|
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: 1246.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 1 MKKVWLNRYPADVPAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALM 80
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAK 160
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 161 GTLVNFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 241 TYGPLLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQ 320
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 321 QLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVP 400
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 401 HGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 481 LEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 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: 900.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 1 MKKVWLNRYPADVPAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALM 80
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQ-SRGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLStAK 160
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLG-FK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 161 GTLVNFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK07059 159 GHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 241 TYGPLL----HPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN 316
Cdd:PRK07059 239 WLQPAFekkpRPDQLNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 317 KEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDED 396
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 397 NEVPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMtADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 476 QHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 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: 819.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 5 WLNRYPADVPAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNL 84
Cdd:PRK05677 6 WKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK05677 86 LQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLKRLLI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 165 NFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGP 244
Cdd:PRK05677 166 NAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 245 LLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDF 324
Cdd:PRK05677 246 NLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 325 STLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEP 404
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 405 GELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEV 483
Cdd:PRK05677 405 GELCVKGPQVMKGYWQRPEATDEILdSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQC 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 484 AAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 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: 774.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 5 WLNRYPADVPAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNL 84
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 165 NFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN---AT 241
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHqwlAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 242 YGPLLhPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ 321
Cdd:PRK08751 247 TGKLE-EGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 322 LDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPH 401
Cdd:PRK08751 326 IDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 402 GEPGELCVRGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK08751 406 GEIGELCIKGPQVMKGYWKRPEETAKVMDaDGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGV 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956626 481 LEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 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: 735.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 5 WLNRYPADVPAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNL 84
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLV 164
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 165 NFVVKYVKRLVPKYHLPDAISFRRALHAGyRMQYVKPEIVS-EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG 243
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQG-RGLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 244 -------PLLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN 316
Cdd:PRK12492 245 qlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 317 KEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDED 396
Cdd:PRK12492 325 PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 397 NEVPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALdAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 476 QHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 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: 718.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 25 LIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 105 NPLYTPRELEHQLNDSGAAAIVIvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdAI 184
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 185 SFRRALHAGYRMQYvKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLlHPGKELVITALPLYHIFA 264
Cdd:cd05936 105 SFTDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDL-LEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 265 LTMNCLLFIELGGQNVLITNPRDIpGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAER 344
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 WVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDA 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 425 TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKK 504
Cdd:cd05936 342 TAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLK 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489956626 505 D-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 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: 574.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 25 LIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 105 NPLYTPRELEHQLNDSGAAAIVIvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdai 184
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 185 sfrralhagyrmqyvkpeivsedlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVITALPLYHIFA 264
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPG-DVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 265 LTMNCLLFIELGGQNVLITNpRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAER 344
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 WVKLTGQYLLEGYGLTECAPLVSVNPHDIDY-HSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPD 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPGErRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 424 ATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVK 503
Cdd:COG0318 315 ATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVL 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489956626 504 KD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:COG0318 395 RPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-552 |
1.82e-171 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 497.60 E-value: 1.82e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 3 KVWLNRYPADVPAEINPDRyQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMP 82
Cdd:PRK05605 13 KPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 83 NLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGT 162
Cdd:PRK05605 91 NCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 163 LVNFVVKYVKRLVPKYH--LPDAISFRRALHA---GYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ 237
Cdd:PRK05605 171 ALRLPIPALRKARAALTgpAPGTVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 238 VNAtYGPLLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNK 317
Cdd:PRK05605 251 GKA-WVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 318 EFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDED- 396
Cdd:PRK05605 329 EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDp 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 397 -NEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK05605 409 dETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 476 QHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-552 |
2.22e-153 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 449.35 E-value: 2.22e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAA-LGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKT-QVKHVILTRMGDqlstakgtlvnfvvkyvkrlvPKYHLP 181
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVICETEE---------------------DDPHTE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 182 DAISFRRALHAGYRmQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhPGKELVITALPLYH 261
Cdd:PRK07656 143 KMKTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADW-AEYLGL--TEGDRYLAANPFFH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 262 IFALT--MN-CLLfielGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGG--MP 336
Cdd:PRK07656 219 VFGYKagVNaPLM----RGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 337 VqqAVAERWVKLTG-QYLLEGYGLTECAPLVSVNPHDID--YHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQ 413
Cdd:PRK07656 295 V--ALLERFESELGvDIVLTGYGLSEASGVTTFNRLDDDrkTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 414 VMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGS 492
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDaDGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 493 SGEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07656 453 LGEVGKAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-551 |
7.67e-148 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 435.38 E-value: 7.67e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 20 DRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQ-VKHVILtrMGDqlsTAKGTLVNFVVKYVkrlvpky 178
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIV--EGD---GPAAPLAPEVGEYE------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 179 hlpdaisfrrALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtyGPLLHPgKELVITALP 258
Cdd:PRK06187 150 ----------ELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCA--WLKLSR-DDVYLVIVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 259 LYHIFALTMnCLLFIELGGQNVLItnPRDIPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPV 337
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVIP--RRFDPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 338 QQAVAERWVKLTGQYLLEGYGLTECAPLVSVNP---HDIDY--HSGSIGLPVPSTEAKLVDDEDNEVPH--GEPGELCVR 410
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQGYGMTETSPVVSVLPpedQLPGQwtKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 411 GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPS 490
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956626 491 GSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK06187 454 EKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-560 |
8.25e-146 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 431.76 E-value: 8.25e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 1 MKKVWLNRYPADVPAEINPDrYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALM 80
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTISYD-IQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 81 MPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAK 160
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 161 GTLVNFVVKYVKRLVPKYHLPDAI----SFRRALHAGYRMQyVKPEivsEDLAFLQYTGGTTGVAKGAMLTHRNMLAN-L 235
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIhlwnSVEKEVNTGVEVP-CDPE---NDLALLQYTGGTTGFPKGVMLTHKNLVSNtL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 236 EQVNATYGplLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLItnPR-DIPGLVKELAKYPFTAMTGVNTLFNALL 314
Cdd:PRK06710 237 MGVQWLYN--CKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 315 NNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDD 394
Cdd:PRK06710 313 NSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 395 EDNEV-PHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PRK06710 393 ETGEAlPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 474 VMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06710 473 LYEHEKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
....*...
