|
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 505808171 1 MKKVWLNRYPADVPAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALM 80
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAK 160
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 TYGPLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQ 320
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 321 QLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVA 400
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 401 PGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 481 QEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 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: 894.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 1 MKKVWLNRYPADVPAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALM 80
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQ-SRGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLStAK 160
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLG-FK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK07059 159 GHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 TYGPLLHRGKE----LVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN 316
Cdd:PRK07059 239 WLQPAFEKKPRpdqlNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 317 KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDD 396
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 NEVAPGEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 476 QHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 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: 815.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 5 WLNRYPADVPAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNL 84
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 165 NFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGP 244
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 245 LLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDF 324
Cdd:PRK05677 246 NLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 325 SSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEP 404
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 405 GELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEV 483
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQC 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 484 AAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
Cdd:PRK05677 485 AAIGVPDEKSGEAIKVFVVvKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGLK 562
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
5-555 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 768.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 5 WLNRYPADVPAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNL 84
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 165 NFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN---AT 241
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHqwlAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 242 YGPLLhRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ 321
Cdd:PRK08751 247 TGKLE-EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 322 LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAP 401
Cdd:PRK08751 326 IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 GEPGELCIKGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK08751 406 GEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 481 QEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
Cdd:PRK08751 486 LEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| 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: 729.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 5 WLNRYPADVPAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNL 84
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 165 NFVVKYIKRLVPKYHLPDAISFRSALQHGyRMQYVKPEIVA-DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG 243
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQG-RGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 244 -------PLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN 316
Cdd:PRK12492 245 qlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 317 KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDD 396
Cdd:PRK12492 325 PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 NEVAPGEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 476 QHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDIA 562
|
|
| 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: 722.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 25 LVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDSGAAAIVIvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdAI 184
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 185 SFRSALQHGYRMQYvKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlHRGKELVVTALPLYHIFA 264
Cdd:cd05936 105 SFTDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDL-LEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LTMNCLLFIELGGQNLLITNPRDIpGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAER 344
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 345 WVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDA 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 425 TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKK 504
Cdd:cd05936 342 TAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 505808171 505 D-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05936 422 EgASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-556 |
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: 575.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 25 LVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDSGAAAIVIvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdai 184
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 185 sfrsalqhgyrmqyvkpeivaddlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFA 264
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG---LTPGDVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LTMNCLLFIELGGQNLLITNpRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAER 344
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 345 WVKLTGQYLLEGYGLTECSPLVSVNPHDIDY-HSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPD 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPGErRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 424 ATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVK 503
Cdd:COG0318 315 ATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 505808171 504 KD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:COG0318 395 RPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-552 |
5.43e-175 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 506.85 E-value: 5.43e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 3 KVWLNRYPADVPAEINPDRyQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMP 82
Cdd:PRK05605 13 KPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 83 NLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGT 162
Cdd:PRK05605 91 NCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 163 LVNFVVKYIKRLVPKYH--LPDAISFRSALQH---GYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ 237
Cdd:PRK05605 171 ALRLPIPALRKARAALTgpAPGTVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 238 VNAtYGPLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNK 317
Cdd:PRK05605 251 GKA-WVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 318 EFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDD- 396
Cdd:PRK05605 329 EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 -NEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK05605 409 dETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 476 QHSGVQEVAAVGVPSGSSGEAVKIFVVKKD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-552 |
4.42e-157 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 458.60 E-value: 4.42e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKT-QVKHVILTRMGDqlstakgtlvnfvvkyikrlvPKYHLP 181
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEE---------------------DDPHTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 182 DAISFRSALQHGYRmQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhRGKELVVTALPLYH 261
Cdd:PRK07656 143 KMKTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADW-AEYLGL--TEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 262 IFALT--MN-CLLfielGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MP 336
Cdd:PRK07656 219 VFGYKagVNaPLM----RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 337 VQQVvaERWVKLTG-QYLLEGYGLTECSPLVSVNPHDID--YHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQ 413
Cdd:PRK07656 295 VALL--ERFESELGvDIVLTGYGLSEASGVTTFNRLDDDrkTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGS 492
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDaDGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 493 SGEAVKIFVVKKD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07656 453 LGEVGKAYVVLKPgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-560 |
2.30e-149 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 441.01 E-value: 2.30e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 1 MKKVWLNRYPADVPAEINPDrYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALM 80
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTISYD-IQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAK 160
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLAN-LEQVN 239
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtLMGVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 240 ATYGplLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLItnPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKE 318
Cdd:PRK06710 241 WLYN--CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 319 FQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNE 398
Cdd:PRK06710 317 LKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLETGE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 399 V-APGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:PRK06710 397 AlPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 478 SGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRK 556
|
....
gi 505808171 557 VDNK 560
Cdd:PRK06710 557 NEDE 560
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-551 |
1.83e-147 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 434.61 E-value: 1.83e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 20 DRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 100 IAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQ-VKHVILTRMGDQLSTAkgtlvnfvvkyikrlvpky 178
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPLA------------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 179 hlPDAISFRSALQHGYRmQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtyGPLLHRgKELVVTALP 258
Cdd:PRK06187 143 --PEVGEYEELLAAASD-TFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA--WLKLSR-DDVYLVIVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 LYHIFALTMnCLLFIELGGQNLLItnPRDIPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPV 337
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVIP--RRFDPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 338 QQVVAERWVKLTGQYLLEGYGLTECSPLVSVNP---HDIDY--HSGSIGLPVPSTEAKLVDDDDNEVAP--GEPGELCIK 410
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 411 GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPS 490
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 491 GSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 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 |
1.44e-145 |
|
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: 426.64 E-value: 1.44e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 29 FEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 109 TPRELEHQLNDSGAAAIVivsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrs 188
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 189 alqhgyrmqyvkpeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATY-GPLLHRGKELVVtaLPLYHIFALTM 267
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNA--VNALAaLDLGPDDVLLVV--APLFHIGGLGV 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 268 NCLLFIELGGQNLLITNPRdiPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWv 346
Cdd:cd17631 157 FTLPTLLRGGTVVILRKFD--PETVLDLiERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 KLTGQYLLEGYGLTECSPLVSVNPH-DIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDAT 425
Cdd:cd17631 234 QARGVKFVQGYGMTETSPGVTFLSPeDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEAT 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 426 DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD 505
Cdd:cd17631 314 AAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 505808171 506 -AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17631 394 gAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
29-461 |
3.32e-137 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 404.39 E-value: 3.32e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 29 FEHATTRYADQPAFINM-GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 108 YTPRELEHQLNDSGAAAIVIVSNFahTLEKVVDKTQ-VKHVILTRMGDQLSTAKGTLVNFVVKYIKRLVPKYHLPDaisf 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsalqhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLL-HRGKELVVTALPLYHIFAL 265
Cdd:pfam00501 154 ------------------PDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFgLGPDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 266 TMNCLLFIELGGQNLLI--TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAE 343
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHS--GSIGLPVPSTEAKLVDDDD-NEVAPGEPGELCIKGPQVMLGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRslGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 505808171 421 RPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:pfam00501 376 DPELTAEaFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
41-545 |
1.77e-133 |
|
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: 397.35 E-value: 1.77e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 41 AFIN--MGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLN 118
Cdd:cd05911 1 AQIDadTGKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 119 DSGAAaIVIVSNfaHTLEKVVDKTQ----VKHVILTRMGDQLSTAKGTLVNFVVKYIKRLVPKYhlpdaisfrsalqhgy 194
Cdd:cd05911 80 ISKPK-VIFTDP--DGLEKVKEAAKelgpKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPP---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 195 rmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRgKELVVTALPLYHIFAL--TMNCLLF 272
Cdd:cd05911 141 ------LKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGS-NDVILGFLPLYHIYGLftTLASLLN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 273 ielgGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ- 351
Cdd:cd05911 214 ----GATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNa 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 352 YLLEGYGLTECSPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDDDNE-VAPGEPGELCIKGPQVMLGYWQRPDATDEII- 429
Cdd:cd05911 290 TIKQGYGMTETGGILTVNP-DGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFd 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 430 KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-L 508
Cdd:cd05911 369 EDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEkL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505808171 509 TEEALITFCRRHLTGYKvpKL---VEFRDELPKSNVGKIL 545
Cdd:cd05911 449 TEKEVKDYVAKKVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-556 |
2.43e-132 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 396.64 E-value: 2.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 104 VNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKG-TLVNFVVKyiKRLVPKYHLPD 182
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEiAVPAWLRA--EPPLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 AISFRSALQHGYRmqyvKPEIVA--DDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvnaTYGPLLHRG--KELVVTA-L 257
Cdd:PRK08314 169 VVAWKEALAAGLA----PPPHTAgpDDLAVLPYTSGTTGVPKGCMHTHRTVMAN------AVGSVLWSNstPESVVLAvL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHI--FALTMNCLLFieLGGQNLLITN-PRDIPGLVkeLAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGG 334
Cdd:PRK08314 239 PLFHVtgMVHSMNAPIY--AGATVVLMPRwDREAAARL--IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 335 MPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDDD-NEVAPGEPGELCIKGPQ 413
Cdd:PRK08314 315 AAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD-RPKLQCLGIPTFGVDARVIDPETlEELPPGEVGEIVVHGPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYWQRPDATDE--IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVP 489
Cdd:PRK08314 394 VFKGYWNRPEATAEafIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 490 SGSSGEAVKIFVVKKDAA---LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK08314 474 DPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
14-552 |
4.99e-124 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 374.65 E-value: 4.99e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 14 PAEINPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 94 ILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLvnfvvkyikr 173
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 174 lvpkyhlpdaiSFRSALQHGYRMQyVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvnatYGPLLHRGK--- 250
Cdd:PRK08316 151 -----------DFADWAEAGSVAE-PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAE-------YVSCIVAGDmsa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 251 -ELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHL 329
Cdd:PRK08316 212 dDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 330 SAGGG--MPVQqVVAERWVKLTGQYLLEGYGLTECSPLVSV-NPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGE 406
Cdd:PRK08316 291 GYYGAsiMPVE-VLKELRERLPGLRFYNCYGQTEIAPLATVlGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 407 LCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAV 486
Cdd:PRK08316 370 IVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 487 GVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 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 |
3.81e-120 |
|
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: 357.75 E-value: 3.81e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFAltMNCLLFIELGGQNLLITNPR 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL---TEGDVFLSTLPLFHIGG--LFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLV 366
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 367 SVN-PHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDE 445
Cdd:cd04433 156 ATGpPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 446 GFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEEALITFCRRHLTGY 524
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 505808171 525 KVPKLVEFRDELPKSNVGKIL 545
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-553 |
8.73e-115 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 352.04 E-value: 8.73e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 5 WLNRYPADVPAEIN-PDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPN 83
Cdd:PRK06178 14 QQAAWPAGIPREPEyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ-RGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 84 LLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTL 163
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 164 VNFVVKyikrlVPKYHLPDAISFRSALqHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYG 243
Cdd:PRK06178 173 LPDSLR-----APRLAAAGAIDLLPAL-RACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA----AAAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 244 PLLHRGKELVVTA--LPLYHIfALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ 321
Cdd:PRK06178 243 AVAVVGGEDSVFLsfLPEFWI-AGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 322 LDFSSLhlsagggmpvQQVVA------------ERWVKLTGQYLLEG-YGLTE---CSPLVS-VNPHDIDYHSGSI--GL 382
Cdd:PRK06178 322 YDLSSL----------RQVRVvsfvkklnpdyrQRWRALTGSVLAEAaWGMTEthtCDTFTAgFQDDDFDLLSQPVfvGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 383 PVPSTEAKLVDDDDNEVAP-GEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPlGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 462 GFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKlVEFRDELPKSN 540
Cdd:PRK06178 472 GMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTA 550
|
570
....*....|...
gi 505808171 541 VGKILRRELRDEA 553
Cdd:PRK06178 551 TGKVRKQDLQALA 563
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
35-549 |
1.06e-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: 347.30 E-value: 1.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 35 RYADQPAFIN--MGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRE 112
Cdd:cd05904 17 AHPSRPALIDaaTGRALTYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 113 LEHQLNDSGAAAIVIVSNfahTLEKVVDktqvkhviltrmgdqlstakgtLVNFVVkyikrLVPKYH-LPDAISFRSALQ 191
Cdd:cd05904 96 IAKQVKDSGAKLAFTTAE---LAEKLAS----------------------LALPVV-----LLDSAEfDSLSFSDLLFEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 192 HGYrmQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGkELVVTALPLYHIFALTMNCLL 271
Cdd:cd05904 146 DEA--EPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE-DVFLCVLPMFHIYGLSSFALG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 272 FIELGGQnLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLH-LSAGG---GMPVQQVVAER--W 345
Cdd:cd05904 223 LLRLGAT-VVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRqIMSGAaplGKELIEAFRAKfpN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 346 VKLtgqylLEGYGLTECSPLVSV--NPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAP-GEPGELCIKGPQVMLGYWQRP 422
Cdd:cd05904 302 VDL-----GQGYGMTESTGVVAMcfAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPpNQTGELWIRGPSIMKGYLNNP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 423 DATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV 501
Cdd:cd05904 377 EATAAtIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 505808171 502 VKK-DAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05904 457 VRKpGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-553 |
1.34e-107 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 333.32 E-value: 1.34e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPA--FINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPN-----LLQYPVAlfgilRAGM 99
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNvpewvLTQFATA-----KIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 100 IAVNVNPLYTPRELEHQLNDSGAAAIVIV-----SNFAHTLEKVVD--KTQ------------VKHVIltRMGDQlsTAK 160
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAAdgfkdSDYVAMLYELAPelATCepgqlqsarlpeLRRVI--FLGDE--KHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 GTLvNFvvkyikrlvpkyhlpDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK08315 170 GML-NF---------------DELLALGRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 T--YGPllhrgKELVVTALPLYHIFAL---TMNCLLFielgGQNLLITNPRDIPGLV-KELAKYPFTAMTGVNTLFNALL 314
Cdd:PRK08315 234 AmkLTE-----EDRLCIPVPLYHCFGMvlgNLACVTH----GATMVYPGEGFDPLATlAAVEEERCTALYGVPTMFIAEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 315 NNKEFQQLDFSSLH--LSAGGGMPV---QQVVAErwvkltgQYLLE---GYGLTECSPlVSV--NPHD-IDYHSGSIGLP 383
Cdd:PRK08315 305 DHPDFARFDLSSLRtgIMAGSPCPIevmKRVIDK-------MHMSEvtiAYGMTETSP-VSTqtRTDDpLEKRVTTVGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 384 VPSTEAKLVDDDDNE-VAPGEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PRK08315 377 LPHLEVKIVDPETGEtVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 462 GFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSN 540
Cdd:PRK08315 457 GENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIIlRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTV 536
|
570
....*....|...
gi 505808171 541 VGKILRRELRDEA 553
Cdd:PRK08315 537 TGKIQKFKMREMM 549
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
13-556 |
1.18e-105 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 328.61 E-value: 1.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 13 VPAEINP-----DRyqslvelfeHATTRyADQPAFINMGE-----VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMP 82
Cdd:COG0365 4 VGGRLNIaynclDR---------HAEGR-GDKVALIWEGEdgeerTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 83 NLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVIltrmgDQLSTAKGT 162
Cdd:COG0365 73 NIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAL-----EELPSLEHV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 163 LVnfvvkyIKRLVPKYHLPDAISFRSALQHGyrMQYVKPEIV-ADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV--- 238
Cdd:COG0365 148 IV------VGRTGADVPMEGDLDWDELLAAA--SAEFEPEPTdADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTaky 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 239 -----------------------NATYGPLLHRGKELVVTALPLYhifaltmncllfielggqnlliTNPRDipgLVKEL 295
Cdd:COG0365 220 vldlkpgdvfwctadigwatghsYIVYGPLLNGATVVLYEGRPDF----------------------PDPGR---LWELI 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 296 AKYPFTAMTGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE-CSPLVSvNPHD 372
Cdd:COG0365 275 EKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFIS-NLPG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 373 IDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQ--VMLGYWQRPDATDEIIKD---GWLHTGDIAVMDDEGF 447
Cdd:COG0365 354 LPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGY 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 448 LRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEE---ALITFCRRHLTG 523
Cdd:COG0365 434 FWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVlKPGVEPSDElakELQAHVREELGP 513
|
570 580 590
....*....|....*....|....*....|...
gi 505808171 524 YKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:COG0365 514 YAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-549 |
1.67e-104 |
|
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: 320.97 E-value: 1.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIV 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 SNFahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivaDDL 208
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNpRDI 288
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL---TPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-WDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 289 PGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSV 368
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 369 NPHdIDYHSGSIGLPVPSTEAKLVD-DDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKDG---WLHTGDIAVMD 443
Cdd:cd05935 243 NPP-LRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsFIEIKgrrFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD---AALTEEALITFCRRH 520
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyrGKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....*....
gi 505808171 521 LTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-554 |
5.04e-104 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 322.19 E-value: 5.04e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKgtlvnfvvkyIKRLVPKYhlpdaisfrsalqhgyrmq 197
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVISITSLKEIEDRK----------IDNFVEKN------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLhRGKELVVTALPLYHIFALTMNCLLFIELGG 277
Cdd:PRK06839 148 -------ESASFIICYTSGTTGKPKGAVLTQENMFWN--ALNNTFAIDL-TMHDRSIVLLPLFHIGGIGLFAFPTLFAGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 QnLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGG----MPVQQVVAERwvkltGQYL 353
Cdd:PRK06839 218 V-IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GFLF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 354 LEGYGLTECSPLV-SVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDG 432
Cdd:PRK06839 292 GQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEE 511
Cdd:PRK06839 372 WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSvLIEK 451
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 505808171 512 ALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PRK06839 452 DVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-550 |
4.06e-101 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 315.39 E-value: 4.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEER-SRAFAAYlqQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVN 105
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRiSRYIQAF--EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 106 PLYTPRELEHQLNDSGAAAIVIvsnfahtlekvvdkTQVKHVilTRMGDQLSTAKGtlvnfvvkyIKRLVPKYHLPDAIS 185
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLIV--------------DPAPFV--ERALALLARVPS---------LKHVLTLGPVPDGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 186 FrSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKELVVTalPLYHIFAL 265
Cdd:PRK06188 149 L-LAAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE-WPADPRFLMCT--PLSHAGGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 266 TMNCLLfieLGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW 345
Cdd:PRK06188 225 FFLPTL---LRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 346 VKLTGQYLLEGYGLTECSPLVSVNP---HDID--YHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQ 420
Cdd:PRK06188 302 IERFGPIFAQYYGQTEAPMVITYLRkrdHDPDdpKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 421 RPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIF 500
Cdd:PRK06188 382 RPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 505808171 501 VV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK06188 462 VVlRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
20-550 |
1.35e-98 |
|
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: 308.53 E-value: 1.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 20 DRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:cd05959 1 EKYNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 100 IAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKgtlvnfvVKYIKRLVPKyh 179
Cdd:cd05959 80 VPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAG-------ALLLAELVAA-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 180 lpDAISFRSALQHgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLH-RGKELVVTAL 257
Cdd:cd05959 151 --EAEQLKPAATH------------ADDPAFWLYSSGSTGRPKGVVHLHADIYWTAE----LYArNVLGiREDDVCFSAA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHIFALTmNCLLF-IELGGQNLLITNpRDIPGLV-KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHL--SAGG 333
Cdd:cd05959 213 KLFFAYGLG-NSLTFpLSVGATTVLMPE-RPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLcvSAGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPVQqvVAERWVKLTGQYLLEGYGLTECSPLVSVN-PHDIDYhsGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGP 412
Cdd:cd05959 291 ALPAE--VGERWKARFGLDILDGIGSTEMLHIFLSNrPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 413 QVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGS 492
Cdd:cd05959 367 SSATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505808171 493 SGEAVKIFVVKKD-----AALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05959 447 GLTKPKAFVVLRPgyedsEALEEE-LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
19-553 |
1.77e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 309.78 E-value: 1.77e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 19 PDRYQSLVELFEHATTRYADQPAFI--NMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 97 AGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFahtlekvvdKTQVKHVILTRMGDQL-STAKGTLVNFVVKYIKRLV 175
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAF---------KTSDYHAMLQELLPGLaEGQPGALACERLPELRGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 176 -------PKYHLPDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHR 248
Cdd:PRK12583 164 slapappPGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 249 GKELVVtALPLYHIFALTMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLH 328
Cdd:PRK12583 242 HDRLCV-PVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 329 LSAGGGMPVQQVVAERWVK-LTGQYLLEGYGLTECSPLV--SVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPG 405
Cdd:PRK12583 321 TGIMAGAPCPIEVMRRVMDeMHMAEVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 406 ELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVA 484
Cdd:PRK12583 401 ELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 485 AVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK12583 481 VFGVPDEKYGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
10-554 |
1.14e-97 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 309.96 E-value: 1.14e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 10 PADVPA-EINP----DRYQSLVELFEHATTRYADQPA---FIN-----MGEVMTYRKLEER-SRAfaAYLQQGLGLQKGD 75
Cdd:PRK07529 7 LADIEAiEAVPlaarDLPASTYELLSRAAARHPDAPAlsfLLDadpldRPETWTYAELLADvTRT--ANLLHSLGVGPGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 76 RVALMMPNLLQYPVALFGILRAGmIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVDK-TQVKHVIL 149
Cdd:PRK07529 85 VVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAAlPELRTVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 150 TRMGDQLSTAKGTLVNFVVKYIKRLVPKYHlpDAIsfrsALQHGYRMQYVKPeIVADDLAFLQYTGGTTGVAKGAMLTHR 229
Cdd:PRK07529 164 VDLARYLPGPKRLAVPLIRRKAHARILDFD--AEL----ARQPGDRLFSGRP-IGPDDVAAYFHTGGTTGMPKLAQHTHG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 230 NMLANLEQVNATygpLLHRGKELVVTALPLYHIFALTMNCLLFIeLGGQNLLITNP---RDiPGLVKEL----AKYPFTA 302
Cdd:PRK07529 237 NEVANAWLGALL---LGLGPGDTVFCGLPLFHVNALLVTGLAPL-ARGAHVVLATPqgyRG-PGVIANFwkivERYRINF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 303 MTGVNTLFNALLnnkefQQ----LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSG 378
Cdd:PRK07529 312 LSGVPTVYAALL-----QVpvdgHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 379 SIGLPVPSTEAKLVDDDDN-----EVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDR 453
Cdd:PRK07529 387 SVGLRLPYQRVRVVILDDAgrylrDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 454 KKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAALTEEALITFCRRHLTG-YKVPKLVE 531
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHVR 546
|
570 580
....*....|....*....|....
gi 505808171 532 FRDELPKSNVGKILRRELR-DEAR 554
Cdd:PRK07529 547 ILDALPKTAVGKIFKPALRrDAIR 570
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-551 |
8.16e-95 |
|
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: 298.07 E-value: 8.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 37 ADQPAFI--NMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELE 114
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 115 HQLNDSGAAaivivsnfahtlekvvdktqvkhVILTRMGDQLSTAKGTLVnfVVKYIKRL---VPKYHLPDAISFRSALQ 191
Cdd:cd05926 80 FYLADLGSK-----------------------LVLTPKGELGPASRAASK--LGLAILELaldVGVLIRAPSAESLSNLL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 192 HGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKELVVtaLPLYHIFALtMNCLL 271
Cdd:cd05926 135 ADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK-LTPDDRTLVV--MPLFHVHGL-VASLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 272 FIELGGQNLLITnPRDIPGLV-KELAKYPFTAMTGVNTLFNALLNN------KEFQQLDF---SSLHLSAgggmpvqqVV 341
Cdd:cd05926 211 STLAAGGSVVLP-PRFSASTFwPDVRDYNATWYTAVPTIHQILLNRpepnpeSPPPKLRFirsCSASLPP--------AV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 342 AERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHS-GSIGLPVpSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQ 420
Cdd:cd05926 282 LEALEATFGAPVLEAYGMTEAAHQMTSNPLPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 421 RPDATDEI-IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKI 499
Cdd:cd05926 361 NPEANAEAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 505808171 500 FVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 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 |
1.11e-94 |
|
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: 295.35 E-value: 1.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIvs 129
Cdd:cd05934 5 TYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 nfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivadDLA 209
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLaNLEQVNATYGPLlhRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLItnPRDIP 289
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLT-FAGYYSARRFGL--GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 290 -GLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVA--ERWvkltGQYLLEGYGLTEcSPLV 366
Cdd:cd05934 160 sRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEfeERF----GVRLLEGYGMTE-TIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 367 SVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIK---GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMD 443
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLT 522
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVlRPGETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 505808171 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-487 |
1.41e-92 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 295.47 E-value: 1.41e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 19 PDRYQSLVELFEHATTRYADQPAFINMG----EVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGI 94
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 95 LRAGmiAVNVnPLY---TPRELEHQLNDSGAAaIVIVSNFAH--TLEKVVDKT-QVKHVILTRMGDQLSTAKgtlvnfvV 168
Cdd:COG1022 86 LAAG--AVTV-PIYptsSAEEVAYILNDSGAK-VLFVEDQEQldKLLEVRDELpSLRHIVVLDPRGLRDDPR-------L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 169 KYIKRLVP---KYHLPDAISFRSAlqhgyrmqyvkpEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPl 245
Cdd:COG1022 155 LSLDELLAlgrEVADPAELEARRA------------AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 246 lhRGKELVVTALPLYHIFALTMnCLLFIELGGQnllITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN--------K 317
Cdd:COG1022 222 --GPGDRTLSFLPLAHVFERTV-SYYALAAGAT---VAFAESPDTLAEDLREVKPTFMLAVPRVWEKVYAGiqakaeeaG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 318 EFQQLDFS---------SLHLSAGGGMP----VQQVVAERWV--KL---------------------TGQY-------LL 354
Cdd:COG1022 296 GLKRKLFRwalavgrryARARLAGKSPSlllrLKHALADKLVfsKLrealggrlrfavsggaalgpeLARFfralgipVL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLvddddnevapGEPGELCIKGPQVMLGYWQRPDATDE-IIKDGW 433
Cdd:COG1022 376 EGYGLTETSPVITVNRPG-DNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEaFDADGW 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 434 LHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:COG1022 445 LHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-551 |
1.69e-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: 285.34 E-value: 1.69e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVivsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmq 197
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivadDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-VNA-TYGP---LLHrgkelvvtALPLYHIFAL--TMNCL 270
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVRAlVDAwRWTEddvLLH--------VLPLHHVHGLvnALLCP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 271 LFIelggQNLLITNPRDIPGLVKEL-AKYPFTAMTGVNTLFNALL--NNKEFQQLDFSS--------LHLSAGGGMPVQq 339
Cdd:cd05941 153 LFA----GASVEFLPKFDPKEVAISrLMPSITVFMGVPTIYTRLLqyYEAHFTDPQFARaaaaerlrLMVSGSAALPVP- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 340 vVAERWVKLTGQYLLEGYGLTECSPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAP-GEPGELCIKGPQVMLGY 418
Cdd:cd05941 228 -TLEEWEAITGHTLLERYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQARIVDEETGEPLPrGEVGEIQVRGPSVFKEY 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 419 WQRPDAT-DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEA 496
Cdd:cd05941 306 WNKPEATkEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 497 VKIFVVKKD--AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05941 386 VVAVVVLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-550 |
7.11e-89 |
|
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: 278.01 E-value: 7.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygpLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNP 285
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGER---LGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 286 RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTG-QYLLEGYGLTECSP 364
Cdd:cd05917 79 FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 365 LVSVN-PHD-IDYHSGSIGLPVPSTEAKLVDDDDNEVAP-GEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIA 440
Cdd:cd05917 159 VSTQTrTDDsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 441 VMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAALTEEALITFCRR 519
Cdd:cd05917 239 VMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrLKEGAELTEEDIKAYCKG 318
|
330 340 350
....*....|....*....|....*....|.
gi 505808171 520 HLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05917 319 KIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-551 |
9.47e-88 |
|
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: 277.68 E-value: 9.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVivs 129
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 nfahtlekvVDktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivADDLA 209
Cdd:cd05972 78 ---------TD----------------------------------------------------------------AEDPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHRGKELVVTALP--LYHIFALTMNCLLfieLGGQNLLITNPR- 286
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDIHWNIADPgwAKGAWSSFFGPWL---LGATVFVYEGPRf 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKELAKYPFTAMTGVNTLFNaLLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLV 366
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 367 SvNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIK--GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDD 444
Cdd:cd05972 239 G-NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-----LTEEaLITFCRR 519
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYepseeLAEE-LQGHVKK 396
|
490 500 510
....*....|....*....|....*....|..
gi 505808171 520 HLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
28-550 |
3.67e-86 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 276.86 E-value: 3.67e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 28 LFEHATtRYADQPAFIN--MGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVN 105
Cdd:PLN02246 29 CFERLS-EFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 106 PLYTPRELEHQLNDSGAAAIVIVSNFAhtlEKVVDKTQVKHVILTRMGDQlstakgtlvnfvvkyikrlvpkyhlPDAIS 185
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQSCYV---DKLKGLAEDDGVTVVTIDDP-------------------------PEGCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 186 FRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLH-RGKELVVTALPLYHIFA 264
Cdd:PLN02246 159 HFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYfHSDDVILCVLPMFHIYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LtmNCLLFIEL-GGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVaE 343
Cdd:PLN02246 239 L--NSVLLCGLrVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKEL-E 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWV--KLTGQYLLEGYGLTECSPLVSVNP----HDIDYHSGSIGLPVPSTEAKLVDDDDNEVAP-GEPGELCIKGPQVML 416
Cdd:PLN02246 316 DAFraKLPNAVLGQGYGMTEAGPVLAMCLafakEPFPVKSGSCGTVVRNAELKIVDPETGASLPrNQPGEICIRGPQIMK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 417 GYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGE 495
Cdd:PLN02246 396 GYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 496 AVKIFVVK-KDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PLN02246 476 VPVAFVVRsNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-550 |
7.61e-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: 265.09 E-value: 7.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 39 QPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLN 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALR-NLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 119 DSgAAAIVIVSnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqy 198
Cdd:cd05919 80 DC-EARLVVTS--------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 199 vkpeivADDLAFLQYTGGTTGVAKGAMLTHRNML--ANLEQVNAtygpLLHRGKELVVTALPLYHIFALTMNCLLFIELG 276
Cdd:cd05919 90 ------ADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAREA----LGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEG 356
Cdd:cd05919 160 ASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 357 YGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHT 436
Cdd:cd05919 240 IGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 437 GDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALI-- 514
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLArd 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 505808171 515 --TFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05919 399 ihRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
28-552 |
1.29e-82 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 266.74 E-value: 1.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 28 LFEHATTRYADQPA-FINM--GEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMM----PNLLQYpvalFGILRAGMI 100
Cdd:PRK07514 5 LFDALRAAFADRDApFIETpdGLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVekspEALALY----LATLRAGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 101 AVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHViLTRMGDqlstAKGTLvnfvvkyikrlvpkyhl 180
Cdd:PRK07514 80 FLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV-ETLDAD----GTGSL----------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 181 PDAisfrsALQHGYRMQYVKPEivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLY 260
Cdd:PRK07514 138 LEA-----AAAAPDDFETVPRG--ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWR---FTPDDVLIHALPIF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 261 HIFAL--TMNCLLFIelGGQnlLITNPRDIPGLVkeLAKYP-FTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPV 337
Cdd:PRK07514 208 HTHGLfvATNVALLA--GAS--MIFLPKFDPDAV--LALMPrATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 338 qqvVAE---RWVKLTGQYLLEGYGLTECSPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDDDN-EVAPGEPGELCIKGPQ 413
Cdd:PRK07514 282 ---LAEthrEFQERTGHAILERYGMTETNMNTS-NPYDGERRAGTVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPN 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYWQRPDAT-DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGS 492
Cdd:PRK07514 358 VFKGYWRMPEKTaEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 493 SGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07514 438 FGEGVTAVVVpKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
21-552 |
2.76e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 258.82 E-value: 2.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 21 RYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:PRK07470 5 RVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 101 AVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVvdktqvkhviltrmgdqlSTAKGTLVNFVVKYIKRLVPKYhl 180
Cdd:PRK07470 84 WVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAV------------------RAASPDLTHVVAIGGARAGLDY-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 181 pDAISFRSAlqhGYRmqyVKPEIVA-DDLAFLQYTGGTTGVAKGAMLTHRNM-------LANLeqVNATygplLHRGKEL 252
Cdd:PRK07470 144 -EALVARHL---GAR---VANAAVDhDDPCWFFFTSGTTGRPKAAVLTHGQMafvitnhLADL--MPGT----TEQDASL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 253 VVTalPLYH---IFALTMncllfIELGGQNLLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLH 328
Cdd:PRK07470 211 VVA--PLSHgagIHQLCQ-----VARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 329 LSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNP---HDID----YHSGSIGLPVPSTEAKLVDDDDNEVAP 401
Cdd:PRK07470 284 YVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPpalHDAEdgpdARIGTCGFERTGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 GEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQ 481
Cdd:PRK07470 364 GETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVS 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 482 EVAAVGVPSGSSGE-AVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07470 444 EVAVLGVPDPVWGEvGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-550 |
6.94e-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: 6.94e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 48 VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVI 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 128 VSNFAHTlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvKPEIVADD 207
Cdd:cd05903 80 PERFRQF-----------------------------------------------------------------DPAAMPDA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLL--ITNP 285
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG---LGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdIWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 286 RDIPGLVKElakYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEC-SP 364
Cdd:cd05903 172 DKALALMRE---HGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECpGA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 365 LVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDD 444
Cdd:cd05903 249 VTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEEALITFCRRH-LT 522
Cdd:cd05903 329 DGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAlLTFDELVAYLDRQgVA 408
|
490 500
....*....|....*....|....*...
