-------VPSTEAKLV--DDDDNEVPPGQP--GElCV 409
Cdd:PLN03052 490 --WLMSRAGYkpIIEYCGGTELGG---------GFVTGSLLQPqafaafsTPAMGCKLFilDDSGNPYPDDAPctGE-LA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 410 KGPQvMLG-------------YWQ-RPDATDEIIKNgwlHtGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PLN03052 558 LFPL-MFGasstllnadhykvYFKgMPVFNGKILRR---H-GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 476 Q-HPGVQEVAAVGVPSGSSG-EAVKIFVVKKDPSLTEESLVTFCRRQLTG--------YKVPKLVEFrDELPKSNVGKIL 545
Cdd:PLN03052 633 AaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLNELKKIFNSAiqkklnplFKVSAVVIV-PSFPRTASNKVM 711
|
....*..
gi 1728558706 546 RRELRDE 552
Cdd:PLN03052 712 RRVLRQQ 718
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
205-549 |
1.58e-07 |
|
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: 54.02 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVVTALPLYHIFALTIncllFIELGGQNLLITN 284
Cdd:cd17654 117 DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN--ITSEDILFLTSPLTFDPSVVEI----FLSLSSGATLLIV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 285 PRDIPGLVKELAKYPFTA--ITGVN---TLFNALLN--NKEFQQLDFSSLHLSAGGGMP-VQQVVAERWV-KLTGQYLLE 355
Cdd:cd17654 191 PTSVKVLPSKLADILFKRhrITVLQatpTLFRRFGSqsIKSTVLSATSSLRVLALGGEPfPSLVILSSWRgKGNRTRIFN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 356 GYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEvppgQPGELCVKGpQVMLGYWQRPDATdeiIKNGWLH 435
Cdd:cd17654 271 IYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTGQVFLGG-LNRVCILDDEVTV---PKGTMRA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 436 TGDIaVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAvgvpSGSSGEAVKIFVVkkdpsLTEESLVT 515
Cdd:cd17654 343 TGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV----TLSDQQRLIAFIV-----GESSSSRI 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 1728558706 516 FCRRQLTG---YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17654 413 HKELQLTLlssHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
392-480 |
8.94e-07 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 51.47 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 392 VDDDDNE-VPPGQPGE-----LCVKGPQVmLGYWqrpdaTDEIIKNGWLH--TGDIAVMDEegflRIVDRKKDMILVSGF 463
Cdd:cd05913 262 IDPETGEpVPPGEVGElvfttLTKEAMPL-IRYR-----TRDITRLLPGPcpCGRTHRRID----RITGRSDDMLIIRGV 331
|
90
....*....|....*..
gi 1728558706 464 NVYPNEIEDVVMQHPGV 480
Cdd:cd05913 332 NVFPSQIEDVLLKIPGL 348
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
276-539 |
5.45e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 49.33 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 276 GGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvqqvvAERWVKLTGQY--- 352
Cdd:PRK07868 671 GGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMP-----TGLWERVVEAFapa 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 353 -LLEGYGLTEC-APLVSVNPYDIdyhsGSIGLPVPST-----------EAKLVDDDD---NEVPPGQPGELCVK--GP-- 412
Cdd:PRK07868 746 hVVEFFATTDGqAVLANVSGAKI----GSKGRPLPGAgrvelaaydpeHDLILEDDRgfvRRAEVNEVGVLLARarGPid 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 413 ---QVMLGYWQRPDAtdeiikngWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVP 489
Cdd:PRK07868 822 ptaSVKRGVFAPADT--------WISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVE 893
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1728558706 490 SGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKvPKLVEFRDELPKS 539
Cdd:PRK07868 894 VGGRQLAVAAVTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLS 942
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
437-554 |
6.40e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 45.58 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728558706 437 GDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HPGVQEVAAVGV-PSGSSGEAVKIFVVKKDPSLT----- 509
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVaPPDGGPELLVIFLVLGEEKKGfdqar 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1728558706 510 EESLVTFCRRQLTG-----YKVPKlVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PLN03051 442 PEALQKKFQEAIQTnlnplFKVSR-VKIVPELPRNASNKLLRRVLRDQLK 490
|
|
| |