gi 489956626 553 ARAKVDNK 560
Cdd:PRK06710 553 EKRKNEDE 560
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-546 |
7.97e-144 |
|
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: 422.02 E-value: 7.97e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 29 FEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLY 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 109 TPRELEHQLNDSGAAAIVivsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrr 188
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 189 alhagyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVITALPLYHIFALTMN 268
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL---GPDDVLLVVAPLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 269 CLLFIELGGQNVLITNPRdiPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWvK 347
Cdd:cd17631 158 TLPTLLRGGTVVILRKFD--PETVLDLiERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRAL-Q 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 348 LTGQYLLEGYGLTECAPLVSVNPH-DIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATD 426
Cdd:cd17631 235 ARGVKFVQGYGMTETSPGVTFLSPeDHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 427 EIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDP 506
Cdd:cd17631 315 AAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489956626 507 S-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17631 395 AeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
29-461 |
3.97e-139 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 409.39 E-value: 3.97e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 29 FEHSVRRYADQPAFVNM-GEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 108 YTPRELEHQLNDSGAAAIVIVSNFahTLEKVVEKTQ-VKHVILTRMGDQLSTAKGTLVNFVVKYVKRLVPKYHLPDAisf 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVI-TALPLYHIFAL 265
Cdd:pfam00501 155 -------------------DDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVlSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 266 TMNCLLFIELGGQNVLI--TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAE 343
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHS--GSIGLPVPSTEAKLVDDED-NEVPHGEPGELCVRGPQVMLGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRslGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 489956626 421 RPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:pfam00501 376 DPELTAEaFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
24-556 |
3.13e-133 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 398.95 E-value: 3.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVN 103
Cdd:PRK08314 11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 104 VNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLStAKGTLVNFVVKYVKRLVPKYHLPDA 183
Cdd:PRK08314 91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLP-AEPEIAVPAWLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 184 ISFRRALHAGYRmqyvkPEIV---SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGkELVITALPLY 260
Cdd:PRK08314 170 VAWKEALAAGLA-----PPPHtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA--VGSVLWSNSTPE-SVVLAVLPLF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 261 HI--FALTMNCLLFieLGGQNVLITN-PRDIPGLVkeLAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPV 337
Cdd:PRK08314 242 HVtgMVHSMNAPIY--AGATVVLMPRwDREAAARL--IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 338 QQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDED-NEVPHGEPGELCVRGPQVML 416
Cdd:PRK08314 318 PEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD-RPKLQCLGIPTFGVDARVIDPETlEELPPGEVGEIVVHGPQVFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 417 GYWQRPDATDE--IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGS 492
Cdd:PRK08314 397 GYWNRPEATAEafIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPR 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 493 SGEAVKIFVVKKDPS---LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK08314 477 RGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-545 |
9.55e-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: 395.43 E-value: 9.55e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAaI 125
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPK-V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNfaHTLEKVVEKTQ----VKHVILTRMGDQLSTAKGTLVNFVVKYVKRLVPKYhlpdaisfrralhagyrmqyvkP 201
Cdd:cd05911 86 IFTDP--DGLEKVKEAAKelgpKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPP----------------------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 202 EIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVITALPLYHIFAL--TMNCLLFielgGQN 279
Cdd:cd05911 142 KDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGS-NDVILGFLPLYHIYGLftTLASLLN----GAT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 280 VLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQ-YLLEGYG 358
Cdd:cd05911 217 VIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 359 LTECAPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDEDNE-VPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHT 436
Cdd:cd05911 297 MTETGGILTVNP-DGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFdEDGWLHT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 437 GDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEDALIT 515
Cdd:cd05911 376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTEKEVKD 455
|
490 500 510
....*....|....*....|....*....|...
gi 489956626 516 FCRRQLTGYKvpKL---VEFRDELPKSNVGKIL 545
Cdd:cd05911 456 YVAKKVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
14-552 |
2.89e-123 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 372.73 E-value: 2.89e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 14 PAEINPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLvnfvvkyvkr 173
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 174 lvpkyhlpdaiSFRRALHAGYRMQyVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvnatYGPLLHPGK--- 250
Cdd:PRK08316 151 -----------DFADWAEAGSVAE-PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAE-------YVSCIVAGDmsa 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 251 -ELVITALPLYHIFALTMNCLLFIELGGQNVLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHL 329
Cdd:PRK08316 212 dDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 330 SAGGG--MPVQ--QAVAERwvkLTGQYLLEGYGLTECAPLVSV-NPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEP 404
Cdd:PRK08316 291 GYYGAsiMPVEvlKELRER---LPGLRFYNCYGQTEIAPLATVlGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 405 GELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVA 484
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 485 AVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK08316 448 VIGLPDPKWIEAVTAVVVpKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-545 |
5.19e-119 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 355.05 E-value: 5.19e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVITALPLYHIFAltMNCLLFIELGGQNVLITNPR 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGL---TEGDVFLSTLPLFHIGG--LFGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLV 366
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 367 SVN-PHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDE 445
Cdd:cd04433 156 ATGpPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 446 GFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPS-LTEDALITFCRRQLTGY 524
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAPY 315
|
330 340
....*....|....*....|.
gi 489956626 525 KVPKLVEFRDELPKSNVGKIL 545
Cdd:cd04433 316 KVPRRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-549 |
7.75e-117 |
|
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: 355.39 E-value: 7.75e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 33 VRRYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTP 110
Cdd:cd05904 15 ASAHPSRPALIDaaTGRALTYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 111 RELEHQLNDSGAAAIVIVSnfahtleKVVEKTQvkhviltrmgdqlstakgtlvNFVVKYVkrLVPKYHLpDAISFRRAL 190
Cdd:cd05904 94 AEIAKQVKDSGAKLAFTTA-------ELAEKLA---------------------SLALPVV--LLDSAEF-DSLSFSDLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 191 HAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVITALPLYHIFALTMNCL 270
Cdd:cd05904 143 FEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSE-DVFLCVLPMFHIYGLSSFAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 271 LFIELGGQNVLItnPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLH-LSAGG---GMPVQQAVAER- 344
Cdd:cd05904 222 GLLRLGATVVVM--PRfDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRqIMSGAaplGKELIEAFRAKf 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 -WVKLtgqylLEGYGLTECAPLVSV--NPHDIDYHSGSIGLPVPSTEAKLVDDEDNEV-PHGEPGELCVRGPQVMLGYWQ 420
Cdd:cd05904 300 pNVDL-----GQGYGMTESTGVVAMcfAPEKDRAKYGSVGRLVPNVEAKIVDPETGESlPPNQTGELWIRGPSIMKGYLN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 421 RPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKI 499
Cdd:cd05904 375 NPEATAAtIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMA 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489956626 500 FVVKK-DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05904 455 FVVRKpGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-553 |
1.11e-113 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 349.34 E-value: 1.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 5 WLNRYPADVPAEIN-PDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLqEGLGLQKGDRVALMMPN 83
Cdd:PRK06178 14 QQAAWPAGIPREPEyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALL-RQRGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 84 LLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTL 163
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 164 VNFVVKyvkrlVPKYHLPDAISFRRALHA-GYRMQYVKPEIvsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATY 242
Cdd:PRK06178 173 LPDSLR-----APRLAAAGAIDLLPALRAcTAPVPLPPPAL--DALAALNYTGGTTGMPKGCEHTQRDMVYTA----AAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 243 GPLLHPGKE--LVITALPLYHIfALTMNCLLF-IELGGQNVLITnpR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKE 318
Cdd:PRK06178 242 YAVAVVGGEdsVFLSFLPEFWI-AGENFGLLFpLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVDNAVELMDHPR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 319 FQQLDFSTL-HLSAGGGM-PVQQAVAERWVKLTGQYLLEG-YGLTE---CAPLVS-VNPHDIDYHSGSI--GLPVPSTEA 389
Cdd:PRK06178 319 FAEYDLSSLrQVRVVSFVkKLNPDYRQRWRALTGSVLAEAaWGMTEthtCDTFTAgFQDDDFDLLSQPVfvGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 390 KLVDDEDNE-VPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPN 468
Cdd:PRK06178 399 KICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 469 EIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKlVEFRDELPKSNVGKILRR 547
Cdd:PRK06178 479 EVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQ 557
|
....*.