gi 505808171 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-551 |
5.46e-78 |
|
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: 254.86 E-value: 5.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDK-TQVKHVILTRMGDqlstakgtlvnfvvkyiKRLVPkyHLPDAISFrSALQHGYRMQYVKPEIVADDL 208
Cdd:cd12119 106 DFLPLLEAIAPRlPTVEHVVVMTDDA-----------------AMPEP--AGVGVLAY-EELLAAESPEYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGkELVVTALPLYHI------FALTMNcllfielgGQNLLI 282
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPVVPMFHVnawglpYAAAMV--------GAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 TNPRDIPG-LVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTE 361
Cdd:cd12119 237 PGPYLDPAsLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 362 CSPLVSVNpHDIDYHSG-----------SIGLPVPSTEAKLVDDDDNEVA--PGEPGELCIKGPQVMLGYWQRPDATDEI 428
Cdd:cd12119 316 TSPLGTVA-RPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGE-AVKIFVVKKDAA 507
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErPLAVVVLKEGAT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 505808171 508 LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd12119 475 VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-552 |
6.33e-78 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 253.73 E-value: 6.33e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQ-YPV--ALFGIlraGMIAVNVNPLYTPRELE 114
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEmILVihALQQL---GAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 115 HQLNDSGAAAIVIVSNFAHtlekvvdktqvKHVILTRmgdqlstakgtlvnfvVKYikrlvpkyhlpdaisfrSALQHGy 194
Cdd:PRK03640 93 WQLDDAEVKCLITDDDFEA-----------KLIPGIS----------------VKF-----------------AELMNG- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 195 rmQYVKPEIVA----DDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqvnATYGPLLHRG---KELVVTALPLYHI--FAL 265
Cdd:PRK03640 128 --PKEEAEIQEefdlDEVATIMYTSGTTGKPKGVIQTYGNHWW------SAVGSALNLGlteDDCWLAAVPIFHIsgLSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 266 TMNCLLFielgGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLnnKEFQQLDFSSlHLSA---GGGmPVQQVVA 342
Cdd:PRK03640 200 LMRSVIY----GMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLL--ERLGEGTYPS-SFRCmllGGG-PAPKPLL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERwVKLTGQYLLEGYGLTE-CSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDdNEVAPGEPGELCIKGPQVMLGYWQR 421
Cdd:PRK03640 272 EQ-CKEKGIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 422 PDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGeAVKIFV 501
Cdd:PRK03640 350 EDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG-QVPVAF 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 505808171 502 VKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK03640 429 VVKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
8-555 |
1.41e-76 |
|
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: 251.60 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 8 RYPADVPAeinpdRY--------QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVAL 79
Cdd:COG1021 7 PWPEEFAA-----RYreagywrgETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 80 MMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS--------NFAHTLEKVVDktQVKHVILTr 151
Cdd:COG1021 81 QLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVP--SLRHVLVV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 152 mGDQlstakgtlvnfvvkyikrlvpkyhlPDAISFRSALQHGyrMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNM 231
Cdd:COG1021 158 -GDA-------------------------GEFTSLDALLAAP--ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 232 LANLEQVNATYGpLLHRGKELVvtALPLYHIFALTMNCLL-FIELGGQNLLITNPRdiPGLVKEL-AKYPFTAMTGVNTL 309
Cdd:COG1021 210 LYSVRASAEICG-LDADTVYLA--ALPAAHNFPLSSPGVLgVLYAGGTVVLAPDPS--PDTAFPLiERERVTVTALVPPL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 310 FNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEcsPLVSVN----PHDIDYHSgsIGLPV- 384
Cdd:COG1021 285 ALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTrlddPEEVILTT--QGRPIs 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 385 PSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDAT----DEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILV 460
Cdd:COG1021 361 PDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNarafTP---DGFYRTGDLVRRTPDGYLVVEGRAKDQINR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 461 SGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFCR-RHLTGYKVPKLVEFRDELPKS 539
Cdd:COG1021 438 GGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLReRGLAAFKLPDRLEFVDALPLT 517
|
570
....*....|....*.
gi 505808171 540 NVGKILRRELRDEARA 555
Cdd:COG1021 518 AVGKIDKKALRAALAA 533
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-487 |
1.49e-76 |
|
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: 249.43 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLY---TPRELEHQLNDSGAAAI 125
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 vIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivA 205
Cdd:cd05907 82 -FVED--------------------------------------------------------------------------P 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHrgkELVVTALPLYHIFALTMNCLLFIELGGQnllITNP 285
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEG---DRHLSFLPLAHVFERRAGLYVPLLAGAR---IYFA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 286 RDIPGLVKELAKYPFTAMTGVNTLFNALLNN-----------KEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLL 354
Cdd:cd05907 161 SSAETLLDDLSEVRPTVFLAVPRVWEKVYAAikvkavpglkrKLFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDddnevapgepGELCIKGPQVMLGYWQRPDATDE-IIKDGW 433
Cdd:cd05907 240 EGYGLTETSAVVTLNPPG-DNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEaLDADGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 434 LHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-550 |
2.08e-76 |
|
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: 248.55 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 39 QPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEhqln 118
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 119 dsgaaaivivsnfahtleKVVDKTQVKHVILTrmgDQLSTAkgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqy 198
Cdd:cd05958 77 ------------------YILDKARITVALCA---HALTAS--------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 199 vkpeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYGP--LLHRGKELVVTALPLYHIFALTMNCLLFIELG 276
Cdd:cd05958 97 -------DDICILAFTSGTTGAPKATMHFHRDPLASAD----RYAVnvLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLI--TNPRDIPGLVkelAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHL--SAGGGMPVQqvVAERWVKLTGQY 352
Cdd:cd05958 166 ASGVLLeeATPDLLLSAI---ARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKcvSAGEALPAA--LHRAWKEATGIP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 353 LLEGYGLTECSPL-VSVNPHDIdyHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQvmlGYWQRPDATDE-IIK 430
Cdd:cd05958 241 IIDGIGSTEMFHIfISARPGDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRtYVQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKK-----D 505
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 505808171 506 AALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05958 396 PVLARE-LQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-552 |
2.09e-76 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 251.59 E-value: 2.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAFI-NMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIvivsnFAHTLEKvvdKTQVKHVILTrMGDQLSTAKGTLVnfvvkyIKRLVPKYhlpD 182
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMF-----FAPTLFK---QTRPVDLILP-LQNQLPQLQQIVG------VDKLAPAT---S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 AISFRSALQHGYRMQYvKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygplLHRGK-ELVVTALPLYH 261
Cdd:PRK06087 165 SLSLSQIIADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR----LNLTWqDVFMMPAPLGH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 262 IFALTMNCLLFIELGGQNLL--ITNPRDIPGLvkeLAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQ 339
Cdd:PRK06087 240 ATGFLHGVTAPFLIGARSVLldIFTPDACLAL---LEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 340 VVAERwVKLTGQYLLEGYGLTECSPLVSVNPHD-IDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGY 418
Cdd:PRK06087 317 KVARE-CQQRGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 419 WQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAV 497
Cdd:PRK06087 396 LDEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERS 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 498 KIFVVKKDAALT---EEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06087 476 CAYVVLKAPHHSltlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
31-555 |
1.35e-74 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 246.61 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFINMGEVMTYRKLEERSRAFAAYL-QQGLGLqkGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYT 109
Cdd:PRK07786 26 HALMQ-PDAPALRFLGNTTTWRELDDRVAALAGALsRRGVGF--GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 110 PRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTrMGDqlSTAKGTLvnfvvkyikrlvpkyHLPDAISfrsa 189
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVV-AGG--SSDDSVL---------------GYEDLLA---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 190 lQHGYRMQYVkpEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHRGKELVVTALPLYHIFALTmNC 269
Cdd:PRK07786 161 -EAGPAHAPV--DIPNDSPALIMYTSGTTGRPKGAVLTHANLTG--QAMTCLRTNGADINSDVGFVGVPLFHIAGIG-SM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 270 LLFIELGGQNLLI-TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKL 348
Cdd:PRK07786 235 LPGLLLGAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 349 TGQYLLEGYGLTECSPLVSV-NPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDE 427
Cdd:PRK07786 315 PEAQILAAFGQTEMSPVTCMlLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 428 IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEA-VKIFVVKKDA 506
Cdd:PRK07786 395 AFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVpVAVAAVRNDD 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 505808171 507 A-LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
Cdd:PRK07786 475 AaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-551 |
2.19e-74 |
|
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: 242.25 E-value: 2.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSgaaaivivs 129
Cdd:cd05912 3 TFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 nfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpEIVADDLA 209
Cdd:cd05912 73 ------------------------------------------------------------------------DVKLDDIA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHRgKELVVTALPLYHIFALT--MNCLLFielgGQNLLITNPRD 287
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG--LTE-DDNWLCALPLFHISGLSilMRSVIY----GMTVYLVDKFD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 288 IPGLVKELAKYPFTAMTGVNTLFNALLnnKEFQQLDFSSLHLSAGGGMPVQQVVAERwVKLTGQYLLEGYGLTE-CSPLV 366
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTEtCSQIV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 367 SVNPHDIDYHSGSIGLPVPSTEAKLVDDDdneVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEG 446
Cdd:cd05912 231 TLSPEDALNKIGSAGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVkKDAALTEEALITFCRRHLTGYKV 526
Cdd:cd05912 308 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-SERPISEEELIAYCSEKLAKYKV 386
|
490 500
....*....|....*....|....*
gi 505808171 527 PKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05912 387 PKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
14-551 |
6.16e-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: 244.74 E-value: 6.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 14 PAEINPDRYQSLVELFEHATTRYADQP---AFIN--MGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYP 88
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKRYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 89 VALFGILRAGMIAVNVNPLYTPRELEHQLNDSgAAAIVIVSNfaHTLEKVVD-KTQVKHVILTRMGDQLSTAKG--TLVN 165
Cdd:cd17642 84 LPVIAGLFIGVGVAPTNDIYNERELDHSLNIS-KPTIVFCSK--KGLQKVLNvQKKLKIIKTIIILDSKEDYKGyqCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 166 FVvkyikrlvpKYHLPDaisfrsalqhGYRMQYVKPEIV--ADDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QVNATY 242
Cdd:cd17642 161 FI---------TQNLPP----------GFNEYDFKPPSFdrDEQVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 243 GPLLHRGKElVVTALPLYHIFAltMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQL 322
Cdd:cd17642 222 GNQIIPDTA-ILTVIPFHHGFG--MFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 323 DFSSLHLSAGGGMP----VQQVVAERwVKLTGqyLLEGYGLTECSPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDDDNE 398
Cdd:cd17642 299 DLSNLHEIASGGAPlskeVGEAVAKR-FKLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDLDTGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 399 -VAPGEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:cd17642 375 tLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 477 HSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEEALITFCRRHLTGYKvpKL---VEFRDELPKSNVGKILRRELRD 551
Cdd:cd17642 455 HPKIFDAGVAGIPDEDAGELPAAVVVLEAGKtMTEKEVMDYVASQVSTAK--RLrggVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
213-546 |
1.39e-73 |
|
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: 237.55 E-value: 1.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 213 YTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKELVVtaLPLYHIFALTMNcLLFIELGGQNLLITNpRDIPGLV 292
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG-LTEADVYLNM--LPLFHIAGLNLA-LATFHAGGANVVMEK-FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 293 KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVqqvVAERWVKLTGQYLLEGYGLTECSPLVSVnpHD 372
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAPE---TIQRFEETTGATFWSLYGQTETSGLVTL--SP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 373 IDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVD 452
Cdd:cd17637 157 YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 453 RK--KDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK-IFVVKKDAALTEEALITFCRRHLTGYKVPKL 529
Cdd:cd17637 237 RKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKKPRY 316
|
330
....*....|....*..
gi 505808171 530 VEFRDELPKSNVGKILR 546
Cdd:cd17637 317 VVFVEALPKTADGSIDR 333
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
4-560 |
1.40e-72 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 242.05 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 4 VWLNRYPadvPAEINPDRYQSLVE-LFEHAttRYADQPAFIN--MGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALM 80
Cdd:PLN02574 24 IYSSKHP---PVPLPSDPNLDAVSfIFSHH--NHNGDTALIDssTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAaivivsnFAHTLEKVVDKtqvkhviLTRMGdqlstak 160
Cdd:PLN02574 99 LPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVG-------LAFTSPENVEK-------LSPLG------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 gtlvnfvvkyikrlVPKYHLPDAISFRSALQHGYRMQY---------VKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNM 231
Cdd:PLN02574 158 --------------VPVIGVPENYDFDSKRIEFPKFYElikedfdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 232 LANLEQ-VNATYGPLLHRGKELV-VTALPLYHIFALTMNCLLFIELGgQNLLITNPRDIPGLVKELAKYPFTAMTGVNTL 309
Cdd:PLN02574 224 IAMVELfVRFEASQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLG-STIVVMRRFDASDMVKVIDRFKVTHFPVVPPI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 310 FNALLNN-KEFQQLDFSSLHLSAGGGMPVQQVVAERWVK-LTGQYLLEGYGLTECSPLVS--VNPHDIDYHSgSIGLPVP 385
Cdd:PLN02574 303 LMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQtLPHVDFIQGYGMTESTAVGTrgFNTEKLSKYS-SVGLLAP 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 386 STEAKLVD-DDDNEVAPGEPGELCIKGPQVMLGYWQRPDATD-EIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGF 463
Cdd:PLN02574 382 NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQsTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 464 NVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKK-DAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVG 542
Cdd:PLN02574 462 QIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRqGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAG 541
|
570
....*....|....*...
gi 505808171 543 KILRRELRDEARAKVDNK 560
Cdd:PLN02574 542 KILRRELKRSLTNSVSSR 559
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-552 |
1.43e-72 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 241.42 E-value: 1.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 4 VWLNRYPAdVPAeinPDRYqSLVELFEHATTRYADQPAFIN--MGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMM 81
Cdd:PLN02330 14 IFRSRYPS-VPV---PDKL-TLPDFVLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 82 PNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAaiVIVSNFAHtLEKVvdktqvkhviltrmgdqlstaKG 161
Cdd:PLN02330 88 PNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAK--LIVTNDTN-YGKV---------------------KG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 162 TLVNFVVkyikrlVPKYHLPDAISFRSALQHGYRM--QYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN 239
Cdd:PLN02330 144 LGLPVIV------LGEEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 240 ATYGPLLhRGKELVVTALPLYHIFALTMNCLLFIELGGQnLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF 319
Cdd:PLN02330 218 FSVGPEM-IGQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 320 QQLDFSSLHLSA--GGGMPVQ-QVVAERWVKLTGQYLLEGYGLTE--CSPLVSVNP---HDIDyHSGSIGLPVPSTEAKL 391
Cdd:PLN02330 296 EEFDLSKLKLQAimTAAAPLApELLTAFEAKFPGVQVQEAYGLTEhsCITLTHGDPekgHGIA-KKNSVGFILPNLEVKF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 392 VDDDDNEVAP-GEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PLN02330 375 IDPDTGRSLPkNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 470 IEDVVMQHSGVQEVAAVGVPSGSSGE-AVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:PLN02330 455 LEAILLTHPSVEDAAVVPLPDEEAGEiPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRL 534
|
....
gi 505808171 549 LRDE 552
Cdd:PLN02330 535 LKEK 538
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-550 |
6.32e-72 |
|
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: 237.34 E-value: 6.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 60 AFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAG----MIAVNVNPLYTPRELEHQLNDSGAAaIVIVSnfahtl 135
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGR-IVLAD------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 136 EKVVDKTQVKHVILTRMGDQLSTakgtlvnfvvkyikrlvpkyhlpDAISFRSALQHGYrmqyvkpEIVADDLAFLQYTG 215
Cdd:cd05922 77 AGAADRLRDALPASPDPGTVLDA-----------------------DGIRAARASAPAH-------EVSHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 216 GTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFALtmNCLLFIELGGQNLLITNPRDIP-GLVKE 294
Cdd:cd05922 127 GSTGSPKLVRLSHQNLLANARSIAEYLG---ITADDRALTVLPLSYDYGL--SVLNTHLLRGATLVLTNDGVLDdAFWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 295 LAKYPFTAMTGVNTLFnALLNNKEFQQLDFSSLHL--SAGGGMPvQQVVAERWVKLTGQYLLEGYGLTECSPLVS-VNPH 371
Cdd:cd05922 202 LREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYltQAGGRLP-QETIARLRELLPGAQVYVMYGQTEATRRMTyLPPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 372 DIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDA-TDEIIKDGWLHTGDIAVMDDEGFLRI 450
Cdd:cd05922 280 RILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLFI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 451 VDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSgSSGEAVKIFVVKKDaALTEEALITFCRRHLTGYKVPKLV 530
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPD-KIDPKDVLRSLAERLPPYKVPATV 437
|
490 500
....*....|....*....|
gi 505808171 531 EFRDELPKSNVGKILRRELR 550
Cdd:cd05922 438 RVVDELPLTASGKVDYAALR 457
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-556 |
8.00e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 238.26 E-value: 8.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNFAHTLEKVVDKTQvKHVILTRMGDQLSTAKGTLVNFVVKYikrlvPKYHLPDaisfRSAlqhGYRMQYvkpeiva 205
Cdd:PRK08276 88 IVSAALADTAAELAAELP-AGVPLLLVVAGPVPGFRSYEEALAAQ-----PDTPIAD----ETA---GADMLY------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 ddlaflqyTGGTTGVAKGAM--LTHRNMLANLEQVNATYGPLLHRGKELV--VTAlPLYHIfALTMNCLLFIELGGqnLL 281
Cdd:PRK08276 148 --------SSGTTGRPKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVylSPA-PLYHT-APLRFGMSALALGG--TV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 282 ITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF--QQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYG 358
Cdd:PRK08276 216 VVMEKfDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 359 LTECSPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEI-IKDGWLHTG 437
Cdd:PRK08276 296 SSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAArNPHGWVTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 438 DIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-----VKKDAALTEEa 512
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadgADAGDALAAE- 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 505808171 513 LITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK08276 454 LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEG 497
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-546 |
1.23e-71 |
|
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: 232.39 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnLEQVNATYGPLLHRGKELVVTalPLYHIFALTMNCLLFIeLGGQNLLITNPR 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR-AAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACL-LTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW-VKLTGQYLLEGYGLTECSPL 365
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 366 VSVNPHD-IDYHSGSIGLPVPSTEAKLVDDddnevapgepGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMD 443
Cdd:cd17638 157 TMCRPGDdAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDA-ALTEEALITFCRRHLT 522
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 505808171 523 GYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-551 |
1.30e-71 |
|
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: 235.79 E-value: 1.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIV 126
Cdd:cd05971 5 EKVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 127 IvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpDAisfrsalqhgyrmqyvkpeivAD 206
Cdd:cd05971 84 T------------------------------------------------------DG---------------------SD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKELVVTALPLYHIFALtMNCLLFIELGGQNLLITNPR 286
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFN-LFPRDGDLYWTPADWAWIGGL-LDVLLPSLYFGVPVLAHRMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 --DIPGLVKELAKYpftamtGVNTLF---NAL-LNNKEFQQLDFSSLHLSA---GGGMPVQQVVAerWVKLT-GQYLLEG 356
Cdd:cd05971 167 kfDPKAALDLMSRY------GVTTAFlppTALkMMRQQGEQLKHAQVKLRAiatGGESLGEELLG--WAREQfGVEVNEF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 357 YGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQ--VMLGYWQRPDATDEIIKDGWL 434
Cdd:cd05971 239 YGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 435 HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALI 514
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 505808171 515 ----TFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05971 399 reiqELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
23-550 |
4.15e-71 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 236.89 E-value: 4.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFI---NMGEV--MTYRKL-EERSRAfaAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIfesSGGVVrrYSYLELnEEINRT--ANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 97 AGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKV--VDKTQVKHVILTRMGDqlstakgtlvnfvvkyikrl 174
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIqqEDATPLRHICLTRVAL-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 vPKyhLPDAISFRSAL-QHGYRMQYVKPeIVADDLAFLQYTGGTTGVAKGAMLTHRNML-ANLeqVNATYGPLlhRGKEL 252
Cdd:PRK08008 145 -PA--DDGVSSFTQLKaQQPATLCYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYNLRfAGY--YSAWQCAL--RDDDV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 253 VVTALPLYHI-FALTMNCLLFiELGGQNLLI-----------------TNPRDIPGLVKELAKYPFTAMTGVNTLFNAL- 313
Cdd:PRK08008 217 YLTVMPAFHIdCQCTAAMAAF-SAGATFVLLekysarafwgqvckyraTITECIPMMIRTLMVQPPSANDRQHCLREVMf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 314 -LNNKEFQQLDFSslhlsagggmpvqqvvaERWvkltGQYLLEGYGLTECspLVSV---NPHDiDYHSGSIGLPVPSTEA 389
Cdd:PRK08008 296 yLNLSDQEKDAFE-----------------ERF----GVRLLTSYGMTET--IVGIigdRPGD-KRRWPSIGRPGFCYEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 390 KLVDDDDNEVAPGEPGELCIKG---PQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNV 465
Cdd:PRK08008 352 EIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 466 YPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
|
....*.
gi 505808171 545 LRRELR 550
Cdd:PRK08008 512 IKKNLK 517
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-553 |
6.25e-71 |
|
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: 235.69 E-value: 6.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQGLglQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNFahtLEK------VVDKTQVKHVILTRMGDQLSTAKGTLVnfvvkYIkrlvpkyhlpdAISFRSALQhgYRMQYV 199
Cdd:cd05909 83 LTSKQF---IEKlklhhlFDVEYDARIVYLEDLRAKISKADKCKA-----FL-----------AGKFPPKWL--LRIFGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 200 KPEiVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFALTMNCLLFIELGGQN 279
Cdd:cd05909 142 APV-QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 280 LLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKefQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGL 359
Cdd:cd05909 218 VFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 360 TECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVD-DDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGD 438
Cdd:cd05909 296 TECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 439 IAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQ-EVAAVGVPSGSSGEAVKIFVVKKDAalTEEALITFC 517
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTDT--DPSSLNDIL 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 505808171 518 RRH-LTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05909 454 KNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
38-551 |
1.80e-70 |
|
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: 234.73 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:TIGR02262 20 GKTAFIDDISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYML 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIVSNFAHTLEKVVDKT-QVKHVILTrmGDQLSTAKgTLVNFVVKyikrlvpkyhlpDAISFRSALQHgyrm 196
Cdd:TIGR02262 99 EDSRARVVFVSGALLPVIKAALGKSpHLEHRVVV--GRPEAGEV-QLAELLAT------------ESEQFKPAATQ---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 197 qyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLH-RGKELVVTALPLYHIFALTmNCLLFIE 274
Cdd:TIGR02262 160 --------ADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAE----LYArNTLGiREDDVCFSAAKLFFAYGLG-NALTFPM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 275 LGGQNLLITNPRDIPGLV-KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYL 353
Cdd:TIGR02262 227 SVGATTVLMGERPTPDAVfDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 354 LEGYGLTECSPLVSVN-PHDIDYhsGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDG 432
Cdd:TIGR02262 307 VDGIGSTEMLHIFLSNlPGDVRY--GTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEE 511
Cdd:TIGR02262 385 WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVlRPGQTALET 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505808171 512 ALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:TIGR02262 465 ELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
30-551 |
3.33e-69 |
|
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: 231.03 E-value: 3.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 30 EHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYT 109
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALA-ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 110 PRELEHQLNDSGAAAIVIVSNFAHtlEKVVDktqvkhviltrMGDqlstakgtlvnfvvkyikrlvpkyhlPDAisfrsa 189
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEY--EDLLA-----------EGD--------------------------PDF------ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 190 lqhgyrmqyvKPEIVAD--DLAFLQYTGGTTGVAKGAMLTHRNMLanleqVNATYGPLLHRGKELVV--TALPLYH---- 261
Cdd:cd12118 125 ----------EWIPPADewDPIALNYTSGTTGRPKGVVYHHRGAY-----LNALANILEWEMKQHPVylWTLPMFHcngw 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 262 --IFALTMncllfieLGGQNLLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFS-SLHLSAGGGMPVQ 338
Cdd:cd12118 190 cfPWTVAA-------VGGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 339 QVVAErwVKLTGQYLLEGYGLTECSPLVSVNPhdidYHSGSIGLPvPSTEAKL----------------VDDDDNEVAP- 401
Cdd:cd12118 262 AVLAK--MEELGFDVTHVYGLTETYGPATVCA----WKPEWDELP-TEERARLkarqgvryvgleevdvLDPETMKPVPr 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 -GEP-GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSG 479
Cdd:cd12118 335 dGKTiGEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPA 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505808171 480 VQEVAAVGVPSGSSGEAVKIFV-VKKDAALTEEALITFCRRHLTGYKVPKLVEFRdELPKSNVGKILRRELRD 551
Cdd:cd12118 415 VLEAAVVARPDEKWGEVPCAFVeLKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
47-551 |
4.68e-69 |
|
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: 232.13 E-value: 4.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFAAYLQQGLGlqKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPRELEHQ------LNDS 120
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPPPTPGRHAerlaaiLADA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 121 GAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLVnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyVK 200
Cdd:cd05931 98 GPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADW----------------------------------PP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 201 PEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFALTMNCLLFIELGGQNL 280
Cdd:cd05931 144 PSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG---LDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 281 LITnPRDI---PGL-VKELAKYPFTAMTGVNtlFnAL------LNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTG 350
Cdd:cd05931 221 LMS-PAAFlrrPLRwLRLISRYRATISAAPN--F-AYdlcvrrVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 351 QY------LLEGYGLTECSPLVSVNPH---------------------DIDYHSG----SIGLPVPSTEAKLVDDDDN-E 398
Cdd:cd05931 297 PFgfrpeaFRPSYGLAEATLFVSGGPPgtgpvvlrvdrdalagravavAADDPAArelvSCGRPLPDQEVRIVDPETGrE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 399 VAPGEPGELCIKGPQVMLGYWQRPDATDEIIK-------DGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIE 471
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 472 DVVMQHSGVQE---VAAVGVPSGSSGEAVKIFVVKKDAALTEEALI------TFCRRH-LTGYKVpKLVEfRDELPKSNV 541
Cdd:cd05931 456 ATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIaaairaAVAREHgVAPADV-VLVR-PGSIPRTSS 533
|
570
....*....|
gi 505808171 542 GKILRRELRD 551
Cdd:cd05931 534 GKIQRRACRA 543
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
38-551 |
1.85e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 228.92 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINM--GEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:PRK09088 10 QRLAAVDLalGRRWTYAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 116 QLNDSGAAAIVivsnfahtlekvvdktqvkhviltrmGDQLSTAKGTLVNFVVKYIKRLvpKYHLPDAisfrsalqhgyr 195
Cdd:PRK09088 89 LLQDAEPRLLL--------------------------GDDAVAAGRTDVEDLAAFIASA--DALEPAD------------ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 196 mqyvKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNmlanLEQVNATYGPLLHRGKELV-VTALPLYHIFALTMNCLLFIE 274
Cdd:PRK09088 129 ----TPSIPPERVSLILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSfLCDAPMFHIIGLITSVRPVLA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 275 LGGqNLLITNPRDIPGLVKELAKyPFTAMT---GVNTLFNALLNNKEFqqlDFSSL-HLSA--GGGMPVQQVVAERWVKl 348
Cdd:PRK09088 201 VGG-SILVSNGFEPKRTLGRLGD-PALGIThyfCVPQMAQAFRAQPGF---DAAALrHLTAlfTGGAPHAAEDILGWLD- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 349 TGQYLLEGYGLTECSPL--VSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATD 426
Cdd:PRK09088 275 DGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 427 EII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD 505
Cdd:PRK09088 355 RAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 505808171 506 AALTEEALI-TFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK09088 435 GAPLDLERIrSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
31-551 |
2.66e-67 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 226.50 E-value: 2.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFI--NMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:PRK13391 6 HAQTT-PDKPAVImaSTGEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 109 TPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDktQVKHVILTRMGDqlstAKGTLVNFVvkyikrlvpkyHLPDAISfrs 188
Cdd:PRK13391 84 TPAEAAYIVDDSGARALITSAAKLDVARALLK--QCPGVRHRLVLD----GDGELEGFV-----------GYAEAVA--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 189 alqhGYRMQYVKPEIVADDLaflQYTGGTTGVAKGAmlthRNMLANLEQVNATygPLLHRGKELV--------VTALPLY 260
Cdd:PRK13391 144 ----GLPATPIADESLGTDM---LYSSGTTGRPKGI----KRPLPEQPPDTPL--PLTAFLQRLWgfrsdmvyLSPAPLY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 261 HIfALTMNCLLFIELGGQNLLITN--PRDIPGLVKelaKYPFTAMTGVNTLFNALLNNKEFQQL--DFSSLHLSAGGGMP 336
Cdd:PRK13391 211 HS-APQRAVMLVIRLGGTVIVMEHfdAEQYLALIE---EYGVTHTQLVPTMFSRMLKLPEEVRDkyDLSSLEVAIHAAAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 337 VQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDDDNEVAPGEPGELCIKGPQvML 416
Cdd:PRK13391 287 CPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGR-PF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 417 GYWQRPDATDEIIKD--GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSG 494
Cdd:PRK13391 365 EYLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 495 EAVKIFV-----VKKDAALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK13391 445 EEVKAVVqpvdgVDPGPALAAE-LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
25-550 |
9.54e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 224.10 E-value: 9.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 25 LVELFEHATTRYADQPAFINMGE-VMTYRKLEERSRAFAAylqqglGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK07787 1 LASLNPAAVAAAADIADAVRIGGrVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 104 VNPLYTPRELEHQLNDSGAAAIvivsnfahtlekvvdktqvkhviLTRMGDQLSTakgtlvnfvvkyikrlVPkyHLPDA 183
Cdd:PRK07787 75 VPPDSGVAERRHILADSGAQAW-----------------------LGPAPDDPAG----------------LP--HVPVR 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 184 ISFRSALQHgyrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIF 263
Cdd:PRK07787 114 LHARSWHRY--------PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ---WTADDVLVHGLPLFHVH 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 264 ALTMNCLLFIELGGQnlLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLdFSSLHLSAGGGMPVQQVVAE 343
Cdd:PRK07787 183 GLVLGVLGPLRIGNR--FVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWVKLTGQYLLEGYGLTECSPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDDDNEVAP-GEP-GELCIKGPQVMLGYWQR 421
Cdd:PRK07787 260 RLAALTGHRPVERYGMTETLITLSTRA-DGERRPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 422 PDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKI 499
Cdd:PRK07787 339 PDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 505808171 500 FVVKKDAAlTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07787 419 YVVGADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-553 |
1.31e-66 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 220.43 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLE--QVNATYGPllhrgKELVVTALPLYHIFALTMNCLLFIELGGQnLLIT 283
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWmlALNSLFDP-----DDVLLCGLPLFHVNGSVVTLLTPLASGAH-VVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 284 NP---RDiPGLVKEL----AKYPFTAMTGVNTLFNALLNNKEfqQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEG 356
Cdd:cd05944 76 GPagyRN-PGLFDNFwklvERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 357 YGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDN-----EVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKD 431
Cdd:cd05944 153 YGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVgrllrDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFVAD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 432 GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAALTE 510
Cdd:cd05944 233 GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 505808171 511 EALITFCRRHLTGY-KVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05944 313 EELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
23-552 |
4.48e-66 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 224.25 E-value: 4.48e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDK-TQVKHVILTRMGDQLSTAKGtlvnfvVKYIKrLVPKYHLP 181
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWLLDAPASVSVPAG------WSTAP-LPPLDAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 182 DAISfrsalqhgyrmqyVKPeivADDLAFLqYTGGTTGVAKGAMLTH-------RNMLANLEqvnatygplLHRGkELVV 254
Cdd:PRK06155 173 PAAA-------------VQP---GDTAAIL-YTSGTTGPSKGVCCPHaqfywwgRNSAEDLE---------IGAD-DVLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 255 TALPLYHIFALTMncllFIE--LGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:PRK06155 226 TTLPLFHTNALNA----FFQalLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 333 GGMPVQQVVA--ERwvklTGQYLLEGYGLTECSPLVSVnPHDIDyHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIK 410
Cdd:PRK06155 302 PGVPAALHAAfrER----FGVDLLDGYGSTETNFVIAV-THGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 411 GPQ---VMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:PRK06155 376 ADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 488 VPSGSSGEAVKIFVVKKDA-ALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDGtALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
35-552 |
2.19e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 221.30 E-value: 2.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 35 RYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELE 114
Cdd:PRK06145 14 RTPDRAALVYRDQEISYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 115 HQLNDSGAAAIVIVSNFAhtlekvVDKTQVKHVILTRMGDQLSTakgtlvnfvvkyikRLVPKYHLPDAISFRSAlqhgy 194
Cdd:PRK06145 93 YILGDAGAKLLLVDEEFD------AIVALETPKIVIDAAAQADS--------------RRLAQGGLEIPPQAAVA----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 195 rmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNM-LANLEQVNATygPLLHRGKELVVTalPLYHIFALTMNCLLFI 273
Cdd:PRK06145 148 ----------PTDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIAL--GLTASERLLVVG--PLYHVGAFDLPGIAVL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 274 ELGGQnLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MPVQQVVAERWVKLTGQ 351
Cdd:PRK06145 214 WVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGekTPESRIRDFTRVFTRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 352 YLlEGYGLTE-CSPLVSVNP-HDIDyHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEII 429
Cdd:PRK06145 293 YI-DAYGLTEtCSGDTLMEAgREIE-KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 430 KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGE-AVKIFVVKKDAAL 508
Cdd:PRK06145 371 YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGErITAVVVLNPGATL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 505808171 509 TEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06145 451 TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-549 |
2.23e-65 |
|
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: 219.71 E-value: 2.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 37 ADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYtPRE-LEH 115
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 116 QLNDSGAaaivivsnfahtlekvvdktqvkHVILTRmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyr 195
Cdd:cd05930 79 ILEDSGA-----------------------KLVLTD-------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 196 mqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHRGKELVVTALP----LYHIFALTMN--C 269
Cdd:cd05930 92 ---------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY-PLTPGDRVLQFTSFSfdvsVWEIFGALLAgaT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 270 LLFIELGGQnllitnpRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQqlDFSSLHLSAGGGMPVQQVVAERWVKL- 348
Cdd:cd05930 162 LVVLPEEVR-------KDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELl 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 349 TGQYLLEGYGLTECSPLVS---VNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDAT 425
Cdd:cd05930 233 PGARLVNLYGPTEATVDATyyrVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 426 DE-IIKD-----GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK 498
Cdd:cd05930 313 AErFVPNpfgpgERMYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 505808171 499 IFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05930 393 AYVVpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-551 |
5.79e-65 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 220.34 E-value: 5.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 48 VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVI 127
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 128 VSNFAHTLEKVVDKT-QVKHViltrmgdqlSTAKGTLVNFVVKYIKRLVPkyhlPDAISFRSALQHGyrMQYVKPEIVAD 206
Cdd:PRK12406 90 HADLLHGLASALPAGvTVLSV---------PTPPEIAAAYRISPALLTPP----AGAIDWEGWLAQQ--EPYDGPPVPQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 dlAFLQYTGGTTGVAKGamlTHRN-----MLANLEQVNAT-YGplLHRGKELVVTAlPLYH----IFALTMncllfIELG 276
Cdd:PRK12406 155 --QSMIYTSGTTGHPKG---VRRAaptpeQAAAAEQMRALiYG--LKPGIRALLTG-PLYHsapnAYGLRA-----GRLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GqnLLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSSL----HLSAGGGMPVQQVVAERWvklt 349
Cdd:PRK12406 222 G--VLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLrhviHAAAPCPADVKRAMIEWW---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 350 GQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVML-GYWQRPDATDEI 428
Cdd:PRK12406 296 GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAA 507
Cdd:PRK12406 376 DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVePQPGAT 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 505808171 508 LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK12406 456 LDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-551 |
1.01e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 220.57 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 20 DRYQSLVELFEHATTRYADQPAFIN-MGEvMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK07788 46 RRYGPFAGLVAHAARRAPDRAALIDeRGT-LTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 99 MIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKG--TLVNFVVKYIKRLVP 176
Cdd:PRK07788 124 ARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTdeTLDDLIAGSSTAPLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 177 KyhlpdaisfrsALQHGyrmqyvkpeivaddlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhRGKELVVTA 256
Cdd:PRK07788 204 K-----------PPKPG---------------GIVILTSGTTGTPKGAPRPEPSPLAPLAGL-LSRVPF--RAGETTLLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 257 LPLYHIFALtMNCLLFIELGgqNLLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSSLHLSAGG 333
Cdd:PRK07788 255 APMFHATGW-AHLTLAMALG--STVVLRRRfDPEATLEDIAKHKATALVVVPVMLSRILDlgPEVLAKYDTSSLKIIFVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQ 413
Cdd:PRK07788 332 GSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYwqrPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSS 493
Cdd:PRK07788 412 PFEGY---TDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 494 GEAVKIFVVKKD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK07788 489 GQRLRAFVVKAPgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-543 |
2.33e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 219.37 E-value: 2.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 28 LFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 108 YTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKT-QVKHVIltRMGDQLSTAkgtlvnfvvkyikrlvpkyHLPDAISF 186
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLpKLRTLV--VVEDGSGND-------------------LLPGAVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 RSAL--QHGYRmqyVKPEIVADDLAFLqYTGGTTGVAKGAMLTHRNM-LANLEQVNATYGPLLHRGKELVVTAL------ 257
Cdd:PRK07798 146 EDALaaGSPER---DFGERSPDDLYLL-YTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDEEELAKRAAagpgmr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 -----PLYHIFAL--TMNCLLFielGGQNLLITNPR-DIPGLVKELAKYPFTAMTGVNT-----LFNALLNNKEFqqlDF 324
Cdd:PRK07798 222 rfpapPLMHGAGQwaAFAALFS---GQTVVLLPDVRfDADEVWRTIEREKVNVITIVGDamarpLLDALEARGPY---DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 325 SSLHLSAGGGMPVQQVVAERWVKLTGQ-YLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPV-PSTeaKLVDDDDNEVAPG 402
Cdd:PRK07798 296 SSLFAIASGGALFSPSVKEALLELLPNvVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIgPRT--VVLDEDGNPVEPG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 403 --EPGELCIKGPqVMLGYWQRPDATDEIIK--DG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK07798 374 sgEIGWIARRGH-IPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 477 HSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:PRK07798 453 HPDVADALVVGVPDERWGQEVVAVVqLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
60-549 |
1.84e-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: 1.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 60 AFAAYlqqglGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGaaaivivsnfahtlekvv 139
Cdd:TIGR01923 15 ALKAQ-----GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 140 dktqvKHVILTrmgDQLSTAKGTlvnfvvkyikrlvpkyhlpDAISFRSALQHGYRMQYVKPEIVADDLAFLQYTGGTTG 219
Cdd:TIGR01923 72 -----VQLLLT---DSLLEEKDF-------------------QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 220 VAKGAMLTHRNMLANLEQVNATYGplLHRGKELVVtALPLYHIFALTMncLLFIELGGQNLLITNPRDipGLVKELAKYP 299
Cdd:TIGR01923 125 KPKAVPHTFRNHYASAVGSKENLG--FTEDDNWLL-SLPLYHISGLSI--LFRWLIEGATLRIVDKFN--QLLEMIANER 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 300 FTAMTGVNTLFNALLNnkefQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTE-CSPLVSVNPhDIDYHSG 378
Cdd:TIGR01923 198 VTHISLVPTQLNRLLD----EGGHNENLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTEtCSQVTTATP-EMLHARP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 379 SIGLPVPSTEAKLVDDDDNEVapgepGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMI 458
Cdd:TIGR01923 272 DVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 459 LVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGeAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPK 538
Cdd:TIGR01923 347 ISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWG-QVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPY 425
|
490
....*....|.
gi 505808171 539 SNVGKILRREL 549
Cdd:TIGR01923 426 NASGKILRNQL 436
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
39-553 |
2.37e-61 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 219.41 E-value: 2.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 39 QPAFIN-MGEVMTYRKLEERSRAFAAYLQQGLGLQKgdRVALMMPNLLQYPVALFGILRAGMIAVNVNplYTprelehql 117
Cdd:PRK08633 631 RLAVADsTGGELSYGKALTGALALARLLKRELKDEE--NVGILLPPSVAGALANLALLLAGKVPVNLN--YT-------- 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 ndSGAAAivivsnfahtLEKVVDKTQVKHVILTRMGDQLSTAKGTLVNFV----VKYIKRLVPKYHLPDAIS-FRSA--- 189
Cdd:PRK08633 699 --ASEAA----------LKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPenvkVIYLEDLKAKISKVDKLTaLLAArll 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 190 ----LQHGYRmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFAL 265
Cdd:PRK08633 767 parlLKRLYG-----PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNL---RNDDVILSSLPFFHSFGL 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 266 TMNCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW 345
Cdd:PRK08633 839 TVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAF 918
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 346 VKLTGQYLLEGYGLTECSPLVSVNPHDI---DYHS------GSIGLPVPSTEAKLVDDDD-NEVAPGEPGELCIKGPQVM 415
Cdd:PRK08633 919 EEKFGIRILEGYGATETSPVASVNLPDVlaaDFKRqtgskeGSVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVM 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 416 LGYWQRPDATDEIIKD----GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ--HSGVQEVAAVGVP 489
Cdd:PRK08633 999 KGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVP 1078
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 490 SGSSGEavKIFVVKKDAALTEEALitfcRRHLTGYKVPKLVEFR-----DELPKSNVGKILRRELRDEA 553
Cdd:PRK08633 1079 DEKKGE--KLVVLHTCGAEDVEEL----KRAIKESGLPNLWKPSryfkvEALPLLGSGKLDLKGLKELA 1141
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-549 |
6.48e-61 |
|
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: 209.29 E-value: 6.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINM--GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 101 AVNVNPLYTPRELEhQLNDSGAAAIVIVSNFAhtleKVVDKTQVKHVILTRMGDQLSTakGTLVNFvvkyikrlvpkyhl 180
Cdd:cd05923 80 PALINPRLKAAELA-ELIERGEMTAAVIAVDA----QVMDAIFQSGVRVLALSDLVGL--GEPESA-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 181 PDAISFRSAlqhgyrmqyvKPEivadDLAFLQYTGGTTGVAKGAMLTHRnmlANLEQV--NATYGPLLHRGKELVVTALP 258
Cdd:cd05923 139 GPLIEDPPR----------EPE----QPAFVFYTSGTTGLPKGAVIPQR---AAESRVlfMSTQAGLRHGRHNVVLGLMP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 LYHI---FALTMNCLLFielGGQNLLIT--NPRDIPGLVKELAkypFTAMTGVNTLFNALLNNKEFQQLDFSSL-HLS-A 331
Cdd:cd05923 202 LYHVigfFAVLVAALAL---DGTYVVVEefDPADALKLIEQER---VTSLFATPTHLDALAAAAEFAGLKLSSLrHVTfA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 332 GGGMPvqQVVAERWVKLTGQYLLEGYGLTEC-SPLVSVNPHdidyhSGSIGLPVPSTEAKLV---DDDDNEVAPGEPGEL 407
Cdd:cd05923 276 GATMP--DAVLERVNQHLPGEKVNIYGTTEAmNSLYMRDAR-----TGTEMRPGFFSEVRIVrigGSPDEALANGEEGEL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 408 CIK--GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAA 485
Cdd:cd05923 349 IVAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVV 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 486 VGVPSGSSGEAVKIFVVKKDAALTEEALITFCR-RHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05923 429 IGVADERWGQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-550 |
6.67e-61 |
|
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: 207.74 E-value: 6.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYT---PRELEHQLNDSGAAAIV 126
Cdd:cd05969 2 TFAQLKVLSARFANVLKS-LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 127 ivsnfahTLEKVVDKTQVKhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivad 206
Cdd:cd05969 78 -------TTEELYERTDPE------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHRGKELVVTALP------LYHIFALTMNcllfielGGQNL 280
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDLHPDDIYWCTADPgwvtgtVYGIWAPWLN-------GVTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 281 LITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF--QQLDFSSLHLSAGGGMPVQQVVAeRW-VKLTGQYLLEGY 357
Cdd:cd05969 161 VYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTW 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 358 GLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKG--PQVMLGYWQRPDATDEIIKDGWLH 435
Cdd:cd05969 240 WQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDA-----ALTE 510
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGfepsdELKE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505808171 511 EaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05969 400 E-IINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
25-555 |
8.23e-61 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 210.29 E-value: 8.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 25 LVELFEHATTRyADQPAFINM----GEV--MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK13295 27 NDDLDACVASC-PDKTAVTAVrlgtGAPrrFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 99 MIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVDK-TQVKHVILTRMGDQLSTAKgtlvnfvvkyiK 172
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPElPALRHVVVVGGDGADSFEA-----------L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 173 RLVPKYHL-PDAISFRSALQHGyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvNATYGPLLHRGKE 251
Cdd:PRK13295 174 LITPAWEQePDAPAILARLRPG-----------PDDVTQLIYTSGTTGEPKGVMHTANTLMAN----IVPYAERLGLGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 252 LVV-TALPLYHIFALTMNCLLFIELGGQNLL--ITNPRDIPGLVKE------LAKYPFTAmtgvntlfnALLNNKEFQQL 322
Cdd:PRK13295 239 DVIlMASPMAHQTGFMYGLMMPVMLGATAVLqdIWDPARAAELIRTegvtftMASTPFLT---------DLTRAVKESGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 323 DFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYH-SGSIGLPVPSTEAKLVDDDDNEVAP 401
Cdd:PRK13295 310 PVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERaSTTDGCPLPGVEVRVVDADGAPLPA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 GEPGELCIKGPQVMLGYWQRPD--ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSG 479
Cdd:PRK13295 390 GQIGRLQVRGCSNFGGYLKRPQlnGTDA---DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPA 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 480 VQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRH-LTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
Cdd:PRK13295 467 IAQVAIVAYPDERLGERACAFVVpRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-546 |
1.22e-60 |
|
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: 207.68 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeiva 205
Cdd:cd05914 84 FVSDE--------------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtYGPLlhrGKELVVTA-LPLYHIFALTMNCLLFIELGGQNLLITN 284
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKE-VVLL---GKGDKILSiLPLHHIYPLTFTLLLPLLNGAHVVFLDK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 PRdiPGLVKELAKYPFTAMTGVNTLF-----------------------NALLNNKEFQQLDFSSLHLSAGG-------- 333
Cdd:cd05914 165 IP--SAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGnikefvig 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPVQQVVAERWVKLTGQYLlEGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDDdnevAPGEPGELCIKGPQ 413
Cdd:cd05914 243 GAKINPDVEEFLRTIGFPYT-IGYGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILV-SGFNVYPNEIEDVVMQHSGVQEvAAVGVPSG 491
Cdd:cd05914 317 VMKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 492 SS-------GEAVKIFVVKKDA---ALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd05914 396 KLvalayidPDFLDVKALKQRNiidAIKWEVRDKVNQKVPNYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
31-550 |
2.41e-60 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 209.37 E-value: 2.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRYADQPAFI----NMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIavnVNP 106
Cdd:PRK04319 52 HADGGRKDKVALRyldaSRKEKYTYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAI---VGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYT---PRELEHQLNDSGAAaiVIVSNFAHTLEKVVDKT-QVKHVILTrmGDQLSTAKGTLvnfvvkyikrlvpkyhlpd 182
Cdd:PRK04319 128 LFEafmEEAVRDRLEDSEAK--VLITTPALLERKPADDLpSLKHVLLV--GEDVEEGPGTL------------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 aiSFRSALQHG---YRMQYVKPEivadDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHRGKELVVTALP- 258
Cdd:PRK04319 185 --DFNALMEQAsdeFDIEWTDRE----DGAILHYTSGSTGKPKGVLHVHNAMLQHY--QTGKYVLDLHEDDVYWCTADPg 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 -----LYHIFALTMNCLLFIELGGQnlliTNPRDIPGLvkeLAKYP----FTAMTGVNTLFNAllNNKEFQQLDFSSLHL 329
Cdd:PRK04319 257 wvtgtSYGIFAPWLNGATNVIDGGR----FSPERWYRI---LEDYKvtvwYTAPTAIRMLMGA--GDDLVKKYDLSSLRH 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 330 SAGGGMPVQ-QVVaeRW-VKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGEL 407
Cdd:PRK04319 328 ILSVGEPLNpEVV--RWgMKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 408 CIKG--PQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAA 485
Cdd:PRK04319 406 AIKKgwPSMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 486 VGVPSGSSGEAVKIFVVKKDA-----ALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVALRPGyepseELKEE-IRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-485 |
2.47e-59 |
|
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: 202.50 E-value: 2.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDktqvkhVILTRMGDQLSTAKGTLVNFVvkyikrlvpkyhlPDAISfrsalqhgyrmqyvkpeiVADDLA 209
Cdd:TIGR01733 81 ALASRLAGLVL------PVILLDPLELAALDDAPAPPP-------------PDAPS------------------GPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhrGKELVVTALPLYH-------IFAltmnCLLFielGGQNLLI 282
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL----DPDDRVLQFASLSfdasveeIFG----ALLA---GATLVVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 TNP--RDIPGLVKEL-AKYPFTAMTGVNTLFNALLnnkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ-YLLEGYG 358
Cdd:TIGR01733 193 PEDeeRDDAALLAALiAEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGaRLINLYG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 359 LTECSPLVSVNPHDIDYHSG----SIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKDG- 432
Cdd:TIGR01733 270 PTETTVWSTATLVDPDDAPRespvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErFVPDPf 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 433 -------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAA 485
Cdd:TIGR01733 350 aggdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
211-551 |
5.40e-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: 200.68 E-value: 5.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 211 LQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLLHRGKELVVTAL---PLYHI--FALTMNCLLfieLGGQNLLITN- 284
Cdd:cd05929 130 MLYSGGTTGRPKGIK---RGLPGGPPDNDTLMAAALGFGPGADSVYLspaPLYHAapFRWSMTALF---MGGTLVLMEKf 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 -PRDIPGLVKelaKYPFTAMTGVNTLFNALLNNKEFQQ--LDFSSL----HlsAGGGMPVQqvVAERWVKLTGQYLLEGY 357
Cdd:cd05929 204 dPEEFLRLIE---RYRVTFAQFVPTMFVRLLKLPEAVRnaYDLSSLkrviH--AAAPCPPW--VKEQWIDWGGPIIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 358 GLTECSPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDDDNEVAPGEPGELCIKGPQVMLgYWQRPDATDE-IIKDGWLHT 436
Cdd:cd05929 277 GGTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAaRNEGGWSTL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 437 GDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA----LTEEA 512
Cdd:cd05929 355 GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGAdagtALAEE 434
|
330 340 350
....*....|....*....|....*....|....*....
gi 505808171 513 LITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05929 435 LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
12-551 |
1.06e-57 |
|
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: 201.57 E-value: 1.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 12 DVPAEINPDRyQSLVELFEHATTRyadqpafinmgeVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVAL 91
Cdd:cd05970 24 DAMAKEYPDK-LALVWCDDAGEER------------IFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 92 FGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNfaHTLEKVVDKTQVKHVILTRM---GDQLSTAkgtLVNFVv 168
Cdd:cd05970 90 LALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAE--DNIPEEIEKAAPECPSKPKLvwvGDPVPEG---WIDFR- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 169 KYIKRLVPKYHLPDAISfrsalqhgyrmqyvkpEIVADDLAFLQYTGGTTGVAKgaMLTHrnmlanleqvNATYgPLLHr 248
Cdd:cd05970 164 KLIKNASPDFERPTANS----------------YPCGEDILLVYFSSGTTGMPK--MVEH----------DFTY-PLGH- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 249 gkelVVTAL--------PLYHIFALT-----MNCLLFIE-LGGQNLLITN-PRDIP-GLVKELAKYPFTAMTGVNTLFNA 312
Cdd:cd05970 214 ----IVTAKywqnvregGLHLTVADTgwgkaVWGKIYGQwIAGAAVFVYDyDKFDPkALLEKLSKYGVTTFCAPPTIYRF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 313 LLNNKeFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHdIDYHSGSIGLPVPSTEAKLV 392
Cdd:cd05970 290 LIRED-LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW-MEPKPGSMGKPAPGYEIDLI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 393 DDDDNEVAPGEPGELCI---KGPQVML--GYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYP 467
Cdd:cd05970 368 DREGRSCEAGEEGEIVIrtsKGKPVGLfgGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGP 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 468 NEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-----KKDAALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVG 542
Cdd:cd05970 448 FEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISG 526
|
....*....
gi 505808171 543 KILRRELRD 551
Cdd:cd05970 527 KIRRVEIRE 535
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
11-551 |
1.15e-56 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 198.83 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 11 ADVPAEINPDRYQSLV-----------ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVAL 79
Cdd:PRK13382 20 AGLIAPMRPDRYLRIVaamrregmgptSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQ-ALPIGEPRVVGI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 80 MMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKhvilTRMGDQLSTA 159
Cdd:PRK13382 99 MCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQA----TRIVAWTDED 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 160 KGTLVnfvvkyikrlvpkyhlpdaisfrSALQHGYRMQYVKPEIVADDLAFLqyTGGTTGVAKGAMlthrnmlanlEQVN 239
Cdd:PRK13382 175 HDLTV-----------------------EVLIAAHAGQRPEPTGRKGRVILL--TSGTTGTPKGAR----------RSGP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 240 ATYGPLLH-------RGKELVVTALPLYH-------IFALTMNCLLfielggqnllITNPR-DIPGLVKELAKYPFTAMT 304
Cdd:PRK13382 220 GGIGTLKAildrtpwRAEEPTVIVAPMFHawgfsqlVLAASLACTI----------VTRRRfDPEATLDLIDRHRATGLA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 305 GVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGL 382
Cdd:PRK13382 290 VVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 383 PVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYwqRPDATDEIIkDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSG 462
Cdd:PRK13382 370 PAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH-DGFMASGDVGYLDENGRLFVVGRDDEMIVSGG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 463 FNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNV 541
Cdd:PRK13382 447 ENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGAT 526
|
570
....*....|
gi 505808171 542 GKILRRELRD 551
Cdd:PRK13382 527 GKILRRELQA 536
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-487 |
1.23e-56 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 197.20 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGmiAVNVnplytPR-------ELEHQLNDSGA 122
Cdd:cd17640 7 TYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALG--AVDV-----VRgsdssveELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 123 AAIVIvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpE 202
Cdd:cd17640 79 VALVV--------------------------------------------------------------------------E 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 203 IVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllHRGKElVVTALPLYHIFALTmnCLLFIELGGQNLLI 282
Cdd:cd17640 85 NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP--QPGDR-FLSILPIWHSYERS--AEYFIFACGCSQAY 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 TNPRDIPglvKELAKYPFTAMTGVNTLFNALLNN--KEFQQLDFSS---LH-----------LSAGGGMPVQqvvAERWV 346
Cdd:cd17640 160 TSIRTLK---DDLKRVKPHYIVSVPRLWESLYSGiqKQVSKSSPIKqflFLfflsggifkfgISGGGALPPH---VDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 KLTGQYLLEGYGLTECSPLVSVNPHDIDYhSGSIGLPVPSTEAKLVDDDDNEV-APGEPGELCIKGPQVMLGYWQRPDAT 425
Cdd:cd17640 234 EAIGIEVLNGYGLTETSPVVSARRLKCNV-RGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEAT 312
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505808171 426 DEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:cd17640 313 SKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
18-555 |
1.37e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 198.63 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 18 NPDRYQSLVEL--FEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGIL 95
Cdd:PRK08162 11 NAANYVPLTPLsfLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 96 RAGMIAVNVNPLYTPRELEHQLnDSGAAAIVIV-SNFAHTLEKVVDKTQVKHVILTRMGDqlstakgtlvnfvvkyikrl 174
Cdd:PRK08162 90 MAGAVLNTLNTRLDAASIAFML-RHGEAKVLIVdTEFAEVAREALALLPGPKPLVIDVDD-------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 vPKY---HLPDAISFRSALQHGY-RMQYVKPEIVADDLAfLQYTGGTTGVAKGAMLTHRNmlANLEQV-NATYGPLLHRG 249
Cdd:PRK08162 149 -PEYpggRFIGALDYEAFLASGDpDFAWTLPADEWDAIA-LNYTSGTTGNPKGVVYHHRG--AYLNALsNILAWGMPKHP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 250 KELVVtaLPLYHI----FALTMNCLlfielGGQNLLItnpRDI-PGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLD 323
Cdd:PRK08162 225 VYLWT--LPMFHCngwcFPWTVAAR-----AGTNVCL---RKVdPKLIFDLiREHGVTHYCGAPIVLSALINAPAEWRAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 324 FS-SLHLSAGGGMPVQQVVAErwVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSI----------GLPVPSTEAKLV 392
Cdd:PRK08162 295 IDhPVHAMVAGAAPPAAVIAK--MEEIGFDLTHVYGLTETYGPATVCAWQPEWDALPLderaqlkarqGVRYPLQEGVTV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 393 DDDDN--EV-APGEP-GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPN 468
Cdd:PRK08162 373 LDPDTmqPVpADGETiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 469 EIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFV-VKKDAALTEEALITFCRRHLTGYKVPKLVEFrDELPKSNVGKILRR 547
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVeLKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKF 531
|
....*...
gi 505808171 548 ELRDEARA 555
Cdd:PRK08162 532 VLREQAKS 539
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-549 |
1.40e-56 |
|
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: 197.04 E-value: 1.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRA-AGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDSGAAAIVIvsnfAHTLEKVVDKTQVKHVILtrmgDQLSTAkgtlvnfvvkyikrlvpkyhlpDAISF 186
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLEVAVVID----EALDAG----------------------PAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 RSALQhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvNATYGPLlhRGKELVVTALPL------Y 260
Cdd:cd12117 130 AVPVS-------------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTL--GPDDRVLQTSPLafdastF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 261 HIFAltmnCLLFielGGQnlLITNPRDIPGLVKELAKypFTAMTGVNTLF--NALlnnkeFQQLD------FSSL-HLSA 331
Cdd:cd12117 193 EIWG----ALLN---GAR--LVLAPKGTLLDPDALGA--LIAEEGVTVLWltAAL-----FNQLAdedpecFAGLrELLT 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 332 GG-GMPVQQV--VAERWVKLTgqyLLEGYGLTE---CSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPG 405
Cdd:cd12117 257 GGeVVSPPHVrrVLAACPGLR---LVNGYGPTEnttFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 406 ELCIKGPQVMLGYWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:cd12117 334 ELYVGGDGLALGYLNRPALTAErFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHP 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 479 GVQEVAAVGVPSGSSGEAVKIFVVkKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12117 414 GVREAVVVVREDAGGDKRLVAYVV-AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
213-538 |
1.59e-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: 190.21 E-value: 1.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 213 YTGGTTGVAKGAMLTHRN------MLANLEQVNATYGPLlhrgkelvvTALPLYHIFALtMNCLLFIELGGQNLLI--TN 284
Cdd:cd17636 7 YTAAFSGRPNGALLSHQAllaqalVLAVLQAIDEGTVFL---------NSGPLFHIGTL-MFTLATFHAGGTNVFVrrVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 PRDIPGLV-KELAKYPFTAMTGVNTLFNAllnNKEFQqLDFSSLHLSAG--GGMPVQQVVAERWVKLTGqylleGYGLTE 361
Cdd:cd17636 77 AEEVLELIeAERCTHAFLLPPTIDQIVEL---NADGL-YDLSSLRSSPAapEWNDMATVDTSPWGRKPG-----GYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 362 CSPLVSVNPHDIDYHSGSiGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAV 441
Cdd:cd17636 148 VMGLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 442 MDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK-IFVVKKDAALTEEALITFCRRH 520
Cdd:cd17636 227 REPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKaIVVLKPGASVTEAELIEHCRAR 306
|
330
....*....|....*...