gi 489956626 548 ELRDEA 553
Cdd:PRK06178 558 DLQALA 563
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-553 |
1.04e-106 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 331.01 E-value: 1.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPA--FVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPN-----LLQYPVAlfgilRAGM 99
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLA-LGIEKGDRVGIWAPNvpewvLTQFATA-----KIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFahtlekvveKTQVKHVILTRMGDQLSTAK-GTLVNFVVKYVKRLV--- 175
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAADGF---------KDSDYVAMLYELAPELATCEpGQLQSARLPELRRVIflg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 176 -PKYhlPDAISFRRALHAGYRMQYVKPEIVSEDLAF-----LQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPG 249
Cdd:PRK08315 165 dEKH--PGMLNFDELLALGRAVDDAELAARQATLDPddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMK--LTEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 250 KELVITaLPLYHIFALTMNCLLFIELGGQNVLITNPRDiPGLV-KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLH 328
Cdd:PRK08315 241 DRLCIP-VPLYHCFGMVLGNLACVTHGATMVYPGEGFD-PLATlAAVEEERCTALYGVPTMFIAELDHPDFARFDLSSLR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 --LSAGGGMPVQqaVAERWVKLtgQYLLE---GYGLTECAPlVSV--NPHD-IDYHSGSIGLPVPSTEAKLVDDEDNE-V 399
Cdd:PRK08315 319 tgIMAGSPCPIE--VMKRVIDK--MHMSEvtiAYGMTETSP-VSTqtRTDDpLEKRVTTVGRALPHLEVKIVDPETGEtV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 400 PHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:PRK08315 394 PRGEQGELCTRGYSVMKGYWNDPEKTAEAIdADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 479 GVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK08315 474 KIQDVQVVGVPDEKYGEEVCAWIIlRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMM 549
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-549 |
1.06e-105 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 324.05 E-value: 1.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIV 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 129 SNFahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivsEDL 208
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVITALPLYHIFALTMNCLLFIELGGQNVLITNpRDI 288
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG--LTPS-DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-WDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 289 PGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSV 368
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 369 NPHdIDYHSGSIGLPVPSTEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKDG---WLHTGDIAVMD 443
Cdd:cd05935 243 NPP-LRPKLQCLGIP*FGVDARVIDIETGrELPPNEVGEIVVRGPQIFKGYWNRPEETEEsFIEIKgrrFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDP---SLTEDALITFCRRQ 520
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....*....
gi 489956626 521 LTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
27-556 |
1.89e-102 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 320.14 E-value: 1.89e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:COG0365 13 NCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRA-LGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 102 VNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVIltrmgDQLSTAKGTLVnfvvkyVKRLVPKYHLP 181
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEAL-----EELPSLEHVIV------VGRTGADVPME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 182 DAISFRRALHAGyrMQYVKPEIV-SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPL---LHPGkELVITAL 257
Cdd:COG0365 161 GDLDWDELLAAA--SAEFEPEPTdADDPLFILYTSGTTGKPKGVVHTHGGYLVHA----ATTAKYvldLKPG-DVFWCTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 258 PLYHIFALTmNCLLFIELGGQNVLI----TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSTLHLSA 331
Cdd:COG0365 234 DIGWATGHS-YIVYGPLLNGATVVLyegrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 332 GGGMPVQQAVAERWVKLTGQYLLEGYGLTE-CAPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR 410
Cdd:COG0365 313 SAGEPLNPEVWEWWYEAVGVPIVDGWGQTEtGGIFIS-NLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 411 GPQ--VMLGYWQRPDATDEIIKD---GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAA 485
Cdd:COG0365 392 GPWpgMFRGYWNDPERYRETYFGrfpGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAV 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956626 486 VGVPSGSSGEAVKIFVV-KKDPSLTED---ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:COG0365 472 VGVPDEIRGQVVKAFVVlKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
30-554 |
6.78e-101 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 314.11 E-value: 6.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 30 EHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYT 109
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 110 PRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVIltRMGDQLSTAKGTLVNFVVKyvkrlvpkyhlpdaisfrra 189
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVI--SITSLKEIEDRKIDNFVEK-------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 190 lhagyrmqyvkpeivSEDLAFLQ-YTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLHpGKELVITALPLYHIFALTMN 268
Cdd:PRK06839 147 ---------------NESASFIIcYTSGTTGKPKGAVLTQENMFWN--ALNNTFAIDLT-MHDRSIVLLPLFHIGGIGLF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 269 CLLFIELGGQnVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGG----MPVQQAVAER 344
Cdd:PRK06839 209 AFPTLFAGGV-IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 wvkltGQYLLEGYGLTECAPLV-SVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPD 423
Cdd:PRK06839 288 -----GFLFGQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPD 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 424 ATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVK 503
Cdd:PRK06839 363 ATEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVK 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489956626 504 KD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PRK06839 443 KSsSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
19-553 |
2.43e-98 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 309.40 E-value: 2.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 19 PDRYQSLIELFEHSVRRYADQPAFV--NMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLL-ALGVQPGDRVGIWAPNCAEWLLTQFATAR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 97 AGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFahtlekvveKTQVKHVILTRMGDQL-STAKGTLVN-------FVV 168
Cdd:PRK12583 93 IGAILVNINPAYRASELEYALGQSGVRWVICADAF---------KTSDYHAMLQELLPGLaEGQPGALACerlpelrGVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 169 KYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHP 248
Cdd:PRK12583 164 SLAPAPPPGFLAWHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 249 GKELVItALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLH 328
Cdd:PRK12583 242 HDRLCV-PVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 LSAGGGMPVQQAVAERWVK-LTGQYLLEGYGLTECAPLV--SVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPG 405
Cdd:PRK12583 321 TGIMAGAPCPIEVMRRVMDeMHMAEVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 406 ELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVA 484
Cdd:PRK12583 401 ELCTRGYSVMKGYWNNPEATAESIdEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQ 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 485 AVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK12583 481 VFGVPDEKYGEEIVAWVRlHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-550 |
3.40e-97 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 305.37 E-value: 3.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEER-SRAFAAYlqEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVN 105
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRiSRYIQAF--EALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 106 PLYTPRELEHQLNDSGAAAIVIVSNfahtleKVVEKTQVkhvILTRmgdqlstakgtlvnfvVKYVKRLVPKYHLPDAIS 185
Cdd:PRK06188 94 PLGSLDDHAYVLEDAGISTLIVDPA------PFVERALA---LLAR----------------VPSLKHVLTLGPVPDGVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 186 FRrALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVITalPLYHIFAL 265
Cdd:PRK06188 149 LL-AAAAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADP-RFLMCT--PLSHAGGA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 266 TMNCLLFieLGGQNVLIT--NPRDIPGLVKElakYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAE 343