gi 505808171 521 LTGYKVPKLVEFRDELPK 538
Cdd:cd17636 307 IASYKKPKSVEFADALPR 324
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-549 |
1.98e-55 |
|
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: 194.08 E-value: 1.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIVIVsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyiKRLVPKYHLPD 182
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVP-------------------------------------------DRHAGFDHRAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 AISFRSALqhgyrmqyvkPEIvaddlAFLQYTGGTTGVAKGAMLTHR----NMLANLEqvnatygpLLHRGKELV-VTAL 257
Cdd:cd05920 131 ARELAESI----------PEV-----ALFLLSGGTTGTPKLIPRTHNdyayNVRASAE--------VCGLDQDTVyLAVL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHIFALT----MNCLLFielGGQNLLITNPRdiPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:cd05920 188 PAAHNFPLAcpgvLGTLLA---GGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 333 GGMPVQQVVAERWVKLTGQYLLEGYGLTEcsPLVSV----NPHDIDYHSGsiGLPV-PSTEAKLVDDDDNEVAPGEPGEL 407
Cdd:cd05920 263 GGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYtrldDPDEVIIHTQ--GRPMsPDDEIRVVDEEGNPVPPGEEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 408 CIKGPQVMLGYWQRPDA-TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAV 486
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHnARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 487 GVPSGSSGEAVKIFVVKKDAALTEEALitfcRRHLTG-----YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05920 419 AMPDELLGERSCAFVVLRDPPPSAAQL----RRFLRErglaaYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-549 |
2.29e-55 |
|
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: 193.23 E-value: 2.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 35 RYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPlYTPREle 114
Cdd:cd05945 3 ANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSPAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 115 hqlndsgaaaivivsnfahtlekvvdktqvkhviltRMGDQLSTAKGTLVnfvvkyikrlvpkyhlpdaisfrsalqhgy 194
Cdd:cd05945 79 ------------------------------------RIREILDAAKPALL------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 195 rmqyvkpEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtYGPLlhrGKELVVTALPLYHiFAL-TMNclLFI 273
Cdd:cd05945 93 -------IADGDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLS-DFPL---GPGDVFLNQAPFS-FDLsVMD--LYP 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 274 ELGGQNLLITNPRDIPG----LVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLS--AGGGMPVQQvvAERWVK 347
Cdd:cd05945 159 ALASGATLVPVPRDATAdpkqLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFlfCGEVLPHKT--ARALQQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 348 LT-GQYLLEGYGLTECSPLVS---VNPHDID-YHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRP 422
Cdd:cd05945 237 RFpDARIYNTYGPTEATVAVTyieVTPEVLDgYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNP 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 423 DATDE----IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK 498
Cdd:cd05945 317 EKTAAaffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELI 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 505808171 499 IFVVKKDA--ALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05945 397 AFVVPKPGaeAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
47-552 |
5.77e-55 |
|
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: 194.22 E-value: 5.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVM-TYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05928 39 EVKwSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNFAHTLEKVVDKTQvkhviltrmgdQLSTakgtlvnfvvkyiKRLVPKYHLPDAISFRSALQHGyRMQYVKPEIVA 205
Cdd:cd05928 119 VTSDELAPEVDSVASECP-----------SLKT-------------KLLVSEKSRDGWLNFKELLNEA-STEHHCVETGS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYgpllhrgkelvVTALPLYHIF--------ALTMNCLLFIE-LG 276
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGL-KVNGRY-----------WLDLTASDIMwntsdtgwIKSAWSSLFEPwIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLITN-PR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLL 354
Cdd:cd05928 242 GACVFVHHlPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTEcSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIK-GPQ----VMLGYWQRPDATDEII 429
Cdd:cd05928 321 EGYGQTE-TGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 430 KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALT 509
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 505808171 510 --EEALITFCRRHLTG----YKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:cd05928 480 hdPEQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
14-558 |
1.49e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 193.04 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 14 PAEINPDRYQSLVElfEHATTRyADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK06164 4 DAAPRADTLASLLD--AHARAR-PDAVALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 94 ILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS-----NFAHTLEKV---VDKTqVKHVILTRMGDQLSTAKGTLVN 165
Cdd:PRK06164 80 CARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVppdALPP-LRAIAVVDDAADATPAPAPGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 166 FVVkyikrlvPKYHLPDAISfrsalqhgyrmQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpl 245
Cdd:PRK06164 159 VQL-------FALPDPAPPA-----------AAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYG-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 246 LHRGkELVVTALPLYHIFALTMncLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNnKEFQQLDFS 325
Cdd:PRK06164 219 YDPG-AVLLAALPFCGVFGFST--LLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILD-TAGERADFP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 326 SLHLS-----AGGGMPVQQVVAERWVKLTGQYllegyGLTECSPLVSVNPHDIDY---HSGSiGLPV-PSTEAKLVDDDD 396
Cdd:PRK06164 295 SARLFgfasfAPALGELAALARARGVPLTGLY-----GSSEVQALVALQPATDPVsvrIEGG-GRPAsPEARVRARDPQD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 NEVAP-GEPGELCIKGPQVMLGYWQRPDAT-DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:PRK06164 369 GALLPdGESGEIEIRAPSLMRGYLDNPDATaRALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 475 MQHSGVQEVAAVGVPSGSSGEAVKiFVVKKDAA-LTEEALITFCRRHLTGYKVPKLVEFRDELP---KSNVGKILRRELR 550
Cdd:PRK06164 449 EALPGVAAAQVVGATRDGKTVPVA-FVIPTDGAsPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLR 527
|
....*...
gi 505808171 551 DEARAKVD 558
Cdd:PRK06164 528 EMAQARLA 535
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
14-551 |
1.34e-53 |
|
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: 190.57 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 14 PAEINPDRYQSLVELFEHATTRYADQ-PAFINM---GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPV 89
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKgITYIDAdgsEEFQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 90 ALFGILRAGMIAVNVNPLYTPRELEHQLNDsgaaaiviVSNFAHTLEKVVdktqvkhvILT--RMGDQLSTAKGTLVnfv 167
Cdd:cd05906 80 AFWACVLAGFVPAPLTVPPTYDEPNARLRK--------LRHIWQLLGSPV--------VLTdaELVAEFAGLETLSG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 168 vkyikrlvpkyHLPDAISFRSALQHGYRmQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG---- 243
Cdd:cd05906 141 -----------LPGIRVLSIEELLDTAA-DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGltpq 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 244 -------PLLHrgkelvVTALPLYHIFALTMNCLLF---IELggqnlLITNPRDIPGLVKelaKYPFTAMTGVNTLFnAL 313
Cdd:cd05906 209 dvflnwvPLDH------VGGLVELHLRAVYLGCQQVhvpTEE-----ILADPLRWLDLID---RYRVTITWAPNFAF-AL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 314 LNNK----EFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTE-CSPLV-----SVNPHDIDYHS 377
Cdd:cd05906 274 LNDLleeiEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPpdairpAFGMTEtCSGVIysrsfPTYDHSQALEF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 378 GSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDeGFLRIVDRKKD 456
Cdd:cd05906 354 VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDN-GNLTITGRTKD 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 457 MILVSGFNVYPNEIEDVVMQHSGVQE--VAAVGV--PSGSSGEAVKIFVVKKDAALTEEALITFCRRHLT---GYKVPKL 529
Cdd:cd05906 433 TIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVrdPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSrevGVSPAYL 512
|
570 580
....*....|....*....|...
gi 505808171 530 VEF-RDELPKSNVGKILRRELRD 551
Cdd:cd05906 513 IPLpKEEIPKTSLGKIQRSKLKA 535
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
31-550 |
1.47e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 186.75 E-value: 1.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFI--NMGEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:PRK13390 6 HAQIA-PDRPAVIvaETGEQVSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 109 TPRELEHQLNDSGAAAIVIVSnfahTLEKVVDKTQVKHVILTRMGdqlstakGTLVNFVvkyikrlvpkyhlpdaiSFRS 188
Cdd:PRK13390 84 TAPEADYIVGDSGARVLVASA----ALDGLAAKVGADLPLRLSFG-------GEIDGFG-----------------SFEA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 189 ALQHGyrmqyvKPEIVADDL-AFLQYTGGTTGVAKGAM--LTHRNMLANLEQVNATYGPLLH-RGKELVVTALPLYHIFA 264
Cdd:PRK13390 136 ALAGA------GPRLTEQPCgAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDiSESDIYYSSAPIYHAAP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LTMnCLLFIELGGqNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALL--NNKEFQQLDFSSLHLSAGGGMPVQQVVA 342
Cdd:PRK13390 210 LRW-CSMVHALGG-TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTeAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRP 422
Cdd:PRK13390 288 HAMIDWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 423 DATDEIIKDG---WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKI 499
Cdd:PRK13390 367 EKTAAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 500 FV-----VKKDAALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK13390 447 VIqlvegIRGSDELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-555 |
2.06e-52 |
|
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: 193.15 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 4 VWLNRYPADVPAEinpdryQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPN 83
Cdd:COG1020 463 AEWNATAAPYPAD------ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLER 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 84 LLQYPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDSGAAAIVIVSNFAHTLekvvDKTQVKHVILtrmgDQLSTAkgt 162
Cdd:COG1020 536 SLEMVVALLAVLKAGAAYVPLDPAY-PAErLAYMLEDAGARLVLTQSALAARL----PELGVPVLAL----DALALA--- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 163 lvnfvvkyikrlvpkyHLPDAisfrsalqhgyrmqYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:COG1020 604 ----------------AEPAT--------------NPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 243 GpLLHRGKELVVTAL----PLYHIFAltmnCLLFielGGQnLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLn 315
Cdd:COG1020 654 G-LGPGDRVLQFASLsfdaSVWEIFG----ALLS---GAT-LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 316 nkEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY-LLEGYGLTECSPLVS---VNPHDIDYHSGSIGLPVPSTEAKL 391
Cdd:COG1020 724 --DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTETTVDSTyyeVTPPDADGGSVPIGRPIANTRVYV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 392 VDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDE------IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGF 463
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 464 NVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALITFC-RRHLTGYKVPKLVEFRDELPKSNVG 542
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGNG 961
|
570
....*....|...
gi 505808171 543 KILRRELRDEARA 555
Cdd:COG1020 962 KLDRLALPAPAAA 974
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-549 |
1.46e-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: 180.56 E-value: 1.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYtPRE-LEHQ 116
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 117 LNDSGAAAIVIVSNFAHTLekvvdktqvkHVILTRMGDQLSTAKGTLVNfvvkyikrlvpkyhlpdaisfrsalqhgyrm 196
Cdd:cd12116 80 LEDAEPALVLTDDALPDRL----------PAGLPVLLLALAAAAAAPAA------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 197 qyVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHRGKELVVTALPLYHIFALTmncLLFIELG 276
Cdd:cd12116 119 --PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLG--LGPGDRLLAVTTYAFDISLLE---LLLPLLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNkEFQQLDfsSLHLSAGGgMPVQQVVAERWVKLTGQyL 353
Cdd:cd12116 192 GARVVIAPRetqRDPEALARLIEAHSITVMQATPATWRMLLDA-GWQGRA--GLTALCGG-EALPPDLAARLLSRVGS-L 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 354 LEGYGLTECSPLVSVnpHDIDYHSGS--IGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKD 431
Cdd:cd12116 267 WNLYGPTETTIWSTA--ARVTAAAGPipIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 432 G--------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVK 503
Cdd:cd12116 345 DpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 505808171 504 KDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12116 425 AGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-551 |
7.01e-49 |
|
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: 172.13 E-value: 7.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHrGKELVvtALPLYHI--FALTMNCLLfielGGQNLLITN 284
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGG-DSWLL--SLPLYHVggLAILVRSLL----AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 PRDipGLVKELAKYPFTAMTGVNT-LFNALLNNKEFQQLDfsSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTECS 363
Cdd:cd17630 74 RNQ--ALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 364 PLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDddnevapgepGELCIKGPQVMLGYWqRPDATDEIIKDGWLHTGDIAVMD 443
Cdd:cd17630 149 SQVATKRPD-GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVkIFVVKKDAALTEEALITFCRRHLTG 523
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLAR 295
|
330 340
....*....|....*....|....*...
gi 505808171 524 YKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-550 |
1.59e-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: 178.07 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGE-----VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIA 101
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 102 VNVNPLYTPRELEHQLNDSGAAAIVIVSNFAH-----TLEKVVDKT-----QVKHVILTRMGDQLSTAkgTLVNFVvkyi 171
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADGFTRrgrevNLKEEADKAcaqcpTVEKVVVVRHLGNDFTP--AKGRDL---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 172 krlvpKYHLPDAisfrSALQHGYRMQyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMlanleqvnatygPLlhrgke 251
Cdd:cd05968 218 -----SYDEEKE----TAGDGAERTE-------SEDPLMIIYTSGTTGKPKGTVHVHAGF------------PL------ 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 252 lvVTALPLYHIFALTMNCLLF-----------------IELGGQNLLITNPRDIPG---LVKELAKYPFTAMTGVNTLFN 311
Cdd:cd05968 264 --KAAQDMYFQFDLKPGDLLTwftdlgwmmgpwlifggLILGATMVLYDGAPDHPKadrLWRMVEDHEITHLGLSPTLIR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 312 ALLNNKE--FQQLDFSSLHLSAGGGMPVQqvvAERWvkltgQYLLEGYGLTECsPLvsvnphdIDYHSG----------- 378
Cdd:cd05968 342 ALKPRGDapVNAHDLSSLRVLGSTGEPWN---PEPW-----NWLFETVGKGRN-PI-------INYSGGteisggilgnv 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 379 --------SIGLPVPSTEAKLVDDDDNEVaPGEPGELCIKGPQVML--GYWQRPDATDEI----IKDGWLHtGDIAVMDD 444
Cdd:cd05968 406 likpikpsSFNGPVPGMKADVLDESGKPA-RPEVGELVLLAPWPGMtrGFWRDEDRYLETywsrFDNVWVH-GDFAYYDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD-----AALTEEaLITFCRR 519
Cdd:cd05968 484 EGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEALAEE-LMERVAD 562
|
570 580 590
....*....|....*....|....*....|.
gi 505808171 520 HLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05968 563 ELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-549 |
5.29e-48 |
|
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: 174.00 E-value: 5.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 26 VELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVN 105
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 106 PLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDqlstakgtlvnfvvkyikrlvpkyHLPDais 185
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPA------------------------TPPL--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 186 frsalqhgyrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHRGKELVVTALPlyhiFAL 265
Cdd:cd17646 133 ---------------VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY-PLGPGDRVLQKTPLS----FDV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 266 TMNCLLFIELGGQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDfsSLHLSAGGGMPVQQVVA 342
Cdd:cd17646 193 SVWELFWPLVAGARLVVARPgghRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQYLLEGYGLTECSplVSVNPH----DIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGY 418
Cdd:cd17646 271 ARFLALPGAELHNLYGPTEAA--IDVTHWpvrgPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 419 WQRPDATDEIIKDGWL-------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSG 491
Cdd:cd17646 349 LGRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAP 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 492 SSGEAVKIFVVKKDAA--LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17646 429 AGAARLVGYVVPAAGAagPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-483 |
1.49e-46 |
|
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: 171.24 E-value: 1.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFA-AYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLY---TPRELEHQLNDSGAAA 124
Cdd:cd05927 6 ISYKEVAERADNIGsALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 125 IVIVSNFahtleKVVDKTQVKHviltrMGDqlstakgtlvnfvvKYIKRLVPKyhlpdaisfrsalqhgyrmqyvKPEiv 204
Cdd:cd05927 83 VFCDAGV-----KVYSLEEFEK-----LGK--------------KNKVPPPPP----------------------KPE-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 205 adDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGKELV-VTALPLYHIF-ALTMNCLLFIelGGQnllI 282
Cdd:cd05927 115 --DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyISYLPLAHIFeRVVEALFLYH--GAK---I 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 TNPR-DIPGLVKELAKYPFTAMTGV----------------------NTLFNALLNNKE-------------FQQLDFSS 326
Cdd:cd05927 188 GFYSgDIRLLLDDIKALKPTVFPGVprvlnriydkifnkvqakgplkRKLFNFALNYKLaelrsgvvraspfWDKLVFNK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 327 LHLSAG--------GGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVD----- 393
Cdd:cd05927 268 IKQALGgnvrlmltGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPG-DTSVGHVGGPLPCAEVKLVDvpemn 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 394 ----DDDNEvapgepGELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYP 467
Cdd:cd05927 347 ydakDPNPR------GEVCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAP 420
|
490
....*....|....*.
gi 505808171 468 NEIEDVVMQHSGVQEV 483
Cdd:cd05927 421 EKIENIYARSPFVAQI 436
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-551 |
1.87e-46 |
|
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: 168.64 E-value: 1.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQ-LGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDSGAAAIVIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTDS-------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsalqhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRgKELVVTALPLYHIFALT 266
Cdd:cd17653 104 ------------------PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGS-RVAQVLSIAFDACIGEI 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 267 MNCLLFielGGQNLLITNPRDIPGLVKELAKYPFTAMtgvntlFNALLNNKEFQQLDFSSLhlsagGGMPVQQVVAERWV 346
Cdd:cd17653 165 FSTLCN---GGTLVLADPSDPFAHVARTVDALMSTPS------ILSTLSPQDFPNLKTIFL-----GGEAVPPSLLDRWS 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 KltGQYLLEGYGLTECSpLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATD 426
Cdd:cd17653 231 P--GRRLYNAYGPTECT-ISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 427 EIIK-----DGWLH--TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HSGVQEVAAVgvpsgSSGEAVK 498
Cdd:cd17653 308 SKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQsQPEVTQAAAI-----VVNGRLV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 505808171 499 IFVVKKDAAltEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17653 383 AFVTPETVD--VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-547 |
2.70e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 170.45 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAFINMGE--VMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIA 101
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 102 VNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHtleKVVDKTQVKHVILTRMGDQLSTAKGTLvnfvvkyikrlvpKYHLP 181
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPH---DRAEPTTRWWPLTVNVGGDSGPSGGTL-------------SVHLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 182 DAI--SFRSALQHGYRmqyvkpeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY--GPllhrgKELVVTAL 257
Cdd:PRK05852 160 AATepTPATSTPEGLR----------PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYrlSP-----RDATVAVM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHIFALTMNCLLFIELGGQNLLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSSLHLSAGGG 334
Cdd:PRK05852 225 PLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLEraATEPSGRKPAALRFIRSCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 335 MPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHS----GSIGLPVPSTEA--KLVDDDDNEVAPGEPGELC 408
Cdd:PRK05852 305 APLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvVSTGLVGRSTGAqiRIVGSDGLPLPAGAVGEVW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 409 IKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGV 488
Cdd:PRK05852 385 LRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 489 PSGSSGEAVKIFVVKKD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRR 547
Cdd:PRK05852 465 PDQLYGEAVAAVIVPREsAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
9.24e-46 |
|
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: 166.92 E-value: 9.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYT---PRELEHQLNDSGAAai 125
Cdd:cd05973 1 LTFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNFAHtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfRSALqhgyrmqyvkpeivA 205
Cdd:cd05973 75 LVVTDAAN-----------------------------------------------------RHKL--------------D 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHRGKELVVTALP--LYHIFALTMNCLLfieLGGQNLLIT 283
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAVDLRPEDSFWNAADPgwAYGLYYAITGPLA---LGHPTILLE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 284 NPRDIPGLVKELAKYPFTAMTGVNTLFNALL-NNKEFQQLDFSSLHLSAGGGMPVQQVVAeRWVKLT-GQYLLEGYGLTE 361
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTAYRLLMaAGAEVPARPKGRLRRVSSAGEPLTPEVI-RWFDAAlGVPIHDHYGQTE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 362 CSpLVSVNPHDIDY--HSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVML----GYWQRPDATdeiIKDGWLH 435
Cdd:cd05973 242 LG-MVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLmwfrGYQLPDTPA---IDGGYYL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-----KKDAALTE 510
Cdd:cd05973 318 TGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPALAD 397
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505808171 511 EaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05973 398 E-LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-550 |
2.78e-45 |
|
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: 166.75 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 29 FEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLR-ARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 109 TPRELEHQLNDSGAAAIVIVSNFAHTLEkvvdktqVKHVILTRMGDQLSTAKGTLVNFvvkyikrlvpkyhlpdaisfrs 188
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELA-------VELVAVTLLDQPGAAAGADAEPD---------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 189 alqhgyrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQVNATYGPLlHRGKELVVTALPLYHIFALTMN 268
Cdd:cd17651 131 ------------PALDADDLAYVIYTSGSTGRPKGVVMPHR-SLANLVAWQARASSL-GPGARTLQFAGLGFDVSVQEIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 269 CLLfieLGGQNLLITNPR---DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLH--LSAGGGMPVQQVVAE 343
Cdd:cd17651 197 STL---CAGATLVLPPEEvrtDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRylLTGGEQLVLTEDLRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWVKLTGQYLLEGYGLTEcSPLVS--VNPHDIDYH--SGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYW 419
Cdd:cd17651 274 FCAGLPGLRLHNHYGPTE-THVVTalSLPGDPAAWpaPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 420 QRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGS 492
Cdd:cd17651 353 NRPELTAErFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 493 SGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17651 433 GEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
38-550 |
7.91e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 165.34 E-value: 7.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKgdRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIvsnfahtlekvvdktqvkhviLTRMGDQLSTAKGTLVNfvVKYIKRLVPKYhlPDAISFRSALQHgyrmq 197
Cdd:PRK07638 94 AISNADMIVT---------------------ERYKLNDLPDEEGRVIE--IDEWKRMIEKY--LPTYAPIENVQN----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivadDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYGPLLHRGKELVVTALpLYHIFALTMNCLLFIelgG 277
Cdd:PRK07638 144 ---------APFYMGFTSGSTGKPKAFLRAQQSWLHSF-DCNVHDFHMKREDSVLIAGTL-VHSLFLYGAISTLYV---G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 QNLLITnPRDIPGLVKE-LAKYPFTAMTGVNTLFNALLNNKEFqqLDFSSLHLSAGGGMPVQQV--VAERWVKLTgqyLL 354
Cdd:PRK07638 210 QTVHLM-RKFIPNQVLDkLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGAKWEAEAKekIKNIFPYAK---LY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWL 434
Cdd:PRK07638 284 EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 435 HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEaVKIFVVKKDAalTEEALI 514
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE-KPVAIIKGSA--TKQQLK 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 505808171 515 TFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07638 441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-549 |
1.06e-44 |
|
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: 164.02 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLR-AEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVivsnfahtlekvvdkTQvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmq 197
Cdd:cd17643 81 ADSGPSLLL---------------TD------------------------------------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY------------------------GPLLHrGKELV 253
Cdd:cd17643 92 -------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgfneddvwtlfhsyafdfsvweiwGALLH-GGRLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 254 VtalPLYHIfALTmncllfielggqnllitnPRDIPGLVKELAkypFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGG 333
Cdd:cd17643 164 V---VPYEV-ARS------------------PEDFARLLRDEG---VTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPVQQVVAERWVK---LTGQYLLEGYGLTECSPLVS---VNPHDIDYHSGS-IGLPVPSTEAKLVDDDDNEVAPGEPGE 406
Cdd:cd17643 219 GEALEAAMLRPWAGrfgLDRPQLVNMYGITETTVHVTfrpLDAADLPAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGE 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 407 LCIKGPQVMLGYWQRPDATDEIIKDG--------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:cd17643 299 LYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505808171 479 GVQEvAAVGVPSGSSGEA--VKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17643 379 SVRD-AAVIVREDEPGDTrlVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
27-549 |
8.78e-44 |
|
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: 161.72 E-value: 8.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDSGAAaivivsnfahtlekvvdktqvkhVILTRmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd12115 82 AYPPERLRFILEDAQAR-----------------------LVLTD----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsalqhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGKeLVVTA----LPLYHI 262
Cdd:cd12115 104 ------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGV-LASTSicfdLSVFEL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 263 FAlTMNCllfielGGQNLLITNPRDIPGLVkelAKYPFTAMTGVNTLFNALLNNKEFQQlDFSSLHLsAGGGMPvQQVVA 342
Cdd:cd12115 165 FG-PLAT------GGKVVLADNVLALPDLP---AAAEVTLINTVPSAAAELLRHDALPA-SVRVVNL-AGEPLP-RDLVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQYLLEGYGLTEC---SPLVSVNPHDIDyhSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYW 419
Cdd:cd12115 232 RLYARLQVERVVNLYGPSEDttySTVAPVPPGASG--EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 420 QRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVGVPSGS 492
Cdd:cd12115 310 GRPGLTAErFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE-AVVVAIGDA 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 493 SGEA--VKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12115 389 AGERrlVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
50-554 |
1.38e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 162.95 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:PRK07008 41 TYRDCERRAKQLAQALA-ALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDK-TQVKHVILtrMGDqlstakgtlvnfvvkyikrlvpKYHLP-DAISFRS--ALQHGYRMQYVKPEIVA 205
Cdd:PRK07008 120 TFLPLVDALAPQcPNVKGWVA--MTD----------------------AAHLPaGSTPLLCyeTLVGAQDGDYDWPRFDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNmlanleQVNATYGPLLH-----RGKELVVTALPLYHIFA--LTMNCllfiELGGQ 278
Cdd:PRK07008 176 NQASSLCYTSGTTGNPKGALYSHRS------TVLHAYGAALPdamglSARDAVLPVVPMFHVNAwgLPYSA----PLTGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 279 NLLITNPrDIPGL-VKEL---AKYPFTAmtGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLL 354
Cdd:PRK07008 246 KLVLPGP-DLDGKsLYELieaERVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSV----NPHDIDYHSGSI------GLPVPSTEAKLVDDDDNEVapgeP------GELCIKGPQVMLGY 418
Cdd:PRK07008 323 HAWGMTEMSPLGTLcklkWKHSQLPLDEQRkllekqGRVIYGVDMKIVGDDGREL----PwdgkafGDLQVRGPWVIDRY 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 419 WQRpdaTDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK 498
Cdd:PRK07008 399 FRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPL 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 499 IFVVKKDAA-LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PRK07008 476 LVVVKRPGAeVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
18-544 |
1.49e-43 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 166.68 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 18 NPDRYQSLVELFEHATTRYADQPAFIN--MGEVMTYRKLEERSRAFAAYLQQGLGLqkGDRVALMMPNLLQYPVALFGIL 95
Cdd:PRK06814 626 TSDYDRTLFEALIEAAKIHGFKKLAVEdpVNGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQ 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 96 RAGMIAVNVNplYTprelehqlndSGAAAIVIVSNFAhtlekvvdktQVKHVILTR-------MGDqLSTAKGTLVNFVv 168
Cdd:PRK06814 704 SAGRVPAMIN--FS----------AGIANILSACKAA----------QVKTVLTSRafiekarLGP-LIEALEFGIRII- 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 169 kYIKRLVPKYHLPDAISfrsALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAT--YGPll 246
Cdd:PRK06814 760 -YLEDVRAQIGLADKIK---GLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARidFSP-- 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 247 hrgKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNP---RDIPGLVKELAKypfTAMTGVNTLFNALLNNKefQQLD 323
Cdd:PRK06814 834 ---EDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSPlhyRIIPELIYDTNA---TILFGTDTFLNGYARYA--HPYD 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 324 FSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVN-P-HDidyHSGSIGLPVPSTEAKLvddddnEVAP 401
Cdd:PRK06814 906 FRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNtPmHN---KAGTVGRLLPGIEYRL------EPVP 976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 G--EPGELCIKGPQVMLGYWqRPDA--TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKK-------DMILVSGFNVYPNEI 470
Cdd:PRK06814 977 GidEGGRLFVRGPNVMLGYL-RAENpgVLEPPADGWYDTGDIVTIDEEGFITIKGRAKrfakiagEMISLAAVEELAAEL 1055
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 471 eDVVMQHsgvqevAAVGVPSGSSGEAVKIFVVKKDAalTEEALITFCRRH-LTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PRK06814 1056 -WPDALH------AAVSIPDARKGERIILLTTASDA--TRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-549 |
1.28e-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: 158.97 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVivsnfahtlekvVDKTQVKHVILTrmgdqlstakgtlvnfvvkyikrlvpkyhlPDAISFRSALQHGYRMQ 197
Cdd:cd12114 81 ADAGARLVL------------TDGPDAQLDVAV------------------------------FDVLILDLDALAAPAPP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHRGKELVVTA-------LPLYHIFALTmncl 270
Cdd:cd12114 119 -PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF----AVGPDDRVLAlsslsfdLSVYDIFGAL---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 271 lfiELGGQNLLITNPRDI-PGLVKELA-KYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGG--MPVQQvvAERWV 346
Cdd:cd12114 190 ---SAGATLVLPDEARRRdPAHWAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDL--PARLR 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 KLTGQYLLEGYG-LTECS------PLVSVNPHDidyhsGSI--GLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLG 417
Cdd:cd12114 265 ALAPDARLISLGgATEASiwsiyhPIDEVPPDW-----RSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 418 YWQRPDATDE---IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGs 492
Cdd:cd12114 340 YLGDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP- 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 493 SGEAVKIFVV--KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12114 419 GGKRLAAFVVpdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
27-549 |
1.66e-42 |
|
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: 159.03 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDSGAAAIVIVSNFAHTLEkvvdktQVKHVILTRMGDqlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIA------FIGLIDLLDEDT-------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsaLQHGYRMQyVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHRGKELVVTALPLYHiFALT 266
Cdd:cd17655 122 ---IYHEESEN-LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI----YQGEHLRVALFASIS-FDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 267 MNCLLFIELGGQNLLITnPR----DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLhLSAGGGMPvqQVVA 342
Cdd:cd17655 193 VTEIFASLLSGNTLYIV-RKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL-IVGGEALS--TELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQ--YLLEGYGLTE---CSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLG 417
Cdd:cd17655 269 KKIIELFGTnpTITNAYGPTEttvDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 418 YWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVGVPS 490
Cdd:cd17655 349 YLNRPELTAEkFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE-AVVIARK 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 491 GSSGEAV--KIFVVKKDaaLTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17655 428 DEQGQNYlcAYIVSEKE--LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
207-546 |
1.79e-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: 155.50 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQvnatygpLLHRGKELVV-----TALPLYHIFAL--TMNCLLF---IELG 276
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVgdvtyLPLPATHIGGLwwILTCLIHgglCVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLITNprdipgLVKELAKYPFTAMTGVNTLFNALLN-----NKEFQQLDFsslhLSAGGGMPVQQVVAE-RWVKLTG 350
Cdd:cd17635 75 GENTTYKS------LFKILTTNAVTTTCLVPTLLSKLVSelksaNATVPSLRL----IGYGGSRAIAADVRFiEATGLTN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 351 qyLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIK 430
Cdd:cd17635 145 --TAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKdAALTE 510
Cdd:cd17635 223 DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS-AELDE 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 505808171 511 E---ALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17635 302 NairALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-546 |
4.13e-42 |
|
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: 153.72 E-value: 4.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 213 YTGGTTGVAKGAMLTHRNMLANLEQVNATYgpLLHRGKELVVTAlPLYHifALTMNCLLFIELGGQNLLITNPRDIPGLV 292
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLF--NISGEDAILAPG-PLSH--SLFLYGAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 293 KELAKYPFTAMTGVNTLFNALLNNkEFQQLDFSSLhLSAGGGMP--VQQVVAERWVKLTgqyLLEGYGLTECSpLVSVNP 370
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFesTKKKLKNIFPKAN---LIEFYGTSELS-FITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 371 HDIDYHSGSIGLPVPSTEAKLVDDDDNEVapgepGELCIKGPQVMLGYWQrpdaTDEIIKDGWLHTGDIAVMDDEGFLRI 450
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVR----GGFSNPDGWMSVGDIGYVDEEGYLYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 451 VDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVkIFVVKKDaALTEEALITFCRRHLTGYKVPKLV 530
Cdd:cd17633 227 VGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFLKQKLSRYEIPKKI 304
|
330
....*....|....*.
gi 505808171 531 EFRDELPKSNVGKILR 546
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
43-553 |
2.14e-41 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 157.27 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 43 INMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGA 122
Cdd:PLN02860 27 ISGNRRRTGHEFVDGVLSLAAGLLR-LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 123 AAIVIVSNFAHTLEKVvDKTQVKHVILTRMGDQLSTAKGTLVNfvvkyikrlvpkyhlpDAISFRSALQHGYRMQYVKPE 202
Cdd:PLN02860 106 VMLVTDETCSSWYEEL-QNDRLPSLMWQVFLESPSSSVFIFLN----------------SFLTTEMLKQRALGTTELDYA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 203 IVADDLAFLQYTGGTTGVAKGAMLTHRNM----LANLEQVNatYGP---LLHrgkelvvTAlPLYHIFALTmNCLLFIEL 275
Cdd:PLN02860 169 WAPDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAIVG--YGEddvYLH-------TA-PLCHIGGLS-SALAMLMV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 276 GGQNLLItnPR-DIPGLVKELAKYPFTAMTGVNTLFNALL--NNKEFQQLDFSSLH--LSAGGGMPVQQVVAERWVkLTG 350
Cdd:PLN02860 238 GACHVLL--PKfDAKAALQAIKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRkiLNGGGSLSSRLLPDAKKL-FPN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 351 QYLLEGYGLTE-CSPLVSVNPHDID---------------------YHSGSIGLPVPSTEAKLVDDDDNEVapgepGELC 408
Cdd:PLN02860 315 AKLFSAYGMTEaCSSLTFMTLHDPTlespkqtlqtvnqtksssvhqPQGVCVGKPAPHVELKIGLDESSRV-----GRIL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 409 IKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:PLN02860 390 TRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 488 VPSGSSGEAVKIFV---------------VKKDAALTEEALITFCR-RHLTGYKVPKL-VEFRDELPKSNVGKILRRELR 550
Cdd:PLN02860 470 VPDSRLTEMVVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCReKNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVR 549
|
...
gi 505808171 551 DEA 553
Cdd:PLN02860 550 REV 552
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
26-557 |
4.84e-41 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 156.33 E-value: 4.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 26 VELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIavnVN 105
Cdd:PLN03102 17 ITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAV---LN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 106 PLYTprelehQLNDSGAAAIVivsnfAHTLEKV--VDKTqvkHVILTRMGDQLSTAKGTLVNFVVKYIKRL-VPKYHLPD 182
Cdd:PLN03102 93 PINT------RLDATSIAAIL-----RHAKPKIlfVDRS---FEPLAREVLHLLSSEDSNLNLPVIFIHEIdFPKRPSSE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 AISFRSALQHG-------YRMQYVKPEivaDDLAFLQYTGGTTGVAKGAMLTHRNmlANLEQVNATYGPLLHRGKELVVT 255
Cdd:PLN03102 159 ELDYECLIQRGeptpslvARMFRIQDE---HDPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 256 aLPLYHIFALTMNCLLFIElGGQNLLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSS-LHLSAGGG 334
Cdd:PLN03102 234 -LPMFHCNGWTFTWGTAAR-GGTSVCMRHV-TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 335 MPVQQVVAErwVKLTGQYLLEGYGLTECS-PLVSVNPHD------------IDYHSGSIGLPVPSTEAKlvDDDDNEVAP 401
Cdd:PLN03102 311 PPPAALVKK--VQRLGFQVMHAYGLTEATgPVLFCEWQDewnrlpenqqmeLKARQGVSILGLADVDVK--NKETQESVP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 GEP---GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:PLN03102 387 RDGktmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 479 GVQEVAAVGVPSGSSGEAVKIFVVKK----------DAALTEEA-LITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRR 547
Cdd:PLN03102 467 KVLETAVVAMPHPTWGETPCAFVVLEkgettkedrvDKLVTRERdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKP 546
|
570
....*....|
gi 505808171 548 ELRDEARAKV 557
Cdd:PLN03102 547 KLRDIAKGLV 556
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
6-473 |
9.48e-41 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 156.41 E-value: 9.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 6 LNRYPaDVPaEInpdryQSLVELFEHATTRYADQPAFIN-------MGEV--MTYRKLEERSRAFAAYLQQgLGLQKGDR 76
Cdd:PLN02736 34 VSRFP-DHP-EI-----GTLHDNFVYAVETFRDYKYLGTrirvdgtVGEYkwMTYGEAGTARTAIGSGLVQ-HGIPKGAC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 77 VALMMPNLLQYPVALFGILRAGMIAVnvnPLYtprelehqlnDS-GAAAIVIVSNFAhTLEKVVDKTQVKHVILTRMGdQ 155
Cdd:PLN02736 106 VGLYFINRPEWLIVDHACSAYSYVSV---PLY----------DTlGPDAVKFIVNHA-EVAAIFCVPQTLNTLLSCLS-E 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 156 LSTAKgTLVnfVVKYIKRLVPKyhLPDA-----ISFRSALQHGYRMQ--YVKPEivADDLAFLQYTGGTTGVAKGAMLTH 228
Cdd:PLN02736 171 IPSVR-LIV--VVGGADEPLPS--LPSGtgveiVTYSKLLAQGRSSPqpFRPPK--PEDVATICYTSGTTGTPKGVVLTH 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 229 RNMLANLE--QVNATYGPllhrgKELVVTALPLYHIFAlTMNCLLFIELG-------GQNLLITNprDIPGL-------V 292
Cdd:PLN02736 244 GNLIANVAgsSLSTKFYP-----SDVHISYLPLAHIYE-RVNQIVMLHYGvavgfyqGDNLKLMD--DLAALrptifcsV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 293 KELAKYPFTAMT-GVNT-------LFNALLNNKE------------FQQLDFSSLHLSAGGGM--------PVQQVVAER 344
Cdd:PLN02736 316 PRLYNRIYDGITnAVKEsgglkerLFNAAYNAKKqalengknpspmWDRLVFNKIKAKLGGRVrfmssgasPLSPDVMEF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 345 WVKLTGQYLLEGYGLTECSPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDDD----NEVAPGEPGELCIKGPQVMLGYWQ 420
Cdd:PLN02736 396 LRICFGGRVLEGYGMTETSCVIS-GMDEGDNLSGHVGSPNPACEVKLVDVPEmnytSEDQPYPRGEICVRGPIIFKGYYK 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 421 RPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYPNEIEDV 473
Cdd:PLN02736 475 DEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-553 |
1.00e-40 |
|
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: 153.85 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYtPRE-LEHQLNDSGAAaIVIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdais 185
Cdd:cd05918 82 SH-PLQrLQEILQDTGAK-VVLTSS------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 186 frsalqhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQvnatYGPLLHRGKELVVTA-------LP 258
Cdd:cd05918 105 -------------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALA----HGRALGLTSESRVLQfasytfdVS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 LYHIF-ALTMNCLLFI--ELGGQNllitnprDIPGLVKELakypftamtGVNTLF-----NALLNNKefqqlDFSSLHLS 330
Cdd:cd05918 162 ILEIFtTLAAGGCLCIpsEEDRLN-------DLAGFINRL---------RVTWAFltpsvARLLDPE-----DVPSLRTL 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 331 AGGGMPVQQVVAERWVKLTGqyLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTeAKLVDDDDNE--VAPGEPGELC 408
Cdd:cd05918 221 VLGGEALTQSDVDTWADRVR--LINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDPDNHDrlVPIGAVGELL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 409 IKGPQVMLGYWQRPDATDEI-IKD-GWLH------------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:cd05918 298 IEGPILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 475 MQHSGVQEVAAVGV--PSGSSGEAVKI-FVVKKDAALTE------------------EALITFCRRHLTGYKVPKLVEFR 533
Cdd:cd05918 378 RQSLPGAKEVVVEVvkPKDGSSSPQLVaFVVLDGSSSGSgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPL 457
|
570 580
....*....|....*....|
gi 505808171 534 DELPKSNVGKILRRELRDEA 553
Cdd:cd05918 458 SHLPLTASGKIDRRALRELA 477
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-552 |
1.52e-40 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 154.52 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRElehqlndsgaaaIVIVS 129
Cdd:PRK06018 41 TYAQIHDRALKVSQALD-RDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQ------------IAWII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDKTQVKhvILTRMGDQLSTAKgtlvNFVVKYIKRLVPKYHLPDAISFRSALQhGYRMQYVKPEIVADDLA 209
Cdd:PRK06018 108 NHAEDRVVITDLTFVP--ILEKIADKLPSVE----RYVVLTDAAHMPQTTLKNAVAYEEWIA-EADGDFAWKTFDENTAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHR-NMLANLEQVNAtyGPLLHRGKELVVTALPLYHIFA--LTMNCllfiELGGQNLLITNPR 286
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHRsNVLHALMANNG--DALGTSAADTMLPVVPLFHANSwgIAFSA----PSMGTKLVMPGAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKEL---AKYPFTAmtGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLtGQYLLEGYGLTECS 363
Cdd:PRK06018 255 LDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 364 PL--VSVNPHDIDYHSGSI--------GLPVPSTEAKLVDDDDNEVA-PGE-PGELCIKGPQVMLGYWQrpdATDEII-K 430
Cdd:PRK06018 332 PLgtLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDAGKELPwDGKtFGRLKVRGPAVAAAYYR---VDGEILdD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGE-AVKIFVVKKDAALT 509
Cdd:PRK06018 409 DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErPLLIVQLKPGETAT 488
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 505808171 510 EEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06018 489 REEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
36-556 |
2.16e-40 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 155.96 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 36 YADQPAFInMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:PRK06060 19 WYDRPAFY-AADVVTHGQIHDGAARLGEVLRN-RGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 116 QLNDSgAAAIVIVSNfahtleKVVDKTQVKHVIltRMGDQLSTAKgtlvnfvvkyikRLVPKYHLPdaisfrsalqhgyr 195
Cdd:PRK06060 97 AARNT-EPALVVTSD------ALRDRFQPSRVA--EAAELMSEAA------------RVAPGGYEP-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 196 mqyvkpeIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV--NAtygpLLHRGKELVVTALPLYHIFALTMNCLLFI 273
Cdd:PRK06060 142 -------MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrKA----LRLTPEDTGLCSARMYFAYGLGNSVWFPL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 274 ELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQldFSSLHLSAGGGMPVQQVVAERWVKLTGQY- 352
Cdd:PRK06060 211 ATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDS--FRSLRCVVSAGEALELGLAERLMEFFGGIp 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 353 LLEGYGLTECSPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDA--TDEiik 430
Cdd:PRK06060 289 ILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSpvANE--- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 dGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTE 510
Cdd:PRK06060 365 -GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATID 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 505808171 511 EALITFCRR----HLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK06060 444 GSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
24-552 |
2.48e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 154.89 E-value: 2.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPA--FINM-----GEV--MTYRKLEERSRAFAAYLQQGLglQKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAyrFLDFsterdGVArdLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 95 LRAGMIAVnvnPLYTPRELEHqlndsgaaaivivsnfAHTLEKVVDKTQVKhVILTRMGdqlsTAKGtlvnfVVKYIKRL 174
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDDCTPS-AILTTTD----SAEG-----VRKFFRAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 vPKYHLPDAISFrSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV-NATYGPLLHRGkelv 253
Cdd:PRK07769 151 -PAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQViDALEGQEGDRG---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 254 VTALPLYHIFALTMncLLFIELGGQNLLITNPRDI---PG-LVKELAKYPftamTGVNTLFNALLN-----------NKE 318
Cdd:PRK07769 225 VSWLPFFHDMGLIT--VLLPALLGHYITFMSPAAFvrrPGrWIRELARKP----GGTGGTFSAAPNfafehaaarglPKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 319 FQQ-LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTECSPLVSVNPHD-------IDYHSGSIG--L 382
Cdd:PRK07769 299 GEPpLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVSTTPMDeeptviyVDRDELNAGrfV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 383 PVPSTE-----------------AKLVD-DDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIK-------------- 430
Cdd:PRK07769 379 EVPADApnavaqvsagkvgvsewAVIVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshaeg 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 ----DGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSG---VQEVAAVGVPSGSSGEAV---KIF 500
Cdd:PRK07769 459 apddALWVRTGDYGVYFD-GELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKalrTGYVAAFSVPANQLPQVVfddSHA 537
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505808171 501 VVKKDAALTEEALITFCRRHLTGYK---------------VPKLVEFRDEL-------PKSNVGKILRRELRDE 552
Cdd:PRK07769 538 GLKFDPEDTSEQLVIVAERAPGAHKldpqpiaddiraaiaVRHGVTVRDVLlvpagsiPRTSSGKIARRACRAA 611
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-555 |
5.36e-40 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 153.08 E-value: 5.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 12 DVPAeiNPDRYQSLVELF--EHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYL-QQGLGLqkGDRVALMMPNLLQYP 88
Cdd:PLN02479 9 DLPK--NAANYTALTPLWflERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALaKRSIGP--GSTVAVIAPNIPAMY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 89 VALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVV------DKTQVKHVILTRMGDQLSTAKGT 162
Cdd:PLN02479 85 EAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALkilaekKKSSFKPPLLIVIGDPTCDPKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 163 lvnfvvkyikrlvpKYHLPD-AISFRSALQHG-YRMQYVKPEIVADDLAfLQYTGGTTGVAKGAMLTHRNMLanleqVNA 240
Cdd:PLN02479 165 --------------QYALGKgAIEYEKFLETGdPEFAWKPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAY-----LMA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 TYGPLLHRGKELVVT--ALPLYHI----FALTMNCLLfielgGQNLLItnpRDIP--GLVKELAKYPFTAMTGVNTLFNA 312
Cdd:PLN02479 225 LSNALIWGMNEGAVYlwTLPMFHCngwcFTWTLAALC-----GTNICL---RQVTakAIYSAIANYGVTHFCAAPVVLNT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 313 LLNN-KEFQQLDFSSL-HLSAGGGMPVQQVVAERWVKltGQYLLEGYGLTECSPLVSVNPHDIDYHSgsigLPvPSTEAK 390
Cdd:PLN02479 297 IVNApKSETILPLPRVvHVMTAGAAPPPSVLFAMSEK--GFRVTHTYGLSETYGPSTVCAWKPEWDS----LP-PEEQAR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 391 L----------------VDDDDNEVAPGEP---GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIV 451
Cdd:PLN02479 370 LnarqgvryiglegldvVDTKTMKPVPADGktmGEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 452 DRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKK------DAALTEEALITFCRRHLTGYK 525
Cdd:PLN02479 450 DRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLPAYW 529
|
570 580 590
....*....|....*....|....*....|
gi 505808171 526 VPKLVEFrDELPKSNVGKILRRELRDEARA 555
Cdd:PLN02479 530 VPKSVVF-GPLPKTATGKIQKHVLRAKAKE 558
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-487 |
3.23e-39 |
|
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: 149.93 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVivs 129
Cdd:cd05932 8 TWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 nfahtLEKVVDKTQVKHVILTRMgdqlstakgtlvnfvvkyIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEIVADDLA 209
Cdd:cd05932 84 -----VGKLDDWKAMAPGVPEGL------------------ISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFALTmncllFIELGG--QNLLITNPRD 287
Cdd:cd05932 141 TLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGT---EENDRMLSYLPLAHVTERV-----FVEGGSlyGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 288 IPGLVKELAKYPFTAMTGVN---TLF----------------------NALLNNKEFQQLDFSSLHLSAGGGMPVQQVVA 342
Cdd:cd05932 213 LDTFVEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkipvvNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ErWVKLTGQYLLEGYGLTECSPLVSVNpHDIDYHSGSIGLPVPSTEAKLVDDddnevapgepGELCIKGPQVMLGYWQRP 422
Cdd:cd05932 293 E-WYRSLGLNILEAYGMTENFAYSHLN-YPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDP 360
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 423 DATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:cd05932 361 EATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
23-543 |
1.07e-38 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 151.02 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRY-ADQPAF--INMGEvMTYRKLEERSRAFAAYLQQGLglQKGDRVALMMPNLLQYPVALFGI----- 94
Cdd:PRK08043 204 ETLYEALLSAQYRYgAGKPCIedVNFTP-DSYRKLLKKTLFVGRILEKYS--VEGERIGLMLPNATISAAVIFGAslrrr 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 95 -------------LRAGMIAVNVNPLYTPRelehQLNDSGaaaivivsNFAHTLEKVvdkTQVKHVILTRMGDQLSTAKG 161
Cdd:PRK08043 281 ipammnytagvkgLTSAITAAEIKTIFTSR----QFLDKG--------KLWHLPEQL---TQVRWVYLEDLKDDVTTADK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 162 TLVNFvvkyiKRLVPkyhlpdaisfrsalqhgyRMQYVKPEivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN-- 239
Cdd:PRK08043 346 LWIFA-----HLLMP------------------RLAQVKQQ--PEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKti 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 240 ATYGPllhrgKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNP---RDIPGLVKELAkypFTAMTGVNTLfnaLLNN 316
Cdd:PRK08043 401 ADFTP-----NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyRIVPELVYDRN---CTVLFGTSTF---LGNY 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 317 KEFQQ-LDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVN-PhdIDYHSGSIGLPVPSTEAKLVDd 394
Cdd:PRK08043 470 ARFANpYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINvP--MAAKPGTVGRILPGMDARLLS- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 395 ddnevAPG--EPGELCIKGPQVMLGYW--------QRPDATDE--IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSG 462
Cdd:PRK08043 547 -----VPGieQGGRLQLKGPNIMNGYLrvekpgvlEVPTAENArgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAG 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 463 FNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVkkDAALTEEALITFCRRH-LTGYKVPKLVEFRDELPKSNV 541
Cdd:PRK08043 622 EMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGS 699
|
..
gi 505808171 542 GK 543
Cdd:PRK08043 700 GK 701
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
44-550 |
2.09e-38 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 149.00 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 44 NMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTP-----RE-----L 113
Cdd:PRK09192 45 QLEEALPYQTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV---PLPLPmgfggREsyiaqL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 114 EHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHViltrmgdqlstakGTLVNFvvkyikrlvpkyHLPDAIsfRSALqhg 193
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHV-------------LSHAWF------------KALPEA--DVAL--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 194 yrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYGpLLHRGKELVVTALPLYHIFALtMNCLLFI 273
Cdd:PRK09192 171 -------PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL-RAISHDG-LKVRPGDRCVSWLPFYHDMGL-VGFLLTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 274 eLGGQ---NLLITNprdipglvkELAKYPF---------TAMTGVNTLFNALL-----NNKEFQQLDFSSLHLSAGGG-- 334
Cdd:PRK09192 241 -VATQlsvDYLPTR---------DFARRPLqwldlisrnRGTISYSPPFGYELcarrvNSKDLAELDLSCWRVAGIGAdm 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 335 --MPVQQVVAERW--VKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSI---------------------------GLP 383
Cdd:PRK09192 311 irPDVLHQFAEAFapAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEVdrdrleyqgkavapgaetrrvrtfvncGKA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 384 VPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGF 463
Cdd:PRK09192 391 LPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 464 NVYPNEIEDVVMQHSGVQ--EVAAVGVPSGsSGEAVKIFV------VKKDAALTEEALITFCRRHLTGYKVpKLVEFRdE 535
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLVqcrisdEERRGQLIHALAALVRSEFGVEAAV-ELVPPH-S 546
|
570
....*....|....*
gi 505808171 536 LPKSNVGKILRRELR 550
Cdd:PRK09192 547 LPRTSSGKLSRAKAK 561
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-561 |
2.95e-38 |
|
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: 148.86 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFI------NMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:cd05966 62 HLKER-GDKVAIIwegdepDQSRTITYRELLREVCRFANVLKS-LGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVDK-----TQVKHVIltrmgdqlstakgtlvnfVVKYIKRL 174
Cdd:cd05966 140 FAGFSAESLADRINDAQCKLVITADGGyrggkVIPLKEIVDEalekcPSVEKVL------------------VVKRTGGE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 VPK-------YHlpDAISFRSAlqhgyrmqYVKPEIV-ADDLAFLQYTGGTTGVAKG-----------AMLTHRNML--- 232
Cdd:cd05966 202 VPMtegrdlwWH--DLMAKQSP--------ECEPEWMdSEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVFdyh 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 233 --------ANLEQVNA----TYGPLLHRGKELVVTALPLYHIFALTMNcllFIELGGQNLLITNPRDIPGLVKELAKYPf 300
Cdd:cd05966 272 pddiywctADIGWITGhsyiVYGPLANGATTVMFEGTPTYPDPGRYWD---IVEKHKVTIFYTAPTAIRALMKFGDEWV- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 301 tamtgvntlfnallnnkefQQLDFSSLHLSAGGGMPVQ----------------QVVAERWVKLTGQYLLegygltecSP 364
Cdd:cd05966 348 -------------------KKHDLSSLRVLGSVGEPINpeawmwyyevigkercPIVDTWWQTETGGIMI--------TP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 365 LvsvnPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGP-QVML------------GYWQR-Pdatdeiik 430
Cdd:cd05966 401 L----PGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwPGMArtiygdheryedTYFSKfP-------- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 431 dGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD----- 505
Cdd:cd05966 469 -GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeeps 547
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 506 AALTEEaLITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEArAKVDNKG 561
Cdd:cd05966 548 DELRKE-LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA-AGEEELG 601
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-549 |
3.29e-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: 145.86 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVivsnfahtlekvvdkTQvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmq 197
Cdd:cd17652 81 ADARPALLL---------------TT------------------------------------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHRGKELVVTALPlyhiFALTMNCLLFIELGG 277
Cdd:cd17652 92 -------PDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPS----FDASVWELLMALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 QNLLITNPRDI---PGLVKELAKYPFTAMTGVNTLFNALlnnKEFQQLDFSSLhLSAGGGMPVQqvVAERWVKltGQYLL 354
Cdd:cd17652 160 ATLVLAPAEELlpgEPLADLLREHRITHVTLPPAALAAL---PPDDLPDLRTL-VVAGEACPAE--LVDRWAP--GRRMI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKD-- 431
Cdd:cd17652 232 NAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErFVADpf 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 432 ----GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVGVPSGSSGEA--VKIFVVKK 504
Cdd:cd17652 312 gapgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKrlVAYVVPAP 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 505808171 505 DAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17652 391 GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
31-556 |
3.63e-38 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 148.62 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRYADQPAFI------NMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:cd05967 59 HVEAGRGDQIALIydspvtGTERTYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDSGAAaIVIVSNFAHTLEKVV------DK------TQVKHVILTRMGDqlstakgtlvnfvvkyiK 172
Cdd:cd05967 138 FGGFAAKELASRIDDAKPK-LIVTASCGIEPGKVVpykpllDKalelsgHKPHHVLVLNRPQ-----------------V 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 173 RLVPKYHLPDaISFRSALQHGYRMQYVKpeIVADDLAFLQYTGGTTGVAKG--------AMLTHRNMlANLEQVNA---- 240
Cdd:cd05967 200 PADLTKPGRD-LDWSELLAKAEPVDCVP--VAATDPLYILYTSGTTGKPKGvvrdngghAVALNWSM-RNIYGIKPgdvw 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 ---------------TYGPLLHRGKELVVTALPLYHifaltmncllfielggqnllitnPrDIPGLVKELAKYPFTAMTG 305
Cdd:cd05967 276 waasdvgwvvghsyiVYGPLLHGATTVLYEGKPVGT-----------------------P-DPGAFWRVIEKYQVNALFT 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 306 VNTLFNAL----LNNKEFQQLDFSSL-HLSAGGgmpvqqvvaER-------WV-KLTGQYLLEGYGLTECSPLVSVNPHD 372
Cdd:cd05967 332 APTAIRAIrkedPDGKYIKKYDLSSLrTLFLAG---------ERldpptleWAeNTLGVPVIDHWWQTETGWPITANPVG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 373 IDYHS---GSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGP---QVMLGYWQRPDATDEII---KDGWLHTGDIAVMD 443
Cdd:cd05967 403 LEPLPikaGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYlskFPGYYDTGDAGYKD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-----KKDAALTEEALITFCR 518
Cdd:cd05967 483 EDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVlkegvKITAEELEKELVALVR 562
|
570 580 590
....*....|....*....|....*....|....*...
gi 505808171 519 RHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:cd05967 563 EQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADGE 600
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
47-474 |
9.70e-38 |
|
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: 147.12 E-value: 9.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFA-AYLQqgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSgAAAI 125
Cdd:cd05933 7 HTLTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNfAHTLEKVvdkTQVKhviltrmgDQLSTAKGtlvnfVVKYikRLVPKYHLPDAISFRSALQHGY---------RM 196
Cdd:cd05933 84 LVVEN-QKQLQKI---LQIQ--------DKLPHLKA-----IIQY--KEPLKEKEPNLYSWDEFMELGRsipdeqldaII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 197 QYVKPeivaDDLAFLQYTGGTTGVAKGAMLTHRNML-------ANLEQVNATygpllhRGKELVVTALPLYHIFALTMNC 269
Cdd:cd05933 145 SSQKP----NQCCTLIYTSGTTGMPKGVMLSHDNITwtakaasQHMDLRPAT------VGQESVVSYLPLSHIAAQILDI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 270 LLFIELGGQnLLITNPRDIPG-LVKELAKYPFTAMTGV------------------------------------------ 306
Cdd:cd05933 215 WLPIKVGGQ-VYFAQPDALKGtLVKTLREVRPTAFMGVprvwekiqekmkavgaksgtlkrkiaswakgvgletnlklmg 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 307 --------NTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQyLLEGYGLTECSPLVSVNpHDIDYHSG 378
Cdd:cd05933 294 gespsplfYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIP-IMELYGMSETSGPHTIS-NPQAYRLL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 379 SIGLPVPSTEAKLVDDDDNEVapgepGELCIKGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDM 457
Cdd:cd05933 372 SCGKALPGCKTKIHNPDADGI-----GEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKEL 446
|
490
....*....|....*...
gi 505808171 458 ILVS-GFNVYPNEIEDVV 474
Cdd:cd05933 447 IITAgGENVPPVPIEDAV 464
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
49-458 |
2.82e-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: 144.67 E-value: 2.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVnplY-TPRE--LEHQLNDSGAAAI 125
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVE-LGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV---YaTLGEdaLIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivA 205
Cdd:cd17639 82 FTDGK--------------------------------------------------------------------------P 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRgKELVVTALPLYHIFALTM-NCLLFIelGG------- 277
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAeNVCLYR--GGtigygsp 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 QNLLITNPRDIPGLVKELAkyPfTAMTGV----------------------NTLFNALLNNKEFQQLD-----------F 324
Cdd:cd17639 165 RTLTDKSKRGCKGDLTEFK--P-TLMVGVpaiwdtirkgvlaklnpmgglkRTLFWTAYQSKLKALKEgpgtplldelvF 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 325 SSLH----------LSAGGGMPVQqvvAERWVKLTGQYLLEGYGLTE-CSPLVSVNPHDIDYhsGSIGLPVPSTEAKLVD 393
Cdd:cd17639 242 KKVRaalggrlrymLSGGAPLSAD---TQEFLNIVLCPVIQGYGLTEtCAGGTVQDPGDLET--GRVGPPLPCCEIKLVD 316
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 394 DDD---NEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMI 458
Cdd:cd17639 317 WEEggySTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
27-549 |
3.47e-37 |
|
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: 143.08 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDSGAAaiVIVSNfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd17645 81 DYPGERIAYMLADSSAK--ILLTN-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsalqhgyrmqyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHRGKELVVTALPlYHIFALT 266
Cdd:cd17645 103 ------------------PDDLAYVIYTSGSTGLPKGVMIEHHN-LVNLCEWHRPYFGVTPADKSLVYASFS-FDASAWE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 267 MNCLLFIelgGQNLLITnPRDIPGLVKELAKYPFTamTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAErwv 346
Cdd:cd17645 163 IFPHLTA---GAALHVV-PSERRLDLDALNDYFNQ--EGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK--- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 kltGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAkLVDDDDNEVAP-GEPGELCIKGPQVMLGYWQRPDAT 425
Cdd:cd17645 234 ---GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRV-YILDEALQLQPiGVAGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 426 DE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVK 498
Cdd:cd17645 310 AEkFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 505808171 499 IFVVKKDAAlTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17645 390 AYVTAPEEI-PHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
47-552 |
5.44e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 143.78 E-value: 5.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNplytprelehqlndsgaaaiv 126
Cdd:cd05908 14 KFVSYRHLREEALGYLGALQE-LGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS--------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 127 IVSNFAHTLEkvvdktqvkhviltrmgdqlstakgtlvnfVVKYIKRLVPKYHLPDAisfrsalqhgyrmqyVKPEIVAD 206
Cdd:cd05908 72 IGSNEEHKLK------------------------------LNKVWNTLKNPYLITEE---------------EVLCELAD 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygpLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITNPR 286
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNS---TEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DI--PGL-VKELAKYPFTAMTGVN---TLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY------LL 354
Cdd:cd05908 184 FIrrPILwLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYglkrnaIL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 355 EGYGLTECSPLVSVNPHDIDY------HSG---------------------SIGLPVPSTEAKLVDDDDNEVAPGEPGEL 407
Cdd:cd05908 264 PVYGLAEASVGASLPKAQSPFktitlgRRHvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 408 CIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQ--EVA 484
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVV 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 485 AVGV-PSGSSGEAVKIFVVKKDAALTEEALITFCRRHL---TGYKVPKLVEFRdELPKSNVGKILRRELRDE 552
Cdd:cd05908 423 ACGVnNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLnkrGGWQINEVLPIR-RIPKTTSGKVKRYELAQR 493
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
38-545 |
9.94e-37 |
|
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: 144.26 E-value: 9.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGE------VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPR 111
Cdd:cd17634 68 DRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 112 ELEHQLNDSGAAAIVIVSNFAH-----TLEKVVDK------TQVKHVI-LTRMGDQLSTAKGTLVNfvvkyikrlvpkYH 179
Cdd:cd17634 147 AVAGRIIDSSSRLLITADGGVRagrsvPLKKNVDDalnpnvTSVEHVIvLKRTGSDIDWQEGRDLW------------WR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 180 lpDAISFRSALQHGYRMQyvkpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA------------------- 240
Cdd:cd17634 215 --DLIAKASPEHQPEAMN-------AEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKyvfdygpgdiywctadvgw 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 241 -------TYGPLLHRGKELVVTALPLYHIFALTMNcllFIELGGQNLLITNPRDIPGLVKElakypftamtgvntlfnal 313
Cdd:cd17634 286 vtghsylLYGPLACGATTLLYEGVPNWPTPARMWQ---VVDKHGVNILYTAPTAIRALMAA------------------- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 314 lNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY---LLEGYGLTECS-PLVSVNPHDIDYHSGSIGLPVPSTEA 389
Cdd:cd17634 344 -GDDAIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAIELKAGSATRPVFGVQP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 390 KLVDDDDNEVAPGEPGELCIKG--PQVMLGYWQRPDATDEIIK---DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFN 464
Cdd:cd17634 423 AVVDNEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 465 VYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKK----DAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSN 540
Cdd:cd17634 503 LGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTR 582
|
....*
gi 505808171 541 VGKIL 545
Cdd:cd17634 583 SGKIM 587
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
47-548 |
7.96e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 141.23 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFAAYLQQgLGlQKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPRELEHQ------LNDS 120
Cdd:PRK05850 34 ETLTWSQLYRRTLNVAEELRR-HG-STGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVPQGGAHDervsavLRDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 121 GAAaivivsnfahtlekvvdktqvkhVILTRmgdqlSTAKGTLVNFVVKYIKRLVPKYHLPDAISFRSALqhgyrmqyvK 200
Cdd:PRK05850 109 SPS-----------------------VVLTT-----SAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPR---------G 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 201 PEIVADDL---AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpLLHRGKEL-----VVTALPLYHIFALTMNCLLF 272
Cdd:PRK05850 152 SDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY--FGDTGGVPppdttVVSWLPFYHDMGLVLGVCAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 273 IeLGGQNLLITNP--------RdipgLVKELAKYP--FTA-----------------MTGvntlfnallnnkefqqLDFS 325
Cdd:PRK05850 230 I-LGGCPAVLTSPvaflqrpaR----WMQLLASNPhaFSAapnfafelavrktsdddMAG----------------LDLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 326 SLHLSAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTEC----------SPLVSVnphDIDYHSGSIGLPVP---- 385
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRetairpSYGLAEAtvyvatrepgQPPESV---RFDYEKLSAGHAKRcetg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 386 ------------STEAKLVDDDDN-EVAPGEPGELCIKGPQVMLGYWQRPDATDEI-----------IKDG-WLHTGDIA 440
Cdd:PRK05850 366 ggtplvsygsprSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTfgatlvdpspgTPEGpWLRTGDLG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 441 VMDDeGFLRIVDRKKDMILVSGFNVYPNEIEdvvmqhSGVQE-----VAAVGVPSGSSGEAVKIFVVKKDAALTEEALIT 515
Cdd:PRK05850 446 FISE-GELFIVGRIKDLLIVDGRNHYPDDIE------ATIQEitggrVAAISVPDDGTEKLVAIIELKKRGDSDEEAMDR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 505808171 516 FC--RRHLT-------GYKVPKLVEF-RDELPKSNVGKILRRE 548
Cdd:PRK05850 519 LRtvKREVTsaiskshGLSVADLVLVaPGSIPITTSGKIRRAA 561
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
20-550 |
2.49e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 139.92 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 20 DRYQSLVELFEHATTRYADQPAFINMG---EVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGIlr 96
Cdd:PRK05620 7 DVPLSLTRILEYGSTVHGDTTVTTWGGaeqEQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 97 AGMIAVnVNPL---YTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKT-QVKHVILTRMGDQLSTAKgtlvnfvvkyik 172
Cdd:PRK05620 85 ACMGAV-FNPLnkqLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKECpCVRAVVFIGPSDADSAAA------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 173 rlvpkyHLPDAISFRS--ALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGk 250
Cdd:PRK05620 152 ------HMPEGIKVYSyeALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHG- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 251 ELVVTALPLYHIFALTMNCLLFieLGGQNLLITNPRDIPglvKELAKYPFTAMT----GVNTLFNALLNNKEFQQLDFSS 326
Cdd:PRK05620 225 ESFLCCVPIYHVLSWGVPLAAF--MSGTPLVFPGPDLSA---PTLAKIIATAMPrvahGVPTLWIQLMVHYLKNPPERMS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 327 LHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPL--VSVNPHDID------YHSGSIGLPVpSTEAKLVDD---- 394
Cdd:PRK05620 300 LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVgtVARPPSGVSgearwaYRVSQGRFPA-SLEYRIVNDgqvm 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 395 ---DDNEvapgepGELCIKGPQVMLGYWQRP-----------------DATDEIIKDGWLHTGDIAVMDDEGFLRIVDRK 454
Cdd:PRK05620 379 estDRNE------GEIQVRGNWVTASYYHSPteegggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 455 KDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD----AALTEEALITFCRRHLTGYKVPKLV 530
Cdd:PRK05620 453 RDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPgiepTRETAERLRDQLRDRLPNWMLPEYW 532
|
570 580
....*....|....*....|
gi 505808171 531 EFRDELPKSNVGKILRRELR 550
Cdd:PRK05620 533 TFVDEIDKTSVGKFDKKDLR 552
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-549 |
3.18e-35 |
|
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: 138.38 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVivsnfahtlekvvdkTQVKHViltrmgDQLSTAKGTlvnfvvkyikrlvpkyHLP--DAISFRSAlqhgyr 195
Cdd:cd17656 82 LDSGVRVVL---------------TQRHLK------SKLSFNKST----------------ILLedPSISQEDT------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 196 mQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMlANLEQVNATYGPLLHRGKELVVTALPL---YH-IFAltmnCLL 271
Cdd:cd17656 119 -SNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM-VNLLHFEREKTNINFSDKVLQFATCSFdvcYQeIFS----TLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 272 FielGGQNLLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSL-HLSAGGGM-----PVQQVVAE 343
Cdd:cd17656 193 S---GGTLYIIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVkHIITAGEQlvitnEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWVKLTGQYlleGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPD 423
Cdd:cd17656 270 HNVHLHNHY---GPSETHVVTTYTINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 424 AT-DEIIKDGW------LHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVGVPSGSSGEA 496
Cdd:cd17656 347 LTaEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEK 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 505808171 497 VKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17656 426 YLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
17-553 |
3.42e-35 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 139.62 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 17 INPDRYQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAA-RGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 97 AGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLsTAKGTLVNfvvkyikrlvp 176
Cdd:PRK08279 110 LGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTL-DDPEGYED----------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 177 kyhLPDAISFRSALQHGYRmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPLLH-RGKELVVT 255
Cdd:PRK08279 178 ---LAAAAAGAPTTNPASR-----SGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAM----GGFGGLLRlTPDDVLYC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 256 ALPLYHIFALT--MNCLLfieLGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGG 333
Cdd:PRK08279 246 CLPLYHNTGGTvaWSSVL---AAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPvqqvvAERWVKLTGQY----LLEGYGLTEC----------------SPLVSVNPHDI---DYHSGSiglPVPSTEAK 390
Cdd:PRK08279 323 GLR-----PDIWDEFQQRFgiprILEFYAASEGnvgfinvfnfdgtvgrVPLWLAHPYAIvkyDVDTGE---PVRDADGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 391 LVddddnEVAPGEPGELC--IKGPQVMLGYWQrPDATDE-IIKDG------WLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PRK08279 395 CI-----KVKPGEVGLLIgrITDRGPFDGYTD-PEASEKkILRDVfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 462 GFNVYPNEIEDVVMQHSGVQEVAAVGVP-SGSSGEA--VKIfVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPK 538
Cdd:PRK08279 469 GENVATTEVENALSGFPGVEEAVVYGVEvPGTDGRAgmAAI-VLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELET 547
|
570
....*....|....*
gi 505808171 539 SNVGKILRRELRDEA 553
Cdd:PRK08279 548 TGTFKYRKVDLRKEG 562
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-543 |
5.42e-35 |
|
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: 135.20 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 205 ADDLaFLQYTGGTTGVAKGAMLTH---RNML---ANLEQVNATYGPLLHRGKE-----LVVTALPLYHifALTMNCLLFI 273
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQediFRMLmggADFGTGEFTPSEDAHKAAAaaagtVMFPAPPLMH--GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 274 ELGGQNLLITNPR-DIPGLVKELAKYPFTAMTGVNT-----LFNALLNNKEFqqlDFSSLHLSAGGGMPVQQVVAERWVK 347
Cdd:cd05924 80 LLGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVGDamarpLIDALRDAGPY---DLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 348 LTGQ-YLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTeaKLVDDDDNEVAPGEPGELCI--KGpQVMLGYWQRPDA 424
Cdd:cd05924 157 LVPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPPGSGGVGWIarRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 425 TDEIIK--DG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVkIF 500
Cdd:cd05924 234 TAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV-VA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 505808171 501 VVKKD--AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:cd05924 313 VVQLRegAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-549 |
6.42e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 137.99 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLI-AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYtPRE-LEHQLNDSGAAAIVIVSnfaHTLEKVVDKTQVKHVILTRMGDQLSTAKGtlvnfvvkyikrlvpkyHLP 181
Cdd:PRK12467 591 PLDPEY-PQDrLAYMLDDSGVRLLLTQS---HLLAQLPVPAGLRSLCLDEPADLLCGYSG-----------------HNP 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 182 DaisfrsalqhgyrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHRGKELVVTalPLYH 261
Cdd:PRK12467 650 E------------------VALDPDNLAYVIYTSGSTGQPKGVAISHGA-LANYVCVIAERLQLAADDSMLMVS--TFAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 262 IFALTMnclLFIELG-GQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLdfSSLHLSAGGGMPV 337
Cdd:PRK12467 709 DLGVTE---LFGALAsGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQRALVCGGEAL 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 338 QQVVAERWVKLT-GQYLLEGYGLTECSPLVSVNP---HDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQ 413
Cdd:PRK12467 784 QVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAG 863
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 414 VMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAA 485
Cdd:PRK12467 864 LARGYHRRPALTAErFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE-AV 942
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 486 VGVPSGSSGEAVKIFVVKKDAA------LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12467 943 VLAQPGDAGLQLVAYLVPAAVAdgaehqATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
49-515 |
8.14e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 135.03 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAiVIV 128
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDA-FIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 SNFAHTLEKVV--DKTQVKHVILTrmGDQLSTAKGTLVNFVvkyikrlvpkyhlpdaisfRSALQHGYRMQYVKPeivaD 206
Cdd:PRK09274 120 IPKAHLARRLFgwGKPSVRRLVTV--GGRLLWGGTTLATLL-------------------RDGAAAPFPMADLAP----D 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFALTmncllfieLGGQNLL----- 281
Cdd:PRK09274 175 DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYG---IEPGEIDLPTFPLFALFGPA--------LGMTSVIpdmdp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 282 ---IT-NPRDIpglVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKL--TGQYLLE 355
Cdd:PRK09274 244 trpATvDPAKL---FAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlpPDAEILT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 356 GYGLTECSPLVSVNPHDI--------DYHSGS-IGLPVPSTEAKLVD---------DDDNEVAPGEPGELCIKGPQVMLG 417
Cdd:PRK09274 321 PYGATEALPISSIESREIlfatraatDNGAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 418 YWQRPDATDEI-IKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGS 492
Cdd:PRK09274 401 YYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVPG 480
|
490 500
....*....|....*....|...