Cdd:PRK06188 225 FFLPTLL--RGGTVIVLAkfDPAEVLRAIEE---QRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RWVKLTGQYLLEGYGLTECAPLVSVNP---HDID--YHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGY 418
Cdd:PRK06188 300 EAIERFGPIFAQYYGQTEAPMVITYLRkrdHDPDdpKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 419 WQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK 498
Cdd:PRK06188 380 WNRPEETAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVT 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 499 IFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK06188 460 AVVVlRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-550 |
4.99e-97 |
|
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: 301.52 E-value: 4.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIvs 129
Cdd:cd05934 5 TYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 nfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivseDLA 209
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLaNLEQVNATYGPLlhPGKELVITALPLYHIFALTMNCLLFIELGGQNVLItnPRDIP 289
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLT-FAGYYSARRFGL--GEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 290 -GLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQ--QAVAERWvkltGQYLLEGYGLTEcAPLV 366
Cdd:cd05934 160 sRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPElhEEFEERF----GVRLLEGYGMTE-TIVG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 367 SVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR---GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMD 443
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEDALITFCRRQLT 522
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGeTLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 489956626 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
20-550 |
6.32e-95 |
|
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: 298.90 E-value: 6.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 20 DRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:cd05959 1 EKYNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEK--TQVKHVILTRmGDQLSTAKGTLVNFVVKYVKRLVPK 177
Cdd:cd05959 80 VPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKseHTLVVLIVSG-GAGPEAGALLLAELVAAEAEQLKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 178 yhlpdaisfrrALHAgyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLHPGK-ELVIT 255
Cdd:cd05959 159 -----------ATHA-------------DDPAFWLYSSGSTGRPKGVVHLHADIYWTAE----LYArNVLGIREdDVCFS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 256 ALPLYHIFALTmNCLLFIELGGQNVLITNPRDIPGLV-KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGG 334
Cdd:cd05959 211 AAKLFFAYGLG-NSLTFPLSVGATTVLMPERPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 335 MPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVN-PHDIDYhsGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQ 413
Cdd:cd05959 290 EALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNrPGRVRY--GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 414 VMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSS 493
Cdd:cd05959 368 SATMYWNNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 494 GEAVKIFVVKK----DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05959 448 LTKPKAFVVLRpgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-487 |
1.31e-93 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 298.17 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 19 PDRYQSLIELFEHSVRRYADQPAFVNMG----EVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGI 94
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLY---TPRELEHQLNDSGAAaIVIVSNFAHtLEKVVE----KTQVKHVILTRMGDQLSTAKgtlvnfv 167
Cdd:COG1022 86 LAAGAVTV---PIYptsSAEEVAYILNDSGAK-VLFVEDQEQ-LDKLLEvrdeLPSLRHIVVLDPRGLRDDPR------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 168 VKYVKRLVP---KYHLPDAISFRRAlhagyrmqyvkpEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGp 244
Cdd:COG1022 154 LLSLDELLAlgrEVADPAELEARRA------------AVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 245 lLHPGkELVITALPLYHIFALTMnCLLFIELGGQNVLITNPRDIPGLVKELAkyPfTAMTGVNTLFNALLNN-------- 316
Cdd:COG1022 221 -LGPG-DRTLSFLPLAHVFERTV-SYYALAAGATVAFAESPDTLAEDLREVK--P-TFMLAVPRVWEKVYAGiqakaeea 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 317 KEFQQLDFST---------LHLSAGGGMP----VQQAVAERWV--KL---------------------TGQY-------L 353
Cdd:COG1022 295 GGLKRKLFRWalavgrryaRARLAGKSPSlllrLKHALADKLVfsKLrealggrlrfavsggaalgpeLARFfralgipV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 354 LEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLvddednevphGEPGELCVRGPQVMLGYWQRPDATDE-IIKDG 432
Cdd:COG1022 375 LEGYGLTETSPVITVNRPG-DNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEaFDADG 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 433 WLHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:COG1022 444 WLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-551 |
2.26e-93 |
|
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: 294.22 E-value: 2.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 37 ADQPAFV--NMGEVMTFRKLEERSRAFAAYLqEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELE 114
Cdd:cd05926 1 PDAPALVvpGSTPALTYADLAELVDDLARQL-AALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 115 HQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTrmgdqlstakgtlvnfVVKYVKRLVPKYhlpDAISFRRALHAGY 194
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGPASRAASKLGLAILELA----------------LDVGVLIRAPSA---ESLSNLLADKKNA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 195 RMQyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITaLPLYHIFALtMNCLLFIE 274
Cdd:cd05926 141 KSE---GVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK--LTPDDRTLVV-MPLFHVHGL-VASLLSTL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 275 LGGQNVLITnPRDIPGLV-KELAKYPFTAMTGVNTLFNALLNN------KEFQQLDFSTlhlSAGGGMPVqqAVAERWVK 347
Cdd:cd05926 214 AAGGSVVLP-PRFSASTFwPDVRDYNATWYTAVPTIHQILLNRpepnpeSPPPKLRFIR---SCSASLPP--AVLEALEA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 348 LTGQYLLEGYGLTECAPLVSVNPHDIDYHS-GSIGLPVpSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATD 426
Cdd:cd05926 288 TFGAPVLEAYGMTEAAHQMTSNPLPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 427 EI-IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KK 504
Cdd:cd05926 367 EAaFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVlRE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489956626 505 DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05926 447 GASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
10-561 |
4.95e-92 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 294.94 E-value: 4.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 10 PADVPA-EINP----DRYQSLIELFEHSVRRYADQPA--FV------NMGEVMTFRKLEER-SRAfaAYLQEGLGLQKGD 75
Cdd:PRK07529 7 LADIEAiEAVPlaarDLPASTYELLSRAAARHPDAPAlsFLldadplDRPETWTYAELLADvTRT--ANLLHSLGVGPGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 76 RVALMMPNLLQYPVALFGILRAGmIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVEK-TQVKHVIL 149
Cdd:PRK07529 85 VVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAAlPELRTVVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 150 TRMGDQLSTAKGTLVNFvvkyvkrLVPKYHLPDaISFRRALHAGYRMQYVKPE-IVSEDLAFLQYTGGTTGVAKGAMLTH 228
Cdd:PRK07529 164 VDLARYLPGPKRLAVPL-------IRRKAHARI-LDFDAELARQPGDRLFSGRpIGPDDVAAYFHTGGTTGMPKLAQHTH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 229 RNMLANLEQVNATYGplLHPGKeLVITALPLYHIFALTMNCLLFIeLGGQNVLITNP---RDiPGLVKEL----AKYPFT 301
Cdd:PRK07529 236 GNEVANAWLGALLLG--LGPGD-TVFCGLPLFHVNALLVTGLAPL-ARGAHVVLATPqgyRG-PGVIANFwkivERYRIN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 302 AMTGVNTLFNALLnnkefQQ----LDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHS 377
Cdd:PRK07529 311 FLSGVPTVYAALL-----QVpvdgHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 378 GSIGLPVPSTEAKLV--DDEDN---EVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVD 452
Cdd:PRK07529 386 GSVGLRLPYQRVRVVilDDAGRylrDCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 453 RKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEDALITFCRRQLTG-YKVPKLV 530
Cdd:PRK07529 466 RAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHV 545
|
570 580 590
....*....|....*....|....*....|.