gi 505808171 493 SGEAVKIFVVKKDAALTEEALIT 515
Cdd:PRK09274 481 AQRPVLCVELEPGVACSKSALYQ 503
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
200-561 |
1.21e-33 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 134.75 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 200 KPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLA--------NLEQVNATYGpllhrgkELVVTALPLYHIFAL--TMNC 269
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilqkeGLNWVTWVVG-------ETTYSPLPATHIGGLwwILTC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 270 LLFielGGqnLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpvQQVVAE--RWVK 347
Cdd:PRK05857 236 LMH---GG--LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAAdvRFIE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 348 LTGQYLLEGYGLTE------CSPLVSVNPHDIDyhSGSIGLPVPSTEAKLVDDD--DNEVAPGEP----GELCIKGPQVM 415
Cdd:PRK05857 308 ATGVRTAQVYGLSEtgctalCLPTDDGSIVKIE--AGAVGRPYPGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANM 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 416 LGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGE 495
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 496 AVKIFVVKKdAALTEEALITFCRRHLTGYK-------VPKLVEFRDELPKSNVGKILRRELR---DEARAKVDNKG 561
Cdd:PRK05857 466 LVGLAVVAS-AELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASLAaaaTADKARVVVRG 540
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-550 |
1.95e-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: 132.49 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAaaivivsnfahtlekvvdktqvkHVILTRMGDQLstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmq 197
Cdd:cd17649 81 EDSGA-----------------------GLLLTHHPRQL----------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivaddlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHRGKELvvtaLPLYHI-FALTMNCLLFIELG 276
Cdd:cd17649 97 -----------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG--LTPGDRE----LQFASFnFDGAHEQLLPPLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 277 GQNLLI------TNPRDIPGLVKELakypftamtGVNT-------LFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAE 343
Cdd:cd17649 160 GACVVLrpdelwASADELAEMVREL---------GVTVldlppayLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLR 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 344 RWVKlTGQYLLEGYGLTEC--SPLVSVNPHDIDYHSGS--IGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYW 419
Cdd:cd17649 231 RWLK-APVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 420 QRPDATDE-IIKDG-------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSG 491
Cdd:cd17649 310 GRPELTAErFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 492 SSGEAVKIFVVKKDAALTE--EALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17649 390 GGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
47-457 |
2.23e-33 |
|
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: 134.09 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 47 EVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLlqyPVALFGILRAGMIAVNVNPLYT---PRELEHQLNDSGAA 123
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 124 AIVivsnfahtlekVVDKTQVKHVIltRMGDQLStakgtLVNFVVKYIKRLVPKYHLPDAISFRSALQHGYRMQYVKPEI 203
Cdd:cd17641 86 VVI-----------AEDEEQVDKLL--EIADRIP-----SVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 204 V--------ADDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYGPLlHRGKElVVTALPL----YHIFALTM---- 267
Cdd:cd17641 148 YerevaagkGEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPL-GPGDE-YVSVLPLpwigEQMYSVGQalvc 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 268 -NCLLFIELG----------GQNLLITNPRDIPGLVKEL-------------------------------AKYPFTAMTG 305
Cdd:cd17641 225 gFIVNFPEEPetmmedlreiGPTFVLLPPRVWEGIAADVrarmmdatpfkrfmfelgmklglraldrgkrGRPVSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 306 VNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAeRWVKLTGQYLLEGYGLTECSPLVSVNP-HDIDYHSgsIGLPV 384
Cdd:cd17641 305 ASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRdGDVDPDT--VGVPF 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505808171 385 PSTEAKLVddddnevapgEPGELCIKGPQVMLGYWQRPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDM 457
Cdd:cd17641 382 PGTEVRID----------EVGEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
34-557 |
2.49e-33 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 133.58 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 34 TRYA--DQPAFINMGEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGILRAGMiaVNVNPLYTPR 111
Cdd:PRK10946 32 TRHAasDAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 112 ELEhqLN---DSGAAAIVIVSNfAHTLekVVDKtqvkhviltRMGDQLSTAKGTLvnfvvkyikRLVPKYHLPDAISFRS 188
Cdd:PRK10946 109 RSE--LNayaSQIEPALLIADR-QHAL--FSDD---------DFLNTLVAEHSSL---------RVVLLLNDDGEHSLDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 189 ALQHGyRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNmlanleqvnatYGPLLHRGKEL--------VVTALPLY 260
Cdd:PRK10946 166 AINHP-AEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHND-----------YYYSVRRSVEIcgftpqtrYLCALPAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 261 HIFALTM-NCLLFIELGGQNLLITNPRdiPGLVKEL-AKYPFTaMT-----GVNTLFNALLNNKEFQQLdfSSLHLSAGG 333
Cdd:PRK10946 234 HNYPMSSpGALGVFLAGGTVVLAPDPS--ATLCFPLiEKHQVN-VTalvppAVSLWLQAIAEGGSRAQL--ASLKLLQVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 334 GMPVQQVVAERWVKLTGQYLLEGYGLTEcsPLVSV----NPHDIDYHSGsiGLPV-PSTEAKLVDDDDNEVAPGEPGELC 408
Cdd:PRK10946 309 GARLSETLARRIPAELGCQLQQVFGMAE--GLVNYtrldDSDERIFTTQ--GRPMsPDDEVWVADADGNPLPQGEVGRLM 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 409 IKGPQVMLGYWQRPD----ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVA 484
Cdd:PRK10946 385 TRGPYTFRGYYKSPQhnasAFDA---NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 485 AVGVPSGSSGEAVKIFVVKKDaALTEEALitfcRRHLTG-----YKVPKLVEFRDELPKSNVGKILRRELRDEARAKV 557
Cdd:PRK10946 462 LVSMEDELMGEKSCAFLVVKE-PLKAVQL----RRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
24-552 |
4.42e-33 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 133.71 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAF-------INMGEV--MTYRKLEERSRAFAAYLQQGLglQKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYryldhshSAAGCAveLTWTQLGVRLRAVGARLQQVA--GPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 95 LRAGMIAVnvnPLYTPRELEHqlndsgaaaivivsnfAHTLEKVVDKTQvKHVILTRmgdqlSTAKGTLVNFVVKYIKRL 174
Cdd:PRK12476 113 IKAGTIAV---PLFAPELPGH----------------AERLDTALRDAE-PTVVLTT-----TAAAEAVEGFLRNLPRLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 VPKYHLPDAISFRSAlqhgyrMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKElVV 254
Cdd:PRK12476 168 RPRVIAIDAIPDSAG------ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSID-LLDRNTH-GV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 255 TALPLYHIFALTMncLLFIELGGQNLLITNP----RDIPGLVKELAK---------------YPFTAMTGVNtlfnalln 315
Cdd:PRK12476 240 SWLPLYHDMGLSM--IGFPAVYGGHSTLMSPtafvRRPQRWIKALSEgsrtgrvvtaapnfaYEWAAQRGLP-------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 316 nKEFQQLDFSSLHLsAGGGMPVQQVVAERWVKLTGQYLLE------GYGLTECSPLVSVNPHD-------IDYH---SG- 378
Cdd:PRK12476 310 -AEGDDIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPrtafkpSYGIAEATLFVATIAPDaepsvvyLDREqlgAGr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 379 ---------------SIGLPVPSTEAKLVDDD-DNEVAPGEPGELCIKGPQVMLGYWQRPDATDEI-------------- 428
Cdd:PRK12476 388 avrvaadapnavahvSCGQVARSQWAVIVDPDtGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsrlaegsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 429 -----IKDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQE---VAAVGVPSGSSGEAVKIF 500
Cdd:PRK12476 468 adgaaDDGTWLRTGDLGVYLD-GELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAEDNERLVIVA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 501 -----VVKKDAALTEEAL-ITFCRRHLTGYKVPKLVEfRDELPKSNVGKILRRELRDE 552
Cdd:PRK12476 547 eraagTSRADPAPAIDAIrAAVSRRHGLAVADVRLVP-AGAIPRTTSGKLARRACRAQ 603
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
5.37e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.47 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 7 NRYPADVPAEinpdryQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYL-QQGLGLQKgdRVALMMPNLL 85
Cdd:PRK12316 4541 NRTDAGYPAT------RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALiARGVGPEV--LVGIAMERSA 4612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 86 QYPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDSGAAAIVivsnfahtlekvvdkTQvkhvilTRMGDQLSTAKGTlv 164
Cdd:PRK12316 4613 EMMVGLLAVLKAGGAYVPLDPEY-PRErLAYMMEDSGAALLL---------------TQ------SHLLQRLPIPDGL-- 4668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 165 nfvvkyikrlvpkyhlpDAISF-RSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG 243
Cdd:PRK12316 4669 -----------------ASLALdRDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE 4731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 244 pLLHRGKELVVTALPlyhiFALTMNCLLFIELGGQNLLITNPR--DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEfQQ 321
Cdd:PRK12316 4732 -LTPDDRVLQFMSFS----FDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RD 4805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 322 LDFSSLHLSAGGGMPVQQVVAER-WVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDDD 396
Cdd:PRK12316 4806 GEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQL 4885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 NEVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPN 468
Cdd:PRK12316 4886 NPLPVGVAGELYLGGEGVARGYLERPALTAErFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELG 4965
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 469 EIEDVVMQHSGVQEVAAVGVPsGSSGEAVKIFVVKKDAALTE---------EALITFCRRHLTGYKVPKLVEFRDELPKS 539
Cdd:PRK12316 4966 EIEARLREHPAVREAVVIAQE-GAVGKQLVGYVVPQDPALADadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLT 5044
|
570
....*....|
gi 505808171 540 NVGKILRREL 549
Cdd:PRK12316 5045 PNGKLDRKAL 5054
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-549 |
7.58e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 134.70 E-value: 7.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK12316 512 GVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 104 VNPLYTPRELEHQLNDSGAAAIVivsnfahtlekvvdkTQvkhvilTRMGDQLSTAKGtlvnfvvkyIKRLVpkyhLPDA 183
Cdd:PRK12316 591 LDPEYPAERLAYMLEDSGVQLLL---------------SQ------SHLGRKLPLAAG---------VQVLD----LDRP 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 184 ISFRSalqhGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRG---KELVVTALPLY 260
Cdd:PRK12316 637 AAWLE----GYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTvlqKTPFSFDVSVW 712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 261 HIFALTMNcllfielgGQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMP- 336
Cdd:PRK12316 713 EFFWPLMS--------GARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPa 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 337 --VQQVVAERWVklTGQYLLegYGLTECSPLVSvnpHDIDYHSG----SIGLPVPSTEAKLVDDDDNEVAPGEPGELCIK 410
Cdd:PRK12316 785 daQEQVFAKLPQ--AGLYNL--YGPTEAAIDVT---HWTCVEEGgdsvPIGRPIANLACYILDANLEPVPVGVLGELYLA 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 411 GPQVMLGYWQRPDATDE-----IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEv 483
Cdd:PRK12316 858 GRGLARGYHGRPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE- 936
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 484 AAVGVPSGSsgEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 937 AAVLAVDGK--QLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-550 |
3.80e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 132.60 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQGLGLqkGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPREL--EHQ------L 117
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESArrHHQerllsiI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIVSNFAHTLEKVvdktqvkhviltrmgDQLSTAKgtlvnfvvkyikrlVPKYHLPDAISfrSALQHGYRmq 197
Cdd:PRK05691 113 ADAEPRLLLTVADLRDSLLQM---------------EELAAAN--------------APELLCVDTLD--PALAEAWQ-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHrGKELVVTALPLYHIFALTMNCLLFIELGG 277
Cdd:PRK05691 160 --EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN-PDDVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 QNLLITnprdiPGL--------VKELAKYPFTAMTGVN---TLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWV 346
Cdd:PRK05691 237 PCVLMS-----PAYflerplrwLEAISEYGGTISGGPDfayRLCSERVSESALERLDLSRWRVAYSGSEPIRQDSLERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 347 K------LTGQYLLEGYGLTECSPLVSVNPH-------DIDYHS----------GSI----GLPVPSTEAKLVDDDDNEV 399
Cdd:PRK05691 312 EkfaacgFDPDSFFASYGLAEATLFVSGGRRgqgipalELDAEAlarnraepgtGSVlmscGRSQPGHAVLIVDPQSLEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 400 AP-GEPGELCIKGPQVMLGYWQRPDATDEII--KDG--WLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:PRK05691 392 LGdNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 475 MQHSGV---QEVAAVGVP-SGSSGEAVKIFVVKK-DAALTEEALITFCRRHLTG--YKVPKLVEFRD--ELPKSNVGKIL 545
Cdd:PRK05691 471 EREVEVvrkGRVAAFAVNhQGEEGIGIAAEISRSvQKILPPQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQ 550
|
....*
gi 505808171 546 RRELR 550
Cdd:PRK05691 551 RSACR 555
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-553 |
9.10e-32 |
|
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: 127.96 E-value: 9.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIViv 128
Cdd:cd05910 3 LSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 snfahtlekvvdktqvkhviltrmgdqlstakGtlvnfvvkyikrlVPKyhlpdaisfrsalqhgyrmqyvkpeivADDL 208
Cdd:cd05910 80 --------------------------------G-------------IPK---------------------------ADEP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhRGKELVVTALPLYHIFALTMNCLLFI-ELGGQNLLITNPRD 287
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGI---RPGEVDLATFPLFALFGPALGLTSVIpDMDPTRPARADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 288 ipgLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLH--LSAGGgmPVQQVVAERWVKLT--GQYLLEGYGLTECS 363
Cdd:cd05910 165 ---LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGA--PVPIALAARLRKMLsdEAEILTPYGATEAL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 364 PLVSVNPHDI--------DYHSGS-IGLPVPSTEAKLVD---------DDDNEVAPGEPGELCIKGPQVMLGYWQRPDAT 425
Cdd:cd05910 240 PVSSIGSRELlatttaatSGGAGTcVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 426 D-EIIKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVpsGSSGEAVKIF 500
Cdd:cd05910 320 AlAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQLPVL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 501 VVK------KDAALTEEALITFCRRHLTGYKVPKLVeFRDELP---KSNvGKILRRELRDEA 553
Cdd:cd05910 398 CVEplpgtiTPRARLEQELRALAKDYPHTQRIGRFL-IHPSFPvdiRHN-AKIFREKLAVWA 457
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-549 |
2.21e-31 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 129.78 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVDKTqvkhviltrmgdqlstakgtlvnfvvkyikrlVPKYHLPD 182
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLT--------------------------------SLCYNAPL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 AISFRSALQHGyrmqyvKPeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLlhRGKELVVTALP---- 258
Cdd:PRK10252 585 APQGAAPLQLS------QP----HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY-PL--TADDVVLQKTPcsfd 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 --LYHIFaltmncLLFIelGGQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLS--- 330
Cdd:PRK10252 652 vsVWEFF------WPFI--AGAKLVMAEPeahRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRqvf 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 331 -AGGGMPVQQVvaERWVKLTGQYLLEGYGLTECSPLVSVNP---HDIDYHSGS---IGLPVPSTEAKLVDDDDNEVAPGE 403
Cdd:PRK10252 724 cSGEALPADLC--REWQQLTGAPLHNLYGPTEAAVDVSWYPafgEELAAVRGSsvpIGYPVWNTGLRILDARMRPVPPGV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 404 PGELCIKGPQVMLGYWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK10252 802 AGDLYLTGIQLAQGYLGRPDLTASrFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQA 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 477 HSGVQEVAAVGV-------PSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK10252 882 LPDVEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-549 |
2.95e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 125.53 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 211 LQYTGGTTGVAKgamlTHRNMLANLEQVNATYGPLLHRGKELV-VTALPLYHIFALTMNCLLFIELGGQNLLIT--NPRD 287
Cdd:PRK08308 106 LQYSSGTTGEPK----LIRRSWTEIDREIEAYNEALNCEQDETpIVACPVTHSYGLICGVLAALTRGSKPVIITnkNPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 288 IpglVKELAKYPFTAMTGVNTLFNAL--LNNKEFQqldFSSLHLSaGGGMPvqqvvaERW---VKLTGQYLLEGYGLTE- 361
Cdd:PRK08308 182 A---LNILRNTPQHILYAVPLMLHILgrLLPGTFQ---FHAVMTS-GTPLP------EAWfykLRERTTYMMQQYGCSEa 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 362 -CsplVSVNPHDIDyhSGSIGLPVPSTEAKLVDDDDNevapgePGELCIKgpqvmlgywqrpdatdeiIKDGWLHTGDIA 440
Cdd:PRK08308 249 gC---VSICPDMKS--HLDLGNPLPHVSVSAGSDENA------PEEIVVK------------------MGDKEIFTKDLG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 441 VMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEaLITFCRRH 520
Cdd:PRK08308 300 YKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQ-LREWCIQH 378
|
330 340
....*....|....*....|....*....
gi 505808171 521 LTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK08308 379 LAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
201-548 |
5.64e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 126.65 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 201 PEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ--VNATYGPllhrGKELVVTALPLYH------IFALTMNCllf 272
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAmfVAAEFDV----ETDVMVSWLPLFHdmgmvgFLTVPMYF--- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 273 ielGGQNLLITnPRDI---PGLVKEL-AKYPFTAMTGVN---TLFNALLNNK-EFQQLDFSSLHLSAGGGMPVQQVVAER 344
Cdd:PRK07768 220 ---GAELVKVT-PMDFlrdPLLWAELiSKYRGTMTAAPNfayALLARRLRRQaKPGAFDLSSLRFALNGAEPIDPADVED 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 345 WV------KLTGQYLLEGYGLTECSPLVSVNPHD----IDY---------------HSG------SIGLPVPSTEAKLVD 393
Cdd:PRK07768 296 LLdagarfGLRPEAILPAYGMAEATLAVSFSPCGaglvVDEvdadllaalrravpaTKGntrrlaTLGPPLPGLEVRVVD 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 394 DDDNEVAPGEPGELCIKGPQVMLGYwQRPD----ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK07768 376 EDGQVLPPRGVGVIELRGESVTPGY-LTMDgfipAQDA---DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 470 IEDVVMQHSGVQE--VAAVGVPSGSSGEAVKIFVVKKDAAltEEALITFCRRHLTgYKVPKLVEFRDE---------LPK 538
Cdd:PRK07768 452 IERAAARVEGVRPgnAVAVRLDAGHSREGFAVAVESNAFE--DPAEVRRIRHQVA-HEVVAEVGVRPRnvvvlgpgsIPK 528
|
410
....*....|
gi 505808171 539 SNVGKiLRRE 548
Cdd:PRK07768 529 TPSGK-LRRA 537
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
2.46e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.00 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 7 NRYPADVPAEInpdryqSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQ 86
Cdd:PRK12316 1993 DRTPEAYPRGP------GVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFE 2065
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 87 YPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDSGAAAIVIVSnfaHTLEKVVDKTQVKHVILTRMGDqlstakgtlvn 165
Cdd:PRK12316 2066 LVVALLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLLTQR---HLLERLPLPAGVARLPLDRDAE----------- 2130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 166 fvvkyikrlvpkyhLPDAISFRSAlqhgyrmqyvkPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpL 245
Cdd:PRK12316 2131 --------------WADYPDTAPA-----------VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE-L 2184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 246 LHRGKELVVTALPlyhiFALTMNCLLFIELGGQNLLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLD 323
Cdd:PRK12316 2185 SPADCELQFMSFS----FDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRP 2260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 324 FSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTEC--SPLV----SVNPHDIDYhsGSIGLPVPSTEAKLVDDDDN 397
Cdd:PRK12316 2261 PAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAvvTPLLwkcrPQDPCGAAY--VPIGRALGNRRAYILDADLN 2338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 398 EVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKDGWLH-------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAErFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGE 2418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 470 IEDVVMQHSGVQEvAAVGVPSGSSGEAVKIFVVKKDAA-LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:PRK12316 2419 IEARLQAHPAVRE-AVVVAQDGASGKQLVAYVVPDDAAeDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKA 2497
|
.
gi 505808171 549 L 549
Cdd:PRK12316 2498 L 2498
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
49-455 |
4.04e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 125.47 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIV 128
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAE-LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 SNFAHTLEKVVDKTQVKHVILTRMGD---QLSTAKGTLVNF--VVkyikrlvpkyhlpdAISFRSALQHGYRMQYVKpei 203
Cdd:PTZ00216 201 GKNVPNLLRLMKSGGMPNTTIIYLDSlpaSVDTEGCRLVAWtdVV--------------AKGHSAGSHHPLNIPENN--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 204 vaDDLAFLQYTGGTTGVAKGAMLTHRNMLANL----EQVNATYGPllHRGKELVVTALPLYHIFALT-MNCLL----FIE 274
Cdd:PTZ00216 264 --DDLALIMYTSGTTGDPKGVMHTHGSLTAGIlaleDRLNDLIGP--PEEDETYCSYLPLAHIMEFGvTNIFLargaLIG 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 275 LGGQN-------------------LLITNPRDIPGLVKEL-AKYP-------------FTA-----MTGVNTLFnalLNN 316
Cdd:PTZ00216 340 FGSPRtltdtfarphgdltefrpvFLIGVPRIFDTIKKAVeAKLPpvgslkrrvfdhaYQSrlralKEGKDTPY---WNE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 317 KEF---QQLDFSSLHLSAGGGMPVQQVVAErWVKLTGQYLLEGYGLTECsplVSVNPHDI--DYHSGSIGLPVPSTEAKL 391
Cdd:PTZ00216 417 KVFsapRAVLGGRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTET---VCCGGIQRtgDLEPNAVGQLLKGVEMKL 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 392 VDDDD--NEVAPgEP-GELCIKGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKK 455
Cdd:PTZ00216 493 LDTEEykHTDTP-EPrGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-553 |
4.57e-30 |
|
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: 122.85 E-value: 4.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKS-LGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeiva 205
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 dDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnatYGPLLHRGKELVVTALPLYHIFALTMnCLLFIELGGQNLLITNP 285
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALIV-GWSACLASGATLVIRKK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 286 RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvqqvvAERWVKLTGQY----LLEGYGLTE 361
Cdd:cd05940 157 FSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLR-----PDIWEEFKERFgvprIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 362 CSpLVSVNphdIDYHSGSIG----LPVPSTEAKLVD-DDDN------------EVAPGEPGELC--IKGPQVMLGYWQrP 422
Cdd:cd05940 232 GN-SGFIN---FFGKPGAIGrnpsLLRKVAPLALVKyDLESgepirdaegrciKVPRGEPGLLIsrINPLEPFDGYTD-P 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 423 DATDEIIK-------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVP-SGSSG 494
Cdd:cd05940 307 AATEKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDG 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 495 EA-VKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05940 387 RAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-553 |
2.37e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 121.71 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAKGTLVNFVVkyikrlvpkyhlPDAisfrsalqhgyrmq 197
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRV------------ADP-------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivaDDLAFLQYTGGTTGVAKGAMLTHR------NMLAnleqvnATYGpllHRGKELVVTALPLYHIFALtMNCLL 271
Cdd:PRK07867 152 --------DDLFMLIFTSGTSGDPKAVRCTHRkvasagVMLA------QRFG---LGPDDVCYVSMPLFHSNAV-MAGWA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 272 FIELGGQNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEfqQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQ 351
Cdd:PRK07867 214 VALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPE--RPDDADNPLRIVYGNEGAPGDIARFARRFGC 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 352 YLLEGYGLTECSPLVSVNPhdiDYHSGSIGLPVPSTeaKLVD-DDDNEVAPGEP------------GELC-IKGPQVMLG 417
Cdd:PRK07867 292 VVVDGFGSTEGGVAITRTP---DTPPGALGPLPPGV--AIVDpDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 418 YWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAV 497
Cdd:PRK07867 367 YYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 498 KIFVV-KKDAALTEEALITF--CRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK07867 447 MAALVlAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEG 505
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
31-553 |
2.96e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 122.17 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFINMGE------VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK00174 76 HLKTR-GDKVAIIWEGDdpgdsrKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVDK-----TQVKHVI-LTRMGDQLSTAKGtlvnfvvkyikR 173
Cdd:PRK00174 154 FGGFSAEALADRIIDAGAKLVITADEGvrggkPIPLKANVDEalancPSVEKVIvVRRTGGDVDWVEG-----------R 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 174 LVpKYHlpDAISFRSAlqhgyrmqYVKPEIV-ADDLAFLQYTGGTTGVAKG-----------AMLTHRNML--------- 232
Cdd:PRK00174 223 DL-WWH--ELVAGASD--------ECEPEPMdAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVFdykdgdvyw 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 233 --ANLEQVNA----TYGPLLHRGKELVVTALPLY-------HIfaltmncllfIELGGQNLLITNPRDIPGLVKELAKYP 299
Cdd:PRK00174 292 ctADVGWVTGhsyiVYGPLANGATTLMFEGVPNYpdpgrfwEV----------IDKHKVTIFYTAPTAIRALMKEGDEHP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 300 ftamtgvntlfnallnnkefQQLDFSSLHLSAGGGMPV--------QQVV-AER-------WVKLTGQYLLegygltecS 363
Cdd:PRK00174 362 --------------------KKYDLSSLRLLGSVGEPInpeawewyYKVVgGERcpivdtwWQTETGGIMI--------T 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 364 PLvsvnPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKG--PQVMLGYWQRPD-------ATdeiIKDGWL 434
Cdd:PRK00174 414 PL----PGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHErfvktyfST---FKGMYF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 435 hTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALI 514
Cdd:PRK00174 487 -TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 505808171 515 TFCRRHLTgyKV------PKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK00174 566 KELRNWVR--KEigpiakPDVIQFAPGLPKTRSGKIMRRILRKIA 608
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-549 |
3.03e-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: 120.26 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 118 NDSGAAAIVIvsnfahtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhLPDaisfrsalqhgyrmq 197
Cdd:cd17650 81 EDSGAKLLLT----------------------------------------------------QPE--------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 198 yvkpeivadDLAFLQYTGGTTGVAKGAMLTHRNMlanleqVNATYGPLLHRG-KELVVTALPLYHI--------FALTmn 268
Cdd:cd17650 94 ---------DLAYVIYTSGTTGKPKGVMVEHRNV------AHAAHAWRREYElDSFPVRLLQMASFsfdvfagdFARS-- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 269 cLLFielGGQnlLITNPRDI----PGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpvqQVVAER 344
Cdd:cd17650 157 -LLN---GGT--LVICPDEVkldpAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS----DGCKAQ 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 345 WVK------LTGQYLLEGYGLTECSPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQV 414
Cdd:cd17650 227 DFKtlaarfGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 415 MLGYWQRPDATDEIIKDGWL-------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVG 487
Cdd:cd17650 307 ARGYLNRPELTAERFVENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVA 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 488 VPSGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17650 386 VREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-553 |
6.04e-29 |
|
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: 119.84 E-value: 6.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQA-QGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VivsnfahtlekvvdktqvkhvilTRMGDQLSTAKGTlvnfvvkyikrlvpkyHLP--DAISFRSALqhgyrmqyvkpei 203
Cdd:cd05939 80 I-----------------------FNLLDPLLTQSST----------------EPPsqDDVNFRDKL------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 204 vaddlaFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKELVVTALPLYHIFALTM---NCLLFielgGQNL 280
Cdd:cd05939 108 ------FYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFG---MRPEDVVYDCLPLYHSAGGIMgvgQALLH----GSTV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 281 LITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvQQVvaerWVKLTGQY----LLEG 356
Cdd:cd05939 175 VIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR-PQI----WEQFVRRFgipqIGEF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 357 YGLTEC-SPLVsvnphDIDYHSGSIGLpVPSTEAKL-------VDDDDNEV-----------APGEPGELC---IKGPQV 414
Cdd:cd05939 250 YGATEGnSSLV-----NIDNHVGACGF-NSRILPSVypirlikVDEDTGELirdsdglcipcQPGEPGLLVgkiIQNDPL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 415 M--LGYWQRPDATDEIIKDGWLH------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAV 486
Cdd:cd05939 324 RrfDGYVNEGATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 487 GVP-SGSSGEAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05939 404 GVEvPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
3.50e-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: 117.28 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLnDSGAAAIVIV 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 SNFAHtlekvvdktqvkhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivADDL 208
Cdd:cd05974 79 DENTH-----------------------------------------------------------------------ADDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLHRGKELVVTALPLYHIFALTmnCLLFIELGGQNLLITN-PR- 286
Cdd:cd05974 88 MLLYFTSGTTSKPKLVEHTHRSYPVG--HLSTMYWIGLKPGDVHWNISSPGWAKHAWS--CFFAPWNAGATVFLFNyARf 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKELAKYPFTAMTGVNTLFNALLnnkefqQLDFSSLHLS----AGGGMPVQQVVAERWVKLTGQYLLEGYGLTEC 362
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLI------QQDLASFDVKlrevVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 363 SPLVSVNPHDIdYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPG-ELCIKGPQ-VMLGYWQRPDATDEIIKDGWLHTGDIA 440
Cdd:cd05974 238 TALVGNSPGQP-VKAGSMGRPLPGYRVALLDPDGAPATEGEVAlDLGDTRPVgLMKGYAGDPDKTAHAMRGGYYRTGDIA 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 441 VMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA----LTEEALITF 516
Cdd:cd05974 317 MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYepspETALEIFRF 396
|
490 500 510
....*....|....*....|....*....|....