gi 489956626 531 EFRDELPKSNVGKILRRELRDEARAKVDNKA 561
Cdd:PRK07529 546 RILDALPKTAVGKIFKPALRRDAIRRVLRAA 576
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-550 |
2.64e-90 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 281.47 E-value: 2.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 211 LQYTGGTTGVAKGAMLTHRNMLANLEQVnatyGPLLHPGKELVIT-ALPLYHIFALTMNCLLFIELGGQNVLITNPRDIP 289
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFI----GERLGLTEQDRLCiPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 290 GLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTG-QYLLEGYGLTECAPLVSV 368
Cdd:cd05917 83 AVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 369 N-PHD-IDYHSGSIGLPVPSTEAKLVDDEDNEVPH-GEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDD 444
Cdd:cd05917 163 TrTDDsIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIdGDGWLHTGDLAVMDE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEDALITFCRRQLTG 523
Cdd:cd05917 243 DGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIrLKEGAELTEEDIKAYCKGKIAH 322
|
330 340
....*....|....*....|....*..
gi 489956626 524 YKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05917 323 YKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-551 |
1.29e-88 |
|
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: 280.33 E-value: 1.29e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmq 197
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-VNA-TYGP---LLHpgkelvitALPLYHIFAL--TMNCL 270
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVRAlVDAwRWTEddvLLH--------VLPLHHVHGLvnALLCP 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 271 LFIelGGQNVLITNPRDIPGLVKELAKyPFTAMTGVNTLFNALL--NNKEFQQLDFST--------LHLSAGGGMPVQqa 340
Cdd:cd05941 153 LFA--GASVEFLPKFDPKEVAISRLMP-SITVFMGVPTIYTRLLqyYEAHFTDPQFARaaaaerlrLMVSGSAALPVP-- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 341 VAERWVKLTGQYLLEGYGLTECAPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDEDNE-VPHGEPGELCVRGPQVMLGYW 419
Cdd:cd05941 228 TLEEWEAITGHTLLERYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEYW 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDAT-DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAV 497
Cdd:cd05941 307 NKPEATkEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERV 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 498 KIFVVKKD--PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05941 387 VAVVVLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-551 |
2.68e-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: 279.22 E-value: 2.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 nfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivsEDLA 209
Cdd:cd05972 81 ----------------------------------------------------------------------------EDPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGKELVITALP--LYHIFALTMNCLLfieLGGQNVLITNPR- 286
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDIHWNIADPgwAKGAWSSFFGPWL---LGATVFVYEGPRf 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKELAKYPFTAMTGVNTLFNaLLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLV 366
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYR-MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 367 SvNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR--GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDD 444
Cdd:cd05972 239 G-NFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDE 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-----PSLTEDaLITFCRR 519
Cdd:cd05972 318 DGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepsEELAEE-LQGHVKK 396
|
490 500 510
....*....|....*....|....*....|..
gi 489956626 520 QLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05972 397 VLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
28-550 |
6.14e-84 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 271.08 E-value: 6.14e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 28 LFEHsVRRYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVN 105
Cdd:PLN02246 29 CFER-LSEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTAN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 106 PLYTPRELEHQLNDSGAAAIVIVSNFAhtlEKVVEKTQVKHVILTRMGDQlstakgtlvnfvvkyvkrlvpkyhlPDAIS 185
Cdd:PLN02246 107 PFYTPAEIAKQAKASGAKLIITQSCYV---DKLKGLAEDDGVTVVTIDDP-------------------------PEGCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 186 FRRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVI-TALPLYHIFA 264
Cdd:PLN02246 159 HFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVIlCVLPMFHIYS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 265 LtmNCLLFIEL-GGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMP----VQQ 339
Cdd:PLN02246 239 L--NSVLLCGLrVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPlgkeLED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 340 AVAerwVKLTGQYLLEGYGLTECAPLVSVNP----HDIDYHSGSIGLPVPSTEAKLVDDEDNE-VPHGEPGELCVRGPQV 414
Cdd:PLN02246 317 AFR---AKLPNAVLGQGYGMTEAGPVLAMCLafakEPFPVKSGSCGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 415 MLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSS 493
Cdd:PLN02246 394 MKGYLNDPEATANTIdKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 494 GEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PLN02246 474 GEVPVAFVVRSNGSeITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-552 |
1.67e-83 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 269.05 E-value: 1.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMM----PNLLQYpvalFGILRAGMIVVNVNPLYTPRELEHQLNDSG 121
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 122 AAAIVIVSNFAHTLEKVVEKTQVKHViLTRMGDqlstAKGTLVnfvvkyvkrlvpkyhlpdaisfRRALHAGYRMQYVKP 201
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGAPHV-ETLDAD----GTGSLL----------------------EAAAAAPDDFETVPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 202 EivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG-----PLLHpgkelvitALPLYHIFAL--TMNCLLFIe 274
Cdd:PRK07514 154 G--ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRftpddVLIH--------ALPIFHTHGLfvATNVALLA- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 275 lGGQnvLITNPRDIPGLVkeLAKYP-FTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYL 353
Cdd:PRK07514 223 -GAS--MIFLPKFDPDAV--LALMPrATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 354 LEGYGLTECAPLVSvNPHDIDYHSGSIGLPVPSTEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYWQRPDAT-DEIIKD 431
Cdd:PRK07514 298 LERYGMTETNMNTS-NPYDGERRAGTVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTaEEFRAD 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 432 GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTE 510
Cdd:PRK07514 377 GFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVpKPGAALDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489956626 511 DALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07514 457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-550 |
7.66e-82 |
|
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: 262.78 E-value: 7.66e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 39 QPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLN 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALR-NLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 119 DSgAAAIVIVSnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqy 198
Cdd:cd05919 80 DC-EARLVVTS--------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 199 vkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNML--ANLEQVNATYgplLHPGkELVITALPLYHIFALTMNCLLFIELG 276
Cdd:cd05919 90 ------ADDIAYLLYSSGTTGPPKGVMHAHRDPLlfADAMAREALG---LTPG-DRVFSSAKMFFGYGLGNSLWFPLAVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 277 GQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEG 356
Cdd:cd05919 160 ASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 357 YGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHT 436
Cdd:cd05919 240 IGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGGWYRT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 437 GDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALI-- 514
Cdd:cd05919 319 GDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLArd 398
|
490 500 510
....*....|....*....|....*....|....*...