gi 505808171 517 CRRHLTGYKVPKLVEFRdELPKSNVGKILRRELR 550
Cdd:cd05974 397 SRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
32-549 |
4.96e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 117.79 E-value: 4.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 32 ATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQGlGLQKGDRVALMMPNLLQYPVALFGilrAGMIAVNVNPLYTPR 111
Cdd:PRK13383 44 TAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFA---VGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 112 ElehqlNDSGAAAIVivsnfAHTLEKVVDKTQvkhviltrMGDQLSTAKgtlvnfvvkyikrlvpkyhlpDAISFRSALQ 191
Cdd:PRK13383 120 R-----SDALAAALR-----AHHISTVVADNE--------FAERIAGAD---------------------DAVAVIDPAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 192 HGYRMQYVKPEIVADDLAFLqYTGGTTGVAKGamlthrnmLANLEQVNATYG---PLLHRGK----ELVVTALPLYHIFA 264
Cdd:PRK13383 161 AGAEESGGRPAVAAPGRIVL-LTSGTTGKPKG--------VPRAPQLRSAVGvwvTILDRTRlrtgSRISVAMPMFHGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LTMnCLLFIELGGqNLLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSSLHLSAGGGMPVQQVVA 342
Cdd:PRK13383 232 LGM-LMLTIALGG-TVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYwqrP 422
Cdd:PRK13383 310 QRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---T 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 423 DATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV 502
Cdd:PRK13383 387 DGGGKAVVDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVV 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 505808171 503 KKDAA-LTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK13383 467 LHPGSgVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
27-549 |
9.76e-28 |
|
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: 116.38 E-value: 9.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 27 ELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 107 LYTPRELEHQLNDsgaaaivivsnfahtlekvvdkTQVKhVILTrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisf 186
Cdd:cd17644 83 NYPQERLTYILED----------------------AQIS-VLLT------------------------------------ 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 187 rsalqhgyrmqyvKPEivadDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKELVVTALPlyhiFALT 266
Cdd:cd17644 104 -------------QPE----NLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG-ITSSDRVLQFASIA----FDVA 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 267 MNCLLFIELGGQNL-LITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDF-SSLHLSAGGGMPVQQVVA 342
Cdd:cd17644 162 AEEIYVTLLSGATLvLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 ERWVKLTGQY--LLEGYGLTECSPLVSV----NPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVML 416
Cdd:cd17644 242 RQWQKNVGNFiqLINVYGPTEATIAATVcrltQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLAR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 417 GYWQRPDATDE-IIKDGWLH--------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVG 487
Cdd:cd17644 322 GYLNRPELTAEkFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKT-AVVI 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505808171 488 VPSGSSGEA--VKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17644 401 VREDQPGNKrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-551 |
1.16e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 118.73 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 7 NRYPADVPAEinpdryQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFA-AYLQQGLGlqkGDR-VALMMPNL 84
Cdd:PRK12467 3085 NATAAAYPSE------RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAhRLIAIGVG---PDVlVGVAVERS 3155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 85 LQYPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDSGAAaiVIVSNfAHTLEKVvdktQVKHVILTRMGDQLStakgtl 163
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEY-PRErLAYMIEDSGVK--LLLTQ-AHLLEQL----PAPAGDTALTLDRLD------ 3221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 164 vnfvvkyikrlvpkyhlpdaisfrsalQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHrNMLANLEQVNATYG 243
Cdd:PRK12467 3222 ---------------------------LNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRH-GALANHLCWIAEAY 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 244 PLLHRGKELVVTALPlyhiFALTMNCLLFIELGGQNLLIT--NPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ 321
Cdd:PRK12467 3274 ELDANDRVLLFMSFS----FDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAD 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 322 LDFSSLHLSAGGGMPVQQVvAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDDDN 397
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAF-EQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDGQLN 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 398 EVAPGEPGELCIKGPQVMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK12467 3429 PVPVGVAGELYIGGVGLARGYHQRPSLTAErFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 3508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 470 IEDVVMQHSGVQEVAAVGVPsGSSGEAVKIFVVKKDAaltEEALITFCRRHLTG----YKVPKLVEFRDELPKSNVGKIL 545
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPADP---QGDWRETLRDHLAAslpdYMVPAQLLVLAAMPLGPNGKVD 3584
|
....*.
gi 505808171 546 RRELRD 551
Cdd:PRK12467 3585 RKALPD 3590
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-549 |
3.68e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.18 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 5 WlNRYPADVPAEinpdryQSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYL-QQGLGLQKgdRVALMMPN 83
Cdd:PRK12467 1563 W-NATHTGYPLA------RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLiALGVGPEV--LVGIAVER 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 84 LLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVSnfaHTLEKVVDKTQVKHVILTRMGDQLStakgtl 163
Cdd:PRK12467 1634 SLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS---HLQARLPLPDGLRSLVLDQEDDWLE------ 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 164 vnfvvkyikrlvpkyhlpdaisfrsalqhGYRMqyVKPEIVADD--LAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAT 241
Cdd:PRK12467 1705 -----------------------------GYSD--SNPAVNLAPqnLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEA 1753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 242 YGpllhrgkeLVVT-ALPLYHIFALTMNC--LLFIELGGQNLLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLN 315
Cdd:PRK12467 1754 YQ--------LSAAdVVLQFTSFAFDVSVweLFWPLINGARLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQ 1825
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 316 NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGS----IGLPVPSTEAKL 391
Cdd:PRK12467 1826 MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYI 1905
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 392 VDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEII-------KDGWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGF 463
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGF 1985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 464 NVYPNEIEDVVMQHSGVQEvAAVGVPSGSSGEAVKIFVVKKDAALTEE-----ALITFCRRHLTG----YKVPKLVEFRD 534
Cdd:PRK12467 1986 RIELGEIEARLREQGGVRE-AVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvALRAILKNHLKAslpeYMVPAHLVFLA 2064
|
570
....*....|....*
gi 505808171 535 ELPKSNVGKILRREL 549
Cdd:PRK12467 2065 RMPLTPNGKLDRKAL 2079
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-550 |
1.77e-26 |
|
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: 112.91 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd05915 26 TYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDktqvkhvILTRMGDQLSTAKgtlvnfvvkyikrlvpKYHlpdaiSFRSALQHGY-RMQYVKPEIVADDL 208
Cdd:cd05915 105 NLLPLVEAIRG-------ELKTVQHFVVMDE----------------KAP-----EGYLAYEEALgEEADPVRVPERAAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AfLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLLHRGKELVVTALPLYHIFALtmnCLLFI--ELGGQNLLITNPR 286
Cdd:cd05915 157 G-MAYTTGTTGLPKGVVYSHRALVLHSLAA-SLVDGTALSEKDVVLPVVPMFHVNAW---CLPYAatLVGAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFS-SLHLSAGGGMPVQqvVAERWVKLTGQYLLEGYGLTECSPL 365
Cdd:cd05915 232 DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtLRRLVVGGSAAPR--SLIARFERMGVEVRQGYGLTETSPV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 366 ------------------VSVNPHD-IDYHSGSIGLPVPSTEAKLVDDDDNEVapgepgeLCIKGPQVMLGYWQRPDATD 426
Cdd:cd05915 310 vvqnfvkshleslseeekLTLKAKTgLPIPLVRLRVADEEGRPVPKDGKALGE-------VQLKGPWITGGYYGNEEATR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 427 EI-IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKD 505
Cdd:cd05915 383 SAlTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRG 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 505808171 506 AALTEEALITFCRRHLTGYK-VPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05915 463 EKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-550 |
8.97e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 108.59 E-value: 8.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 175 VPKYHLPDAISFRSALQHGyrmqyvkpEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnATYGPLLHRGKELVv 254
Cdd:PRK07824 12 VPAQDERRAALLRDALRVG--------EPIDDDVALVVATSGTTGTPKGAMLTAAALTASAD---ATHDRLGGPGQWLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 255 tALPLYHIFAltMNCLLFIELGGQNLLIT------NPRDIPGLVKELA---KYpfTAMTGVNtLFNALLNNKEFQQL-DF 324
Cdd:PRK07824 80 -ALPAHHIAG--LQVLVRSVIAGSEPVELdvsagfDPTALPRAVAELGggrRY--TSLVPMQ-LAKALDDPAATAALaEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 325 SSLhLSAGGGMPVQqvVAERWVKLtGQYLLEGYGLTECSplvsvnphdidyhSGSI--GLPVPSTEAKLVDdddnevapg 402
Cdd:PRK07824 154 DAV-LVGGGPAPAP--VLDAAAAA-GINVVRTYGMSETS-------------GGCVydGVPLDGVRVRVED--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 403 epGELCIKGPQVMLGYwQRPDATDEIIKDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQE 482
Cdd:PRK07824 208 --GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 483 VAAVGVPSGSSGEAVKIFVVKK-DAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07824 284 CAVFGLPDDRLGQRVVAAVVGDgGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
190-510 |
8.15e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 108.95 E-value: 8.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 190 LQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLA-------NLEQVNATYGPllhrgKELVVTALPLYHI 262
Cdd:PLN02614 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTliagvirLLKSANAALTV-----KDVYLSYLPLAHI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 263 FALTMN-CllFIELGGQ--------NLLITN------------PRDI----PGLVKELA--------------KYPFTAM 303
Cdd:PLN02614 282 FDRVIEeC--FIQHGAAigfwrgdvKLLIEDlgelkptifcavPRVLdrvySGLQKKLSdggflkkfvfdsafSYKFGNM 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 304 ------TGVNTLFNALLNNKEFQQLDfSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE-CSPLVSVNPHDIDYh 376
Cdd:PLN02614 360 kkgqshVEASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDM- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 377 SGSIGLPVPSTEAKLVDDDDNE---VAPGEPGELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDR 453
Cdd:PLN02614 438 LGTVGPPVPNVDIRLESVPEMEydaLASTPRGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDR 517
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 505808171 454 KKDMI-LVSGFNVYPNEIEDVvmqHSGVQEVAAVGVpSGSSGEAVKIFVVKKDAALTE 510
Cdd:PLN02614 518 KKNIFkLSQGEYVAVENIENI---YGEVQAVDSVWV-YGNSFESFLVAIANPNQQILE 571
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
49-549 |
9.69e-25 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 107.10 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAIViv 128
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 snfahtlekvvdkTQVKhviltrmgdqlstakgtlvnfvvkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeivadDL 208
Cdd:cd17648 91 -------------TNST-------------------------------------------------------------DL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHRGKElVVTALPLYhIFALTMNCLLFIELGGQNLLITNPR-- 286
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDE-AVLFFSNY-VFDFFVEQMTLALLNGQKLVVPPDEmr 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 287 -DIPGLVKELAKYPFTAMTGVNTLFnallnnkefQQLDFSSL-HL----SAGggmpvQQVVAERWVKLTGQY---LLEGY 357
Cdd:cd17648 174 fDPDRFYAYINREKVTYLSGTPSVL---------QQYDLARLpHLkrvdAAG-----EEFTAPVFEKLRSRFaglIINAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 358 GLTEcsplVSVNPHDIDYHSG-----SIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPD--------- 423
Cdd:cd17648 240 GPTE----TTVTNHKRFFPGDqrfdkSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPEltaerflpn 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 424 --ATDEIIKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG--VPSGSSGE 495
Cdd:cd17648 316 pfQTEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkeDASQAQSR 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 496 AVKIFV---VKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17648 396 IQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
49-452 |
1.01e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 108.43 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYT-----PRELEHQLN----- 118
Cdd:PRK08180 70 LTYAEALERVRAIAQALL-DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSlvsqdFGKLRHVLElltpg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 119 ----DSGAA---AIVIVSnFAHTlEKVVDKTQVKHVILTRMGDQLSTAKGTLVnfvvkyikrlvpkyhlpDAISFRsalq 191
Cdd:PRK08180 149 lvfaDDGAAfarALAAVV-PADV-EVVAVRGAVPGRAATPFAALLATPPTAAV-----------------DAAHAA---- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 192 hgyrmqyvkpeIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHRGKELVVTALPLYHIFALTMNCLL 271
Cdd:PRK08180 206 -----------VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPPVLVDWLPWNHTFGGNHNLGI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 272 FIELGGqNLLITNPRDIPGLVKE----LAKYPFTAMTGVNTLFNALLN----NKEFQQLDFSSLHLS--AGGGMPvqQVV 341
Cdd:PRK08180 274 VLYNGG-TLYIDDGKPTPGGFDEtlrnLREISPTVYFNVPKGWEMLVPalerDAALRRRFFSRLKLLfyAGAALS--QDV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 342 AERWVKLTGQYLLE------GYGLTECSPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEvapgepgELCIKGPQVM 415
Cdd:PRK08180 351 WDRLDRVAEATCGErirmmtGLGMTETAPSAT-FTTGPLSRAGNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVT 422
|
410 420 430
....*....|....*....|....*....|....*..
gi 505808171 416 LGYWQRPDATDEiikdgwlhtgdiaVMDDEGFLRIVD 452
Cdd:PRK08180 423 PGYWRAPELTAE-------------AFDEEGYYRSGD 446
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
3.39e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.12 E-value: 3.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 7 NRYPADVPAEINPDRyqslveLFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQ 86
Cdd:PRK12316 3047 NATAAEYPLERGVHR------LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLE 3119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 87 YPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAaaivivsnfahtlekvvdktqvkHVILTRMGDQLSTAKGTLVNF 166
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA-----------------------QLLLSQSHLRLPLAQGVQVLD 3176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 167 VvkyikrlvpkyhlpdaisfrSALQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplL 246
Cdd:PRK12316 3177 L--------------------DRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG--L 3234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 247 HRGKELVVTALPLYHIFALTMNCLLfieLGGQNLLITNPR---DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLD 323
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPL---MSGARVVLAGPEdwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 324 FSSLHLSAGGGMPVQqvVAERWVklTGQYLLEGYGLTECSPLVSVNPHDIDYHSGS-IGLPVPSTEAKLVDDDDNEVAPG 402
Cdd:PRK12316 3312 SLKRIVCGGEALPAD--LQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVG 3387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 403 EPGELCIKGPQVMLGYWQRPDATDE-------IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK12316 3388 ALGELYLGGEGLARGYHNRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505808171 476 QHSGVQEVAAVGVpsgsSGEAVKIFVVKKD-AALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 3468 EHPWVREAVVLAV----DGRQLVAYVVPEDeAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
50-452 |
3.49e-24 |
|
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: 106.36 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH----QLNDSGAAAI 125
Cdd:cd05921 27 TYAEALRQVRAIAQGLLD-LGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDLaklkHLFELLKPGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSN---FAHTLEKVVDkTQVKHVILTRMGDQLstakgtlvnfvvkyikrlvpkyhlpDAISFRS--ALQHGYRMQYVK 200
Cdd:cd05921 106 VFAQDaapFARALAAIFP-LGTPLVVSRNAVAGR-------------------------GAISFAElaATPPTAAVDAAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 201 PEIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlhRGKELV-VTALPLYHIFALTMNCLLFIELGGqN 279
Cdd:cd05921 160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFF--GEEPPVlVDWLPWNHTFGGNHNFNLVLYNGG-T 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 280 LLITNPRDIPGLVKELAK--------YPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW----VK 347
Cdd:cd05921 237 LYIDDGKPMPGGFEETLRnlreisptVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLqalaVA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 348 LTGQY--LLEGYGLTECSPLvSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEvapgepgELCIKGPQVMLGYWQRPDAT 425
Cdd:cd05921 317 TVGERipMMAGLGATETAPT-ATFTHWPTERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPELT 388
|
410 420
....*....|....*....|....*..
gi 505808171 426 deiikdgwlhtgdIAVMDDEGFLRIVD 452
Cdd:cd05921 389 -------------AQAFDEEGFYCLGD 402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
205-549 |
4.08e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.95 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 205 ADDLAFLQYTGGTTGVAKGAMLTHRNMLAN-LEQVnatygPLLHRGKELVVtALPLYHIFALTMNCLLFIELGGQNLLIT 283
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNqLSKV-----PYLALSEADVI-AQTASQSFDISVWQFLAAPLFGARVEIV 3941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 284 nPRDIP----GLVKELAKYPFTAMTGVNTLFNALLNNKEfQQLDFSSLHLSAGGGMPVQqvVAERWVKLTGQY-LLEGYG 358
Cdd:PRK05691 3942 -PNAIAhdpqGLLAHVQAQGITVLESVPSLIQGMLAEDR-QALDGLRWMLPTGEAMPPE--LARQWLQRYPQIgLVNAYG 4017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 359 LTECSPLVSVNPHDIDYHSGS---IGLPVPSTEAKLVDDDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEI------- 428
Cdd:PRK05691 4018 PAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAfvphpfg 4097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 429 -IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEvAAVGVPSGSSGEAVKIFVVKKDAA 507
Cdd:PRK05691 4098 aPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTV 4176
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 505808171 508 LTEEALITFCRRHLTG----YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 4177 LAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
4.96e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 107.56 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 103 NVNPLYTPRELEHQLNDSGAAAIVIVSnfaHTLEKVvdkTQVKHVILTRMgDQLStakgtLVNFVVKyikrlVPKYHLpd 182
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQS---HLLERL---PQAEGVSAIAL-DSLH-----LDSWPSQ-----APGLHL-- 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 183 aisfrsalqHGyrmqyvkpeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHRGKELVVTA-----L 257
Cdd:PRK05691 1271 ---------HG------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDSDVLMQKApisfdV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHIF-ALTMNCLLFIELGGQNlliTNPRDIPGLVKElakYPFTAMTGVNTLFNALLNnkEFQQLDFSSLHLSAGGGMP 336
Cdd:PRK05691 1328 SVWECFwPLITGCRLVLAGPGEH---RDPQRIAELVQQ---YGVTTLHFVPPLLQLFID--EPLAAACTSLRRLFSGGEA 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 337 VQQVVAERWVKLTGQYLLEG-YGLTECSPLVSvnpH----DIDYHSGSIGLPVPSTEAKLVDDDDNEVAPGEPGELCIKG 411
Cdd:PRK05691 1400 LPAELRNRVLQRLPQVQLHNrYGPTETAINVT---HwqcqAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 412 PQVMLGYWQRPDAT------DEIIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEv 483
Cdd:PRK05691 1477 AGLARGYLGRPALTaerfvpDPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ- 1555
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505808171 484 AAVGVPSGSSG-EAVKIFVVKKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 1556 AAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
49-452 |
1.50e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 104.74 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH----QLNDSGAAA 124
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLD-LGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHaklkHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 125 IVIVSN---FAHTLEkVVDKTQVKHVILTRMGDQLSTAKgtlvnfvvkyIKRLVPKyhlPDAISFRSAlqhgyrMQYVKP 201
Cdd:PRK12582 160 VVFAQSgapFARALA-ALDLLDVTVVHVTGPGEGIASIA----------FADLAAT---PPTAAVAAA------IAAITP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 202 EIVADDLaflqYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHRGKELVVTALPLYHIFA--LTMNCLLFielGGQN 279
Cdd:PRK12582 220 DTVAKYL----FTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnANFNGLLW---GGGT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 280 LLITNPRDIPGLVKELAK--------YPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERW----VK 347
Cdd:PRK12582 293 LYIDDGKPLPGMFEETIRnlreisptVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMqalaVR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 348 LTGQY--LLEGYGLTECSPlVSVNPHDIDYHSGSIGLPVPSTEAKLvddddnevAP-GEPGELCIKGPQVMLGYWQRPDA 424
Cdd:PRK12582 373 TTGHRipFYTGYGATETAP-TTTGTHWDTERVGLIGLPLPGVELKL--------APvGDKYEVRVKGPNVTPGYHKDPEL 443
|
410 420
....*....|....*....|....*...
gi 505808171 425 TDeiikdgwlhtgdiAVMDDEGFLRIVD 452
Cdd:PRK12582 444 TA-------------AAFDEEGFYRLGD 458
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
48-499 |
2.16e-23 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 103.74 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 48 VMTYRKLEERSRAFAAYLQQglglQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGaaaivi 127
Cdd:PRK06334 45 KLSYNQVRKAVIALATKVSK----YPDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVG------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 128 vsnfahtlekvvdktqVKHVILTR-MGDQLSTAKGTLVN--FVVKYIKRLVPKYHLPDA--ISFRSALQHGYRMQYVK-P 201
Cdd:PRK06334 115 ----------------VTHVLTSKqLMQHLAQTHGEDAEypFSLIYMEEVRKELSFWEKcrIGIYMSIPFEWLMRWFGvS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 202 EIVADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlhrGKELVVTALPLYHIFALTmNCLLFIELGGQNLL 281
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK---EDDVMMSFLPPFHAYGFN-SCTLFPLLSGVPVV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 282 IT-NPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLL-EGYGL 359
Cdd:PRK06334 255 FAyNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLrQGYGT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 360 TECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDN-EVAPGEPGELCIKGPQVMLGYWQRpDATDEIIK---DGWLH 435
Cdd:PRK06334 335 TECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGE-DFGQGFVElggETWYV 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG--VPSGSSGEAVKI 499
Cdd:PRK06334 414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAADHAGplVVCGLPGEKVRL 479
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-536 |
2.44e-23 |
|
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: 103.53 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 VIVSNFAHTLEKVVDKTQVKHVILTRMGDQLSTAK-GTLVNFVVKYIKRLVPKYhLPDAISFRSalqhgyrmqyvkpeiv 204
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGvISLLDKVDAASDEPVPAS-LRAHVTIKS---------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 205 addLAFLQYTGGTTGVAKGAMLTHRNMLanleQVNATYGPLLHRGKELVVTALPLYHIFALTMNCLLFIELGGQNLLITn 284
Cdd:cd05938 146 ---PALYIYTSGTTGLPKAARISHLRVL----QCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKP- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 prdipglvK--------ELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGmpVQQVVAERWVKLTGQ-YLLE 355
Cdd:cd05938 218 --------KfsasqfwdDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNG--LRADVWREFLRRFGPiRIRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 356 GYGLTECSplVSVnphdIDY--HSGSIG---------LPV------PSTEAKLVDDDDN--EVAPGEPGELCIKGPQV-- 414
Cdd:cd05938 288 FYGSTEGN--IGF----FNYtgKIGAVGrvsylykllFPFelikfdVEKEEPVRDAQGFciPVAKGEPGLLVAKITQQsp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 415 MLGYWQRPDATD-----EIIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:cd05938 362 FLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 505808171 488 VP-SGSSGE----AVKIfvvKKDAALTEEALITFCRRHLTGYKVPKLVEFRDEL 536
Cdd:cd05938 442 VTvPGHEGRigmaAVKL---KPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-458 |
2.47e-23 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 104.43 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 2 KKVWLNRYPADVPAE----INPDRYQSLVE-----------LFEHATTRYADQP-----AFIN----------------M 45
Cdd:PLN02387 22 KKGKKRGVPVDVGGEpgyaIRNARFPELVEtpwegattlaaLFEQSCKKYSDKRllgtrKLISrefetssdgrkfeklhL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEV--MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAA 123
Cdd:PLN02387 102 GEYewITYGQVFERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 124 AIVivsnfahtlekvVDKTQVKHVIltRMGDQLSTAKGtlvnfvVKYIKRLVPKYHLPDA-------ISFRSALQHGyRM 196
Cdd:PLN02387 181 TVI------------CDSKQLKKLI--DISSQLETVKR------VIYMDDEGVDSDSSLSgssnwtvSSFSEVEKLG-KE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 197 QYVKPEI-VADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlhrGKELVVTA-LPLYHIFALTMNCLLF-- 272
Cdd:PLN02387 240 NPVDPDLpSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAyLPLAHILELAAESVMAav 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 273 -IELG-GQNLLITN-----PRDIPGLVKELAKypfTAMTGV----------------------NTLFN-------ALLNN 316
Cdd:PLN02387 317 gAAIGyGSPLTLTDtsnkiKKGTKGDASALKP---TLMTAVpaildrvrdgvrkkvdakgglaKKLFDiaykrrlAAIEG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 317 KEF----------QQLDFSSLHLSAG--------GGMPVQQVvAERWVKLT-GQYLLEGYGLTE-CSPLVSVNPHDIDYh 376
Cdd:PLN02387 394 SWFgawglekllwDALVFKKIRAVLGgrirfmlsGGAPLSGD-TQRFINIClGAPIGQGYGLTEtCAGATFSEWDDTSV- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 377 sGSIGLPVPSTEAKLVDDDDNEV----APGEPGELCIKGPQVMLGYWQRPDATDEIIKDG-----WLHTGDIAVMDDEGF 447
Cdd:PLN02387 472 -GRVGPPLPCCYVKLVSWEEGGYlisdKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGC 550
|
570
....*....|.
gi 505808171 448 LRIVDRKKDMI 458
Cdd:PLN02387 551 LEIIDRKKDIV 561
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
3.28e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.87 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYL-QQGLGLQKgdRVALMMPNLLQYPVALFGILRAGMIA 101
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALrERGVGPQV--RVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 102 VNVNPLYTPRELEHQLNDSGAAaiVIVSNFAhtlekvvdktqvkhviltrmgdqLSTAKGTLVNFVVKYI--KRLVPKYH 179
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIG--LLLSDRA-----------------------LFEALGELPAGVARWCleDDAAALAA 2320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 180 LPDA-ISFRSALQHgyrmqyvkpeivaddLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHRGKElvvTALP 258
Cdd:PRK05691 2321 YSDApLPFLSLPQH---------------QAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG---MRADD---CELH 2379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 259 LYHI-FALTMNCLLFIELGGQNLLIT-----NPRDIPGLVKELAkypfTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAG 332
Cdd:PRK05691 2380 FYSInFDAASERLLVPLLCGARVVLRaqgqwGAEEICQLIREQQ----VSILGFTPSYGSQLAQWLAGQGEQLPVRMCIT 2455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 333 GGmpvQQVVAERWVKLTG----QYLLEGYGLTE--CSPLVSVNPHDIDYHSGS--IGLPVPSTEAKLVDDDDNEVAPGEP 404
Cdd:PRK05691 2456 GG---EALTGEHLQRIRQafapQLFFNAYGPTEtvVMPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGAT 2532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 405 GELCIKGPQVMLGYWQRPDATDE-IIKDGWLH-------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAErFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLE 2612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 477 HSGVQE--VAAVGVPsgsSGEAVKIFVVKKDAALTE-------EALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRR 547
Cdd:PRK05691 2613 HPAVREavVLALDTP---SGKQLAGYLVSAVAGQDDeaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRR 2689
|
..
gi 505808171 548 EL 549
Cdd:PRK05691 2690 AL 2691
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
23-555 |
1.67e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 100.74 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 23 QSLVELFEHATTRYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVAL---MMPNLLqypVALFGILRAG- 98
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDS-LKLPDKSPIIVfghMSPEML---ATFLGAVKAGh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 99 -MIAVNVnplYTPRELEHQLNDSGAAAIVIvsnfaHTLEKVVDKTQVKHVILtrmgDQLSTAKGTLVNFVVKyikrlvpk 177
Cdd:PRK04813 78 aYIPVDV---SSPAERIEMIIEVAKPSLII-----ATEELPLEILGIPVITL----DELKDIFATGNPYDFD-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 178 yhlpdaisfrsalqhgyrmQYVKpeivADDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllhRGKELVVTAL 257
Cdd:PRK04813 138 -------------------HAVK----GDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFA----LPEGPQFLNQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYHiFALT-MN---CLLfieLGGQ-NLL----ITNPRDipgLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSL- 327
Cdd:PRK04813 191 APYS-FDLSvMDlypTLA---SGGTlVALpkdmTANFKQ---LFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLt 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 328 H-LSAGGGMPVQqvvaerwvklTGQYLLE---------GYGLTECSPLVS---VNPHDID-YHSGSIGLPVPSTEAKLVD 393
Cdd:PRK04813 264 HfLFCGEELPHK----------TAKKLLErfpsatiynTYGPTEATVAVTsieITDEMLDqYKRLPIGYAKPDSPLLIID 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 394 DDDNEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIK--DGW--LHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK04813 334 EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFtfDGQpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 470 IEDVVMQHSGVQEvaAVGVPSGSSGEAVKI--FVVKKDAALTEEALITFCRR-----HLTGYKVPKLVEFRDELPKSNVG 542
Cdd:PRK04813 413 IEQNLRQSSYVES--AVVVPYNKDHKVQYLiaYVVPKEEDFEREFELTKAIKkelkeRLMEYMIPRKFIYRDSLPLTPNG 490
|
570
....*....|...