gi 489956626 515 --TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05919 399 ihRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-551 |
2.17e-81 |
|
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: 263.72 E-value: 2.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 NFAHTLEKVVEK-TQVKHVILTRMGDqlstakgtlvnfvvkyvKRLVPkyHLPDAISFRRALHAGyRMQYVKPEIVSEDL 208
Cdd:cd12119 106 DFLPLLEAIAPRlPTVEHVVVMTDDA-----------------AMPEP--AGVGVLAYEELLAAE-SPEYDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 209 AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVITALPLYHI------FALTMncllfieLGGQNVLi 282
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSES-DVVLPVVPMFHVnawglpYAAAM-------VGAKLVL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNPRDIPG-LVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLtGQYLLEGYGLTE 361
Cdd:cd12119 237 PGPYLDPAsLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 362 CAPLVSVNpHDIDYHSG-----------SIGLPVPSTEAKLVDDEDNEVPH--GEPGELCVRGPQVMLGYWQRPDATDEI 428
Cdd:cd12119 316 TSPLGTVA-RPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGE-AVKIFVVKKDPS 507
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErPLAVVVLKEGAT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489956626 508 LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd12119 475 VTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
21-552 |
9.00e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 257.28 E-value: 9.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 21 RYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:PRK07470 5 RVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAA-RGVRKGDRILVHSRNCNQMFESMFAAFRLGAV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 101 VVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKT-QVKHVIltrmgdQLSTAKGTlvnfvvkyvkrlvPKYh 179
Cdd:PRK07470 84 WVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASpDLTHVV------AIGGARAG-------------LDY- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 180 lpDAISfrrALHAGYRmqyVKPEIVS-EDLAFLQYTGGTTGVAKGAMLTHRNM-------LANLeqVNATygplLHPGKE 251
Cdd:PRK07470 144 --EALV---ARHLGAR---VANAAVDhDDPCWFFFTSGTTGRPKAAVLTHGQMafvitnhLADL--MPGT----TEQDAS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 252 LVITalPLYH---IFALTMncllfIELGGQNVLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTL 327
Cdd:PRK07470 210 LVVA--PLSHgagIHQLCQ-----VARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 328 HLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNP---HDID----YHSGSIGLPVPSTEAKLVDDEDNEVP 400
Cdd:PRK07470 283 RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITVLPpalHDAEdgpdARIGTCGFERTGMEVQIQDDEGRELP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 401 HGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:PRK07470 363 PGETGEICVIGPAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAV 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956626 481 LEVAAVGVPSGSSGE-AVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK07470 443 SEVAVLGVPDPVWGEvGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-550 |
1.09e-78 |
|
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: 254.23 E-value: 1.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 48 VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVI 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 128 VSNFAhtlekvvektQVKHViltrmgdqlstakgtlvnfvvkyvkrlvpkyHLPDAIsfrralhagyrmqyvkpeivsed 207
Cdd:cd05903 80 PERFR----------QFDPA-------------------------------AMPDAV----------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 208 lAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVITALPLYHIFALTMNCLLFIELGGQNVL--ITNP 285
Cdd:cd05903 96 -ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG---LGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLqdIWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 286 RDIPGLVKElakYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECA-P 364
Cdd:cd05903 172 DKALALMRE---HGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPgA 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 365 LVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDD 444
Cdd:cd05903 249 VTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEDALITFCRRQ-LT 522
Cdd:cd05903 329 DGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVAYLDRQgVA 408
|
490 500
....*....|....*....|....*...
gi 489956626 523 GYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05903 409 KQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-552 |
9.22e-77 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 252.75 E-value: 9.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAFV-NMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIvivsnFAHTLEKvveKTQVKHVILTrMGDQLSTAKGTLVnfvvkyVKRLVPKYhlpD 182
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMF-----FAPTLFK---QTRPVDLILP-LQNQLPQLQQIVG------VDKLAPAT---S 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 183 AISFRRALHAGYRMQYvKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygpLLHPGKELVITALPLYHI 262
Cdd:PRK06087 165 SLSLSQIIADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCAR---LNLTWQDVFMMPAPLGHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 263 FALTMNCLLFIELGGQNVL--ITNPRDIPGLvkeLAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQA 340
Cdd:PRK06087 241 TGFLHGVTAPFLIGARSVLldIFTPDACLAL---LEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 341 VAERwVKLTGQYLLEGYGLTECAPLVSVNPHD-IDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYW 419
Cdd:PRK06087 318 VARE-CQQRGIKLLSVYGSTESSPHAVVNLDDpLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK 498
Cdd:PRK06087 397 DEPELTARALdEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 499 IFVVKKDPSLT---EDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06087 477 AYVVLKAPHHSltlEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
8-555 |
1.83e-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: 251.22 E-value: 1.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 8 RYPADVPAeinpdRY--------QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVAL 79
Cdd:COG1021 7 PWPEEFAA-----RYreagywrgETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLA-LGLRPGDRVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 80 MMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS--------NFAHTLEKVVEktQVKHVILTr 151
Cdd:COG1021 81 QLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVP--SLRHVLVV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 152 mGDQlstakgtlvnfvvkyvkrlvpkyhlPDAISFRRALHAGyrMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNM 231
Cdd:COG1021 158 -GDA-------------------------GEFTSLDALLAAP--ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 232 LANLEQVNA--------TYgpllhpgkeLVitALPLYHIFALTMNCLL-FIELGGQNVLITNPRdiPGLVKEL-AKYPFT 301
Cdd:COG1021 210 LYSVRASAEicgldadtVY---------LA--ALPAAHNFPLSSPGVLgVLYAGGTVVLAPDPS--PDTAFPLiERERVT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 302 AMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTEcaPLVSVN----PHDIDYHS 377
Cdd:COG1021 277 VTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE--GLVNYTrlddPEEVILTT 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 378 gsIGLPV-PSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDAT----DEiikDGWLHTGDIAVMDDEGFLRIVD 452
Cdd:COG1021 355 --QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNarafTP---DGFYRTGDLVRRTPDGYLVVEG 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 453 RKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFCR-RQLTGYKVPKLVE 531
Cdd:COG1021 430 RAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLReRGLAAFKLPDRLE 509
|
570 580
....*....|....*....|....
gi 489956626 532 FRDELPKSNVGKILRRELRDEARA 555
Cdd:COG1021 510 FVDALPLTAVGKIDKKALRAALAA 533
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-487 |
3.01e-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: 248.28 E-value: 3.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLY---TPRELEHQLNDSGAAAI 125
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 vIVSNfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivS 205
Cdd:cd05907 82 -FVED--------------------------------------------------------------------------P 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPLLHPGK-ELVITALPLYHIFALTMNCLLFIELGGQNVLitn 284
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNA----LALAERLPATEgDRHLSFLPLAHVFERRAGLYVPLLAGARIYF--- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 285 PRDIPGLVKELAKYPFTAMTGVNTLFNALLNN------KEFQQLDFSTLHLS-----AGGGMPVQQAVAERWVKLtGQYL 353
Cdd:cd05907 160 ASSAETLLDDLSEVRPTVFLAVPRVWEKVYAAikvkavPGLKRKLFDLAVGGrlrfaASGGAPLPAELLHFFRAL-GIPV 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 354 LEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDednevphgepGELCVRGPQVMLGYWQRPDATDE-IIKDG 432
Cdd:cd05907 239 YEGYGLTETSAVVTLNPPG-DNRIGTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEaLDADG 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
14-551 |
1.98e-75 |
|
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: 248.60 E-value: 1.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 14 PAEINPDRYQSLIELFEHSVRRYADQP---AFVN--MGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYP 88
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKRYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 89 VALFGILRAGMIVVNVNPLYTPRELEHQLNDSgAAAIVIVSNfaHTLEKVVE-KTQVKHVILTRMGDQLSTAKG--TLVN 165
Cdd:cd17642 84 LPVIAGLFIGVGVAPTNDIYNERELDHSLNIS-KPTIVFCSK--KGLQKVLNvQKKLKIIKTIIILDSKEDYKGyqCLYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 166 FVvkyvkrlvpKYHLPdaisfrralhAGYRMQYVKPEIVS--EDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-QVNATY 242
Cdd:cd17642 161 FI---------TQNLP----------PGFNEYDFKPPSFDrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 243 GPLLHPGKElVITALPLYHIFALTmNCLLFIELGGQNVLITNpRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQL 322
Cdd:cd17642 222 GNQIIPDTA-ILTVIPFHHGFGMF-TTLGYLICGFRVVLMYK-FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 323 DFSTLHLSAGGGMP----VQQAVAERwVKLTGqyLLEGYGLTECAPLVSVNPhDIDYHSGSIGLPVPSTEAKLVD-DEDN 397
Cdd:cd17642 299 DLSNLHEIASGGAPlskeVGEAVAKR-FKLPG--IRQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDlDTGK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 398 EVPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQ 476
Cdd:cd17642 375 TLGPNERGELCVKGPMIMKGYVNNPEATKALIdKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQ 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 477 HSGVLEVAAVGVPSGSSGEAVKIFVVKK-DPSLTEDALITFCRRQLTGYKvpKL---VEFRDELPKSNVGKILRRELRD 551
Cdd:cd17642 455 HPKIFDAGVAGIPDEDAGELPAAVVVLEaGKTMTEKEVMDYVASQVSTAK--RLrggVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-552 |
1.54e-74 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 244.87 E-value: 1.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQ-YPV--ALFGIlraGMIVVNVNPLYTPRELE 114
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEmILVihALQQL---GAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 115 HQLNDSGAAAIVIVSNFAHtleKVVEKTQVKHVILtrmgdqlstAKGTLVNFVvkyvkrLVPKYHLpdaisfrralhagy 194
Cdd:PRK03640 93 WQLDDAEVKCLITDDDFEA---KLIPGISVKFAEL---------MNGPKEEAE------IQEEFDL-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 195 rmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLAnleqvnATYGPLLHPG---KELVITALPLYHI--FALTMNC 269
Cdd:PRK03640 141 -----------DEVATIMYTSGTTGKPKGVIQTYGNHWW------SAVGSALNLGlteDDCWLAAVPIFHIsgLSILMRS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 270 LLFielgGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLnnKEFQQL----DFSTLHLsaGGGmPVQQAVAERw 345
Cdd:PRK03640 204 VIY----GMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLL--ERLGEGtypsSFRCMLL--GGG-PAPKPLLEQ- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKLTGQYLLEGYGLTE-CAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEdNEVPHGEPGELCVRGPQVMLGYWQRPDA 424
Cdd:PRK03640 274 CKEKGIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKDG-VVVPPFEEGEIVVKGPNVTKGYLNREDA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 425 TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGeAVKIFVVKK 504
Cdd:PRK03640 353 TRETFQDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG-QVPVAFVVK 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489956626 505 DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK03640 432 SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-552 |
8.82e-74 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 244.89 E-value: 8.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 4 VWLNRYPAdVPAeinPDRYqSLIELFEHSVRRYADQPAFVN--MGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMM 81
Cdd:PLN02330 14 IFRSRYPS-VPV---PDKL-TLPDFVLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 82 PNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAaiVIVSNFAHtLEKVvektqvkhviltrmgdqlstaKG 161
Cdd:PLN02330 88 PNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAK--LIVTNDTN-YGKV---------------------KG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 162 TLVNFVVkyvkrlVPKYHLPDAISFRRALHAGYRM--QYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN 239
Cdd:PLN02330 144 LGLPVIV------LGEEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 240 ATYGPLLhPGKELVITALPLYHIFALTMNCLLFIELGGQnVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF 319
Cdd:PLN02330 218 FSVGPEM-IGQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 320 QQLDFSTLHLSA--GGGMPVQQAVAERW-VKLTGQYLLEGYGLTE--CAPLVSVNP---HDIDyHSGSIGLPVPSTEAKL 391
Cdd:PLN02330 296 EEFDLSKLKLQAimTAAAPLAPELLTAFeAKFPGVQVQEAYGLTEhsCITLTHGDPekgHGIA-KKNSVGFILPNLEVKF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 392 VD-DEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PLN02330 375 IDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIdEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 470 IEDVVMQHSGVLEVAAVGVPSGSSGE-AVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:PLN02330 455 LEAILLTHPSVEDAAVVPLPDEEAGEiPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRL 534
|
....
gi 489956626 549 LRDE 552
Cdd:PLN02330 535 LKEK 538
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-550 |
1.53e-73 |
|
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: 240.84 E-value: 1.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 39 QPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLN 118
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 119 DSGAAAIVIVsnfahtlekvvektqvkhviltrmgDQLSTakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqy 198
Cdd:cd05958 81 KARITVALCA-------------------------HALTA---------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 199 vkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYGP-LLHPGKELVITALP-LYHIFALTMNCLLFIELG 276
Cdd:cd05958 96 ------SDDICILAFTSGTTGAPKATMHFHRDPLASAD----RYAVnVLRLREDDRFVGSPpLAFTFGLGGVLLFPFGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 277 GQNVLI--TNPRDIPGLVkelAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHL--SAGGGMPvqQAVAERWVKLTGQY 352
Cdd:cd05958 166 ASGVLLeeATPDLLLSAI---ARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKcvSAGEALP--AALHRAWKEATGIP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPL-VSVNPHDIdyHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQvmlGYWQRPDATDE-IIK 430
Cdd:cd05958 241 IIDGIGSTEMFHIfISARPGDA--RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRtYVQ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKK-----D 505
Cdd:cd05958 316 GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489956626 506 PSLTEdALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05958 396 PVLAR-ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-551 |
2.79e-73 |
|
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: 240.41 E-value: 2.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 47 EVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIV 126
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 127 IvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpDAisfrralhagyrmqyvkpeivSE 206
Cdd:cd05971 84 T------------------------------------------------------DG---------------------SD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVITALPLYHIFALtMNCLLFIELGGQNVLITNPR 286
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFN-LFPRDGDLYWTPADWAWIGGL-LDVLLPSLYFGVPVLAHRMT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 --DIPGLVKELAKYpftamtGVNTLF---NAL-LNNKEFQQLDFSTLHLSA---GGGMPVQQAVAerWVKLT-GQYLLEG 356
Cdd:cd05971 167 kfDPKAALDLMSRY------GVTTAFlppTALkMMRQQGEQLKHAQVKLRAiatGGESLGEELLG--WAREQfGVEVNEF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 357 YGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQ--VMLGYWQRPDATDEIIKDGWL 434
Cdd:cd05971 239 YGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGDWL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 435 HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALI 514
Cdd:cd05971 319 LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 489956626 515 ----TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05971 399 reiqELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
213-546 |
5.35e-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: 236.01 E-value: 5.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 213 YTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVItaLPLYHIFALTMNcLLFIELGGQNVLITNpRDIPGLV 292
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG-LTEADVYLNM--LPLFHIAGLNLA-LATFHAGGANVVMEK-FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 293 KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPvqqAVAERWVKLTGQYLLEGYGLTECAPLVSVnpHD 372
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTL--SP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 373 IDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVD 452
Cdd:cd17637 157 YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 453 RK--KDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK-IFVVKKDPSLTEDALITFCRRQLTGYKVPKL 529
Cdd:cd17637 237 RKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKKPRY 316
|
330
....*....|....*..