gi 505808171 543 KILRRELRDEARA 555
Cdd:PRK04813 491 KIDRKALIEEVNK 503
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
209-550 |
5.66e-22 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 99.46 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHRGKELVVTALPLYHIFALTMncLLFIELGGQNLLITnprdi 288
Cdd:PRK05851 155 AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG--LDAATDVGCSWLPLYHDMGLAF--LLTAALAGAPLWLA----- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 289 PglVKELAKYPF---TAMTGVNTLFNALLN---------NKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQY---- 352
Cdd:PRK05851 226 P--TTAFSASPFrwlSWLSDSRATLTAAPNfaynligkyARRVSDVDLGALRVALNGGEPVDCDGFERFATAMAPFgfda 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 353 --LLEGYGLTECSPLVSVnP--------HDIDYHSGS-------IGLPVPSTEAKLV-DDDDNEVAPGEPGELCIKGPQV 414
Cdd:PRK05851 304 gaAAPSYGLAESTCAVTV-PvpgiglrvDEVTTDDGSgarrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASM 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 415 MLGYWqrpdATDEIIKDGWLHTGDIAVMDDEGfLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQE--VAAVGVPSGS 492
Cdd:PRK05851 383 MSGYL----GQAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREgaVVAVGTGEGS 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505808171 493 --SGEAVKIFVVKKDAALTEEALITfcRRHLTGYKVPKLVEFRD--ELPKSNVGKILRRELR 550
Cdd:PRK05851 458 arPGLVIAAEFRGPDEAGARSEVVQ--RVASECGVVPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-550 |
1.38e-21 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 98.87 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 31 HATTRyADQPAFI------NMGEVMTYRKLEERSRAFAAYLQqGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK10524 62 HLAKR-PEQLALIavstetDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 105 NPLYTPRELEHQLNDsgAAAIVIVS-----------NFAHTLEKVVDKTQVK--HVILTRMG-DQLSTAKGTLVNFvvky 170
Cdd:PRK10524 140 FGGFASHSLAARIDD--AKPVLIVSadagsrggkvvPYKPLLDEAIALAQHKprHVLLVDRGlAPMARVAGRDVDY---- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 171 ikrlvpkyhlpdaisfrSALQHGYRMQYVKPEIV-ADDLAFLQYTGGTTGVAKGAmltHRNMlanleqvnatygpllhrG 249
Cdd:PRK10524 214 -----------------ATLRAQHLGARVPVEWLeSNEPSYILYTSGTTGKPKGV---QRDT-----------------G 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 250 KELVVTALPLYHIF----ALTMNCLLFIE-------------LGGQNLLI---TNPRDIPGLVKEL-AKYpftamtGVNT 308
Cdd:PRK10524 257 GYAVALATSMDTIFggkaGETFFCASDIGwvvghsyivyaplLAGMATIMyegLPTRPDAGIWWRIvEKY------KVNR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 309 LFNA-----LLNNKEFQQL---DFSSLHLSAGGGMPVQQVVAeRWVKLT-GQYLLEGYGLTECS-PLVSVNP--HDIDYH 376
Cdd:PRK10524 331 MFSAptairVLKKQDPALLrkhDLSSLRALFLAGEPLDEPTA-SWISEAlGVPVIDNYWQTETGwPILAIARgvEDRPTR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 377 SGSIGLPVPSTEAKLVDDDDNE-VAPGEPGELCIKGP---QVMLGYWqRPDatDEIIKDGWLH-------TGDIAVMDDE 445
Cdd:PRK10524 410 LGSPGVPMYGYNVKLLNEVTGEpCGPNEKGVLVIEGPlppGCMQTVW-GDD--DRFVKTYWSLfgrqvysTFDWGIRDAD 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 446 GFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEA---------LITF 516
Cdd:PRK10524 487 GYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlalekeIMAL 566
|
570 580 590
....*....|....*....|....*....|....
gi 505808171 517 CRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK10524 567 VDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
207-487 |
2.13e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 98.35 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHR--GKELVVTALPLYHIFAlTMNCLLFIELGG------- 277
Cdd:PLN02430 221 DICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQFEDKmtHDDVYLSFLPLAHILD-RMIEEYFFRKGAsvgyyhg 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 ---------QNLLITNPRDIPGLVKELAKYPFTAMTGVNTL----FNALLN------NKEFQQLDFS------------- 325
Cdd:PLN02430 300 dlnalrddlMELKPTLLAGVPRVFERIHEGIQKALQELNPRrrliFNALYKyklawmNRGYSHKKASpmadflafrkvka 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 326 ----SLHLSAGGGMPVQQVVaERWVKLTG-QYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDDDNEVA 400
Cdd:PLN02430 380 klggRLRLLISGGAPLSTEI-EEFLRVTScAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRLEEVPEMGYD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 401 P-GEP--GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQ 476
Cdd:PLN02430 459 PlGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYGQ 538
|
330
....*....|.
gi 505808171 477 HSGVQEVAAVG 487
Cdd:PLN02430 539 NPIVEDIWVYG 549
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
201-553 |
4.11e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 97.02 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 201 PEIVADDLAFLQYTGGTTGVAKGAMLTHrNMLANLEQVNAT-YGplLHRGkELVVTALPLYHIFALTMNCLLFIELGGqn 279
Cdd:PRK13388 145 REVDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFAGRALTErFG--LTRD-DVCYVSMPLFHSNAVMAGWAPAVASGA-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 280 lLITNPRDIP--GLVKELAKYPFTAMTGVNTLFNALLNNKEfqQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGY 357
Cdd:PRK13388 219 -AVALPAKFSasGFLDDVRRYGATYFNYVGKPLAYILATPE--RPDDADNPLRVAFGNEASPRDIAEFSRRFGCQVEDGY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 358 GLTECSPLVSVNPhdiDYHSGSIGLPVPSTE----------AKLVDDDDNEVAPGEP--GELCIK-GPQVMLGYWQRPDA 424
Cdd:PRK13388 296 GSSEGAVIVVREP---GTPPGSIGRGAPGVAiynpetltecAVARFDAHGALLNADEaiGELVNTaGAGFFEGYYNNPEA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 425 TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAV-KIFVVK 503
Cdd:PRK13388 373 TAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVmAALVLR 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 505808171 504 KDAALTEEALITF--CRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK13388 453 DGATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
357-551 |
7.26e-20 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 92.36 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 357 YGLTE-CSPLVSVNPHDIDYHSGSIGLPVPstEAKLvddddnEVAPGEPGELCIKGPQVMLGYWqrPDATDeiiKDGWLH 435
Cdd:PRK07445 261 YGMTEtASQIATLKPDDFLAGNNSSGQVLP--HAQI------TIPANQTGNITIQAQSLALGYY--PQILD---SQGIFE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAALTEEALIT 515
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKT 407
|
170 180 190
....*....|....*....|....*....|....*....
gi 505808171 516 FCRRHLTGYKVPK---LVEfrdELPKSNVGKILRRELRD 551
Cdd:PRK07445 408 AIKDQLSPFKQPKhwiPVP---QLPRNPQGKINRQQLQQ 443
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
469-543 |
1.66e-19 |
|
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: 82.59 E-value: 1.66e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505808171 469 EIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV-KKDAALTEEALITFCRRHLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-561 |
2.80e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 88.42 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSgAAAIVIV 128
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC-KPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 129 SNFAHTLEKVVDKTQVKHVILTRmgdqlSTAKGTLVNFVVKY-----IKRLVPKYHLPDAISFRSALQHgYRMQYVKPEI 203
Cdd:PLN02654 199 CNAVKRGPKTINLKDIVDAALDE-----SAKNGVSVGICLTYenqlaMKREDTKWQEGRDVWWQDVVPN-YPTKCEVEWV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 204 VADDLAFLQYTGGTTGVAKGAMLTHRNML----------------------ANLEQVNA----TYGPLLHRGKELVVTAL 257
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMvytattfkyafdykptdvywctADCGWITGhsyvTYGPMLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 258 PLYhifaltmncllfielggqnllitnPRdiPGLVKELA-KYPFTAMTGVNTLFNALLNNKEFQQLDFS--SLHLSAGGG 334
Cdd:PLN02654 353 PNY------------------------PD--SGRCWDIVdKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 335 MPVQ--------QVVAER--------WVKLTGQYLLegygltecSPLVSVNPHDidyhSGSIGLPVPSTEAKLVDDDDNE 398
Cdd:PLN02654 407 EPINpsawrwffNVVGDSrcpisdtwWQTETGGFMI--------TPLPGAWPQK----PGSATFPFFGVQPVIVDEKGKE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 399 VAPGEPGELCIKGP-----QVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PLN02654 475 IEGECSGYLCVKKSwpgafRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESA 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 474 VMQHSGVQEVAAVGVPSGSSGEAVKIFVVKKDAA-LTEE---ALITFCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PLN02654 555 LVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVpYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
570
....*....|..
gi 505808171 550 RDEARAKVDNKG 561
Cdd:PLN02654 635 RKIASRQLDELG 646
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-551 |
6.00e-18 |
|
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: 87.02 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 50 TYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEhqlndsgaaaiVIVS 129
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG-----------FLLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 130 NFAHTLEKVVDKTQVKHVILTRmgdqLSTAKGTLVNfvvkyiKRLVPKYHLPDAISFRSALQHgyRMQYVKPEIVADDLA 209
Cdd:cd05905 85 TCKVRVALTVEACLKGLPKKLL----KSKTAAEIAK------KKGWPKILDFVKIPKSKRSKL--KKWGPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 210 FLQYTGGTTGVAKGAMLTHRNMLA---NLEQVNATYgpllhrGKELVVTALPLYHIFALTMNCLLFIELGGQNLLI---- 282
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAhcrALKEACELY------ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIppel 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 --TNPrdiPGLVKELAKYP-FTAMTGVNTLFNALLN---NKEFQQL---DFSSLH-LSAGGGMPVQQVVAERWVKLTGQy 352
Cdd:cd05905 227 mkTNP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDlssTLASLKNrdvNLSSLRmCMVPCENRPRISSCDSFLKLFQT- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 353 llEGYGLTECSPLVS-------------------------------VNPHDIDY-HSGSI---GLPVPSTEAKLVDDDD- 396
Cdd:cd05905 303 --LGLSPRAVSTEFGtrvnpficwqgtsgpepsrvyldmralrhgvVRLDERDKpNSLPLqdsGKVLPGAQVAIVNPETk 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 397 NEVAPGEPGELCIKGPQVMLGYWQRPDATDEIIKD-------------GWLHTGDI----------AVMDDEGFLRIVDR 453
Cdd:cd05905 381 GLCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnnSYARTGLLgflrptkctdLNVEEHDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 454 KKDMILVSGFNVYPNEIEDVVMQ-HSGVQEVAA----------VGVPSGSSGEAVKIFVVKKDAALTEEALITFCRrhlt 522
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRvHPYRGRCAVfsitglvvvvAEQPPGSEEEALDLVPLVLNAILEEHQVIVDCV---- 536
|
570 580
....*....|....*....|....*....
gi 505808171 523 gykvpKLVEfRDELPKSNVGKILRRELRD 551
Cdd:cd05905 537 -----ALVP-PGSLPKNPLGEKQRMEIRQ 559
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
206-511 |
9.70e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 86.82 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtygpLLHRGKELVVTA------LPLYHIFALTMNcLLFIELGG-- 277
Cdd:PLN02861 220 TDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDH----LLKVTDRVATEEdsyfsyLPLAHVYDQVIE-TYCISKGAsi 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 278 --------------QNLLITNPRDIP------------------GLVKELAKYPFTAMTG----------VNTLFNALLN 315
Cdd:PLN02861 295 gfwqgdirylmedvQALKPTIFCGVPrvydriytgimqkissggMLRKKLFDFAYNYKLGnlrkglkqeeASPRLDRLVF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 316 NKEFQQLDfSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIGLPVPSTEAKL--VD 393
Cdd:PLN02861 375 DKIKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLesVP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 394 DDDNEVAPGEP-GELCIKGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIE 471
Cdd:PLN02861 454 EMGYDALSDVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLE 533
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 505808171 472 DVVMQHSgvqEVAAVGVpSGSSGEAVKIFVVKKDAALTEE 511
Cdd:PLN02861 534 NTYSRCP---LIASIWV-YGNSFESFLVAVVVPDRQALED 569
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
24-461 |
3.04e-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: 84.81 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 24 SLVELFEHATTRYADQPAF--------------------INMGEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPN 83
Cdd:cd17632 23 RLAQIIATVMTGYADRPALgqratelvtdpatgrttlrlLPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 84 LLQYPVALFGILRAGmiAVNVnPLYT---PRELEHQLNDSGAAAI-VIVSNFAHTLEKVVDKTQVKHVI-------LTRM 152
Cdd:cd17632 103 SPDYATVDLALTRLG--AVSV-PLQAgasAAQLAPILAETEPRLLaVSAEHLDLAVEAVLEGGTPPRLVvfdhrpeVDAH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 153 GDQLSTAKGTLVNFVVKYIkrlvpkyhLPDAISFRSalQHGYRMQYVKPEIVADDLAFLQYTGGTTGVAKGAMLTHRNML 232
Cdd:cd17632 180 RAALESARERLAAVGIPVT--------TLTLIAVRG--RDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 233 ANLEQVNATYGPLLHRGkeLVVTALPLYHIfaltmncllfielGGQNLLITnprdipGLVKELAKYpFTAMTGVNTLFN- 311
Cdd:cd17632 250 TFWLKVSSIQDIRPPAS--ITLNFMPMSHI-------------AGRISLYG------TLARGGTAY-FAAASDMSTLFDd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 312 -ALLNNKE-----------FQQLDFSSLHLSAGGGMPV---QQVVAE-RWVKLTGQY----------------------- 352
Cdd:cd17632 308 lALVRPTElflvprvcdmlFQRYQAELDRRSVAGADAEtlaERVKAElRERVLGGRLlaavcgsaplsaemkafmeslld 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 353 --LLEGYGLTECSpLVSVNphdidyhsGSIGLPvPSTEAKLVDdddneVA---------PGEPGELCIKGPQVMLGYWQR 421
Cdd:cd17632 388 ldLHDGYGSTEAG-AVILD--------GVIVRP-PVLDYKLVD-----VPelgyfrtdrPHPRGELLVKTDTLFPGYYKR 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 505808171 422 PDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:cd17632 453 PEVTAEVFdEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLS 493
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
35-560 |
9.06e-17 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 83.00 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 35 RYADQPAFINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPlytprele 114
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQ-QGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 115 hQLNDSgaaaivivsnfahTLEKVVDKTQVKHVILTRMGDQLSTakgtlvnfvvkyikrLVPKYHLPDAISFRSALQHgy 194
Cdd:PRK09029 86 -QLPQP-------------LLEELLPSLTLDFALVLEGENTFSA---------------LTSLHLQLVEGAHAVAWQP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 195 rmqyvkpeivaDDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA--TYGP----LLhrgkelvvtALPLYHIfaltmn 268
Cdd:PRK09029 135 -----------QRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSlmPFTAqdswLL---------SLPLFHV------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 269 cllfielGGQnllitnprdipGLV-------KEL---AKYPFTAMTG-------VNTLFNALLNNKefqQLDFSSLHLSA 331
Cdd:PRK09029 189 -------SGQ-----------GIVwrwlyagATLvvrDKQPLEQALAgcthaslVPTQLWRLLDNR---SEPLSLKAVLL 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 332 GGGM-PV---QQVVA---ERWVkltgqylleGYGLTECSPLVSVNPhdIDYHSGsIGLPVPSTEAKLVDDddnevapgep 404
Cdd:PRK09029 248 GGAAiPVeltEQAEQqgiRCWC---------GYGLTEMASTVCAKR--ADGLAG-VGSPLPGREVKLVDG---------- 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 405 gELCIKGPQVMLGYWQ----RPdATDEiikDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK09029 306 -EIWLRGASLALGYWRqgqlVP-LVND---EGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLV 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 481 QEVAAVGVPSGSSGE---AvkifVVKKDAALTEEALITFCRRHLTGYKVPklVEF---RDELPKSNVgKILRRELRDEAR 554
Cdd:PRK09029 380 QQVFVVPVADAEFGQrpvA----VVESDSEAAVVNLAEWLQDKLARFQQP--VAYyllPPELKNGGI-KISRQALKEWVA 452
|
....*.
gi 505808171 555 AKVDNK 560
Cdd:PRK09029 453 QQLGNN 458
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
194-461 |
1.20e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 83.61 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 194 YRMQYVKPEIVADdlafLQYTGGTTGVAKGAMLTHRNMLANL-----EQVNATYGPLLHrgkelvVTALPLYHIFALTMN 268
Cdd:PTZ00342 296 YKIQNEDPDFITS----IVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTH------LSYLPISHIYERVIA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 269 CLLFIeLGGQnLLITNpRDIPGLVKELAKYPFTAMTGVNTLFNALLNN-----------------------KEFQQLDFS 325
Cdd:PTZ00342 366 YLSFM-LGGT-INIWS-KDINYFSKDIYNSKGNILAGVPKVFNRIYTNimteinnlpplkrflvkkilslrKSNNNGGFS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 326 SL-----HLSA---------------GGGMPVQQVVAERWVKLTGQYLlEGYGLTECSPLVSVNPHDiDYHSGSIGLPV- 384
Cdd:PTZ00342 443 KFlegitHISSkikdkvnpnlevilnGGGKLSPKIAEELSVLLNVNYY-QGYGLTETTGPIFVQHAD-DNNTESIGGPIs 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505808171 385 PSTEAKLVDDDDNEVAPGEP-GELCIKGPQVMLGYWQRPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PTZ00342 521 PNTKYKVRTWETYKATDTLPkGELLIKSDSIFSGYFLEKEQTKNaFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
46-552 |
5.61e-16 |
|
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: 80.55 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 46 GEVMTYRKLEERSRAFAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNplytprelehqLNDSGAAai 125
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN-----------YNLSGDP-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 vivsnFAHTLekvvdktqvkhviltrmgdQLSTAKgtlvnFVVkyikrlvpkyhlpdaisfrsalqhgyrmqyvkpeIVA 205
Cdd:cd05937 70 -----LIHCL-------------------KLSGSR-----FVI----------------------------------VDP 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 206 DDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYgplLHRGKEL-VVTALPLYHIFAL---TMNCLLfielGGQNLL 281
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVT-SNLLSHD---LNLKNGDrTYTCMPLYHGTAAflgACNCLM----SGGTLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 282 ITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGM--PVQQVVAERW-VKLTGQYllegYG 358
Cdd:cd05937 159 LSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLrpDIWERFRERFnVPEIGEF----YA 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 359 LTEcSPLVSVNPHDIDYHSGSIGL--------------PV---PSTEAKLVDDDDN--EVAP-GEPGELCIKGPQVML-- 416
Cdd:cd05937 235 ATE-GVFALTNHNVGDFGAGAIGHhglirrwkfenqvvLVkmdPETDDPIRDPKTGfcVRAPvGEPGEMLGRVPFKNRea 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 417 --GYWQRPDATD-EIIK------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVG 487
Cdd:cd05937 314 fqGYLHNEDATEsKLVRdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYG 393
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505808171 488 VP-SGSSGEAVKIFVVKKDAALTEEALI-----TFCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:cd05937 394 VKvPGHDGRAGCAAITLEESSAVPTEFTksllaSLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
38-546 |
3.31e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 65.92 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 38 DQPA------FINMGEVMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPR 111
Cdd:PTZ00237 76 DQDAliyecpYLKKTIKLTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 112 ELEHQLnDSGAAAIVIVSNFAHTLEKVVDKT-QVKHVIltrmgdQLSTAKGTLV-----NFVV-----KYIKRLVPkyhL 180
Cdd:PTZ00237 155 SLIDRI-ETITPKLIITTNYGILNDEIITFTpNLKEAI------ELSTFKPSNVitlfrNDITsesdlKKIETIPT---I 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 181 PDAISFRSALQHgYRMQYVKP--EIVADDLA---FLQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLLHRGKELVVt 255
Cdd:PTZ00237 225 PNTLSWYDEIKK-IKENNQSPfyEYVPVESShplYILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVV- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 256 aLPLYHIFALTMNCLLFIELGGQNLL------ITNPRDIP-GLVKELAKYPFT-AMTGVNTLFNALLNNKEFQQL----D 323
Cdd:PTZ00237 300 -FSHSSIGWVSFHGFLYGSLSLGNTFvmfeggIIKNKHIEdDLWNTIEKHKVThTLTLPKTIRYLIKTDPEATIIrskyD 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 324 FSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTE--CSPLVSVNPHDIDYHSgsIGLPVPSTEAKLVDDDDNEVAP 401
Cdd:PTZ00237 379 LSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEigITYLYCYGHINIPYNA--TGVPSIFIKPSILSEDGKELNV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 402 GEPGELCIK---GPQVMLGYWQRpdatDEIIKD------GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIED 472
Cdd:PTZ00237 457 NEIGEVAFKlpmPPSFATTFYKN----DEKFKQlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIET 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 473 VVMQHSGVQEVAAVGVPSGSSGEA-VKIFVVKKDAALTEEALITF-------CRRHLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PTZ00237 533 SILKHPLVLECCSIGIYDPDCYNVpIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKI 612
|
..
gi 505808171 545 LR 546
Cdd:PTZ00237 613 PR 614
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
320-480 |
4.27e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 55.54 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 320 QQLDFSSLHLSAG--GGMPV----QQVVAERW-VKLtgqylLEGYGLTECSPLVSVNPHDIDyhsgsiGLPVPS----TE 388
Cdd:COG1541 196 EGIDPRDLSLKKGifGGEPWseemRKEIEERWgIKA-----YDIYGLTEVGPGVAYECEAQD------GLHIWEdhflVE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 389 akLVDDDDNE-VAPGEPGELCI----KGPQVMLGYwqrpdatdeiikdgwlHTGDIAVMDDEG---------FLRIVDRK 454
Cdd:COG1541 265 --IIDPETGEpVPEGEEGELVVttltKEAMPLIRY----------------RTGDLTRLLPEPcpcgrthprIGRILGRA 326
|
170 180
....*....|....*....|....*.
gi 505808171 455 KDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:COG1541 327 DDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
204-539 |
5.07e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 55.88 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 204 VADDLAFLQYTG-GTTGVAKgAMLTHRNMLANLEQVNATYgplLHRGkELVVTALPLYHIFALtMNCLLFIELGGQNLLI 282
Cdd:PRK07868 604 LARDLAFIAFSTaGGELVAK-QITNYRWALSAFGTASAAA---LDRR-DTVYCLTPLHHESGL-LVSLGGAVVGGSRIAL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 283 TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPvqqvvAERWVKLTGQY----LLEGYG 358
Cdd:PRK07868 678 SRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMP-----TGLWERVVEAFapahVVEFFA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 359 LTECSP-LVSVNPHDIdyhsGSIGLPVPST-----------EAKLVDDDDNEVAPGEPGElcikgPQVMLGYWQRP-DAT 425
Cdd:PRK07868 753 TTDGQAvLANVSGAKI----GSKGRPLPGAgrvelaaydpeHDLILEDDRGFVRRAEVNE-----VGVLLARARGPiDPT 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 426 DEIIK------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKI 499
Cdd:PRK07868 824 ASVKRgvfapaDTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQLAVAA 903
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 505808171 500 FVVKKDAALTEEALITFCRRHLTGYKvPKLVEFRDELPKS 539
Cdd:PRK07868 904 VTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLS 942
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
10-545 |
1.45e-06 |
|
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: 51.12 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 10 PADVPAEINPDryqslVELFEHATTRYADQ---------PAFINMGE-----VMTYRKLEERSRAFAAYLQQgLGLQKGD 75
Cdd:cd05943 51 VVVVSGRIMPG-----ARWFPGARLNYAENllrhadaddPAAIYAAEdgertEVTWAELRRRVARLAAALRA-LGVKPGD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 76 RVALMMPNLLQYPVALFGILRAGMIAVNVNPlytprelehqlnDSGAAAI----------VIVSNFAHTLE-KVVDKTQV 144
Cdd:cd05943 125 RVAGYLPNIPEAVVAMLATASIGAIWSSCSP------------DFGVPGVldrfgqiepkVLFAVDAYTYNgKRHDVREK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 145 KHVILTRMGDQLSTakgTLVNFVVKYIKRLVPKYhlPDAISFRSALQHGyrmQYVKPEIV---ADDLAFLQYTGGTTGVA 221
Cdd:cd05943 193 VAELVKGLPSLLAV---VVVPYTVAAGQPDLSKI--AKALTLEDFLATG---AAGELEFEplpFDHPLYILYSSGTTGLP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 222 KGAmlthrnmlanleqVNATYGPLLHRGKELVVtalplyH--------IFALT-----M-NCLLFIELGGQNLLITN--- 284
Cdd:cd05943 265 KCI-------------VHGAGGTLLQHLKEHIL------HcdlrpgdrLFYYTtcgwmMwNWLVSGLAVGATIVLYDgsp 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 285 ----PRDIPGLVKELAkypfTAMTGVNTLFNALLNNKEFQQ---LDFSSLH--LSAGGGMPVQQVvaeRWV--KLTGQYL 353
Cdd:cd05943 326 fypdTNALWDLADEEG----ITVFGTSAKYLDALEKAGLKPaetHDLSSLRtiLSTGSPLKPESF---DYVydHIKPDVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 354 LEGY-GLTE-CSPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDDDNEVaPGEPGEL-CIKG-PQVMLGYWQRPDATD--- 426
Cdd:cd05943 399 LASIsGGTDiISCFVGGNP-LLPVYRGEIQCRGLGMAVEAFDEEGKPV-WGEKGELvCTKPfPSMPVGFWNDPDGSRyra 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 427 ---EIIKDGWLHtGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVQEVAAVGVPSGSSGEAVKIFVV- 502
Cdd:cd05943 477 ayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKl 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 505808171 503 KKDAALTEE---ALITFCRRHLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:cd05943 556 REGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
153-549 |
1.95e-06 |
|
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: 50.55 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 153 GDQLSTAKGTLVNFVVkYIKRL--VPKYHLPDAISFRSALQHGyrmqyvkpeivaddLAFLQYTGGTTGVAKGAMLTHRN 230
Cdd:cd17654 78 QRSLTVMKKCHVSYLL-QNKELdnAPLSFTPEHRHFNIRTDEC--------------LAYVIHTSGTTGTPKIVAVPHKC 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 231 MLANLEQVNATYGplLHRGKELVVTALPLYHIFALTmnclLFIELGGQNLLITNPRDIPGLVKELAKYPF-----TAMTG 305
Cdd:cd17654 143 ILPNIQHFRSLFN--ITSEDILFLTSPLTFDPSVVE----IFLSLSSGATLLIVPTSVKVLPSKLADILFkrhriTVLQA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 306 VNTLFNALLN--NKEFQQLDFSSLHLSAGGGMP-VQQVVAERWV-KLTGQYLLEGYGLTECSPLVSVNPHDIDYHSGSIG 381
Cdd:cd17654 217 TPTLFRRFGSqsIKSTVLSATSSLRVLALGGEPfPSLVILSSWRgKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 382 LPVPSTEAKLVDDDDNEVApgepGELCIKGpQVMLGYWQRPDATdeiIKDGWLHTGDIaVMDDEGFLRIVDRKKDMILVS 461
Cdd:cd17654 297 SPLLGTVIEVRDQNGSEGT----GQVFLGG-LNRVCILDDEVTV---PKGTMRATGDF-VTVKDGELFFLGRKDSQIKRR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 462 GFNVYPNEIEDVVMQHSGVQEVAAvgvpSGSSGEAVKIFVVkkdaaLTEEALITFCRRHLTG---YKVPKLVEFRDELPK 538
Cdd:cd17654 368 GKRINLDLIQQVIESCLGVESCAV----TLSDQQRLIAFIV-----GESSSSRIHKELQLTLlssHAIPDTFVQIDKLPL 438
|
410
....*....|.
gi 505808171 539 SNVGKILRREL 549
Cdd:cd17654 439 TSHGKVDKSEL 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
29-228 |
2.64e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.18 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 29 FEHATTRYA---------DQPAFINMGE-----VMTYRKLEERSRAFAAYLQQgLGLQKGDRVALMMPNLlqyPVALFGI 94
Cdd:PRK03584 81 FPGARLNYAenllrhrrdDRPAIIFRGEdgprrELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNI---PETVVAM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 95 LRA---GMIAVNVNPlytprelehqlnDSGAAAIV-----------IVSNFAHTLEKVVDKTQVkhviLTRMGDQLSTAK 160
Cdd:PRK03584 157 LATaslGAIWSSCSP------------DFGVQGVLdrfgqiepkvlIAVDGYRYGGKAFDRRAK----VAELRAALPSLE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 161 GTLvnfVVKYIKRLVPKYHLPDAISFRSALQHgyrmqYVKPEIVADDLAF-----LQYTGGTTGVAK-------GAMLTH 228
Cdd:PRK03584 221 HVV---VVPYLGPAAAAAALPGALLWEDFLAP-----AEAAELEFEPVPFdhplwILYSSGTTGLPKcivhghgGILLEH 292
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
392-480 |
4.50e-06 |
|
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: 49.16 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 392 VDDDDNE-VAPGEPGELCIK------GPqvMLGYWqrpdatdeiikdgwlhTGDIAVMDDEG---------FLRIVDRKK 455
Cdd:cd05913 262 IDPETGEpVPPGEVGELVFTtltkeaMP--LIRYR----------------TRDITRLLPGPcpcgrthrrIDRITGRSD 323
|
90 100
....*....|....*....|....*
gi 505808171 456 DMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:cd05913 324 DMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
49-552 |
1.05e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 48.54 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 49 MTYRKLEERSRAfAAYLQQGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDSGAAAI--- 125
Cdd:PLN03052 209 MTLSELRSQVSR-VANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 126 -VIV-SNFAHTL-EKVVDKTQVKHVILTRMGDQLSTakgTLVNFVVKYIKRLVPKYHLPDAISFRSALQHgyrmqyvkpe 202
Cdd:PLN03052 288 dVIVrGGKSIPLySRVVEAKAPKAIVLPADGKSVRV---KLREGDMSWDDFLARANGLRRPDEYKAVEQP---------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 203 ivADDLAFLQYTGGTTGVAKGAMLTHRNML-------ANLE-QVNATY----------GPLLHRGKELVVTALPLYHIFA 264
Cdd:PLN03052 355 --VEAFTNILFSSGTTGEPKAIPWTQLTPLraaadawAHLDiRKGDIVcwptnlgwmmGPWLVYASLLNGATLALYNGSP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 265 LTMNCLLFIELGGQNLLITnprdIPGLVKelakypftamTGVNTlfNALLNnkefqqLDFSSLHL--SAGGGMPVQQVVa 342
Cdd:PLN03052 433 LGRGFAKFVQDAKVTMLGT----VPSIVK----------TWKNT--NCMAG------LDWSSIRCfgSTGEASSVDDYL- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 343 erWVKLTGQY--LLEGYGLTEC-SPLVS---VNPHDIdyhsGSIGLPVPSTEAKLVDDDDNEVAPGEP--GELCIkGPQv 414
Cdd:PLN03052 490 --WLMSRAGYkpIIEYCGGTELgGGFVTgslLQPQAF----AAFSTPAMGCKLFILDDSGNPYPDDAPctGELAL-FPL- 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 415 MLG-------------YWQ-RPDATDEIIKDgwlHtGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HSG 479
Cdd:PLN03052 562 MFGasstllnadhykvYFKgMPVFNGKILRR---H-GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAaDES 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 480 VQEVAAVGVPSGSSG-EAVKIFVVKKD----AALTEEALITFCR---RHLTG-YKVPKLVEFrDELPKSNVGKILRRELR 550
Cdd:PLN03052 638 VLETAAIGVPPPGGGpEQLVIAAVLKDppgsNPDLNELKKIFNSaiqKKLNPlFKVSAVVIV-PSFPRTASNKVMRRVLR 716
|
..
gi 505808171 551 DE 552
Cdd:PLN03052 717 QQ 718
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
437-554 |
2.15e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 47.12 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505808171 437 GDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ-HSGVQEVAAVGV-PSGSSGEAVKIFVVKKDAALT----- 509
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVaPPDGGPELLVIFLVLGEEKKGfdqar 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 505808171 510 EEALITFCRRHLTG-----YKVPKlVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PLN03051 442 PEALQKKFQEAIQTnlnplFKVSR-VKIVPELPRNASNKLLRRVLRDQLK 490
|
|
| |