gi 489956626 530 VEFRDELPKSNVGKILR 546
Cdd:cd17637 317 VVFVEALPKTADGSIDR 333
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
46-560 |
8.76e-73 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 242.44 E-value: 8.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAai 125
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 vivsnFAHTLEKVVEKtqvkhviLTRMGdqlstakgtlvnfvvkyvkrlVPKYHLPDAISF---RRALHAGYRMQY---- 198
Cdd:PLN02574 142 -----LAFTSPENVEK-------LSPLG---------------------VPVIGVPENYDFdskRIEFPKFYELIKedfd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 199 --VKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-VNATYGPLLHPGKELV-ITALPLYHIFALTMNCLLFIE 274
Cdd:PLN02574 189 fvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELfVRFEASQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 275 LGgQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNN-KEFQQLDFSTLHLSAGGGMPVQQAVAERWVK-LTGQY 352
Cdd:PLN02574 269 LG-STIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQtLPHVD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPLVS--VNPHDIDYHSgSIGLPVPSTEAKLVDDEDNE-VPHGEPGELCVRGPQVMLGYWQRPDATD-EI 428
Cdd:PLN02574 348 FIQGYGMTESTAVGTrgFNTEKLSKYS-SVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQsTI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPS- 507
Cdd:PLN02574 427 DKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSt 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 508 LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNK 560
Cdd:PLN02574 507 LSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSR 559
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-546 |
1.94e-72 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 234.70 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnLEQVNATYGPLLHPGKELVITalPLYHIFALTMNCLLFIeLGGQNVLITNPR 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR-AAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACL-LTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERW-VKLTGQYLLEGYGLTECAPL 365
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMrSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 366 VSVNPHD-IDYHSGSIGLPVPSTEAKLVDDednevphgepGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMD 443
Cdd:cd17638 157 TMCRPGDdAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIdADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDP-SLTEDALITFCRRQLT 522
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 489956626 523 GYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-553 |
2.46e-72 |
|
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: 239.16 E-value: 2.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEGLglQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VivsnfahTLEKVVEKTQVKHVIltrmgDQLSTAKgtlvnfvVKYVKRLVPKYHLPDAIsfRRALHA------GYRMQYV 199
Cdd:cd05909 83 L-------TSKQFIEKLKLHHLF-----DVEYDAR-------IVYLEDLRAKISKADKC--KAFLAGkfppkwLLRIFGV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 200 KPEiVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVITALPLYHIFALTMNCLLFIELGGQN 279
Cdd:cd05909 142 APV-QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 280 VLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKefQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGL 359
Cdd:cd05909 218 VFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 360 TECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGD 438
Cdd:cd05909 296 TECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDGWYDTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 439 IAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGV-LEVAAVGVPSGSSGEavKIFVVKKDPSLTEDALITFC 517
Cdd:cd05909 376 IGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDIL 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 489956626 518 RR-QLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05909 454 KNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-555 |
1.34e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 238.91 E-value: 1.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQE-GLGLqkGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQ 116
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSRrGVGF--GDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 117 LNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTrMGDqlSTAKGTLvnfvvkyvkrlvpkyHLPDAISFRRALHAgyrm 196
Cdd:PRK07786 110 VSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVV-AGG--SSDDSVL---------------GYEDLLAEAGPAHA---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 197 qyvkPEIVSEDL-AFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHPGKELVITALPLYHIFALTmNCLLFIEL 275
Cdd:PRK07786 168 ----PVDIPNDSpALIMYTSGTTGRPKGAVLTHANLTG--QAMTCLRTNGADINSDVGFVGVPLFHIAGIG-SMLPGLLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 276 GGQNVLI-TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLL 354
Cdd:PRK07786 241 GAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 355 EGYGLTECAPLVSV-NPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGW 433
Cdd:PRK07786 321 AAFGQTEMSPVTCMlLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 434 LHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEaVKIFVVKKDPS---LTE 510
Cdd:PRK07786 401 FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGE-VPVAVAAVRNDdaaLTL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 489956626 511 DALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
Cdd:PRK07786 480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGA 524
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-550 |
3.83e-71 |
|
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: 235.41 E-value: 3.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 60 AFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAG----MIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTL 135
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 136 EKVvektqvkhviLTRMGDQLSTAKGtlvnfvvkyvkrlvpkyhlpDAISFRRALHAGYrmqyvkpEIVSEDLAFLQYTG 215
Cdd:cd05922 84 RDA----------LPASPDPGTVLDA--------------------DGIRAARASAPAH-------EVSHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 216 GTTGVAKGAMLTHRNMLANLEQVNATYGplLHpGKELVITALPLYHIFALtmNCLLFIELGGQNVLITNPRDIP-GLVKE 294
Cdd:cd05922 127 GSTGSPKLVRLSHQNLLANARSIAEYLG--IT-ADDRALTVLPLSYDYGL--SVLNTHLLRGATLVLTNDGVLDdAFWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 295 LAKYPFTAMTGVNTLFnALLNNKEFQQLDFSTLHL--SAGGGMPvQQAVAERWVKLTGQYLLEGYGLTECAPLVS-VNPH 371
Cdd:cd05922 202 LREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRYltQAGGRLP-QETIARLRELLPGAQVYVMYGQTEATRRMTyLPPE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 372 DIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDA-TDEIIKDGWLHTGDIAVMDDEGFLRI 450
Cdd:cd05922 280 RILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYrRKEGRGGGVLHTGDLARRDEDGFLFI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 451 VDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSgSSGEAVKIFVVKKDpSLTEDALITFCRRQLTGYKVPKLV 530
Cdd:cd05922 360 VGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGEKLALFVTAPD-KIDPKDVLRSLAERLPPYKVPATV 437
|
490 500
....*....|....*....|
gi 489956626 531 EFRDELPKSNVGKILRRELR 550
Cdd:cd05922 438 RVVDELPLTASGKVDYAALR 457
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-561 |
2.30e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 234.41 E-value: 2.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRA-LGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNFAHTLEKVVEKTQvKHVILTRMGDqlstakGTlVNFVVKYVKRL--VPKYHLPDAIsfrralhAGYRMQYvkpei 203
Cdd:PRK08276 88 IVSAALADTAAELAAELP-AGVPLLLVVA------GP-VPGFRSYEEALaaQPDTPIADET-------AGADMLY----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 vsedlaflqyTGGTTGVAKGAM--LTHRNMLANLEQ--VNATYGPLLHPGKELVITAlPLYHIfALTMNCLLFIELGGQN 279
Cdd:PRK08276 148 ----------SSGTTGRPKGIKrpLPGLDPDEAPGMmlALLGFGMYGGPDSVYLSPA-PLYHT-APLRFGMSALALGGTV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 280 VLitNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF--QQLDFSTLHLSAGGGMP----VQQAVAERWvkltGQY 352
Cdd:PRK08276 216 VV--MEKfDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEvrARYDVSSLRVAIHAAAPcpveVKRAMIDWW----GPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEI-IKD 431
Cdd:PRK08276 290 IHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAArNPH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 432 GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTED 511
Cdd:PRK08276 369 GWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGD 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489956626 512 A----LITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNKA 561
Cdd:PRK08276 449 AlaaeLIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRAI 502
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-551 |
5.19e-70 |
|
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: 230.70 E-value: 5.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSgaaaivivs 129
Cdd:cd05912 3 TFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 nfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpEIVSEDLA 209
Cdd:cd05912 73 ------------------------------------------------------------------------DVKLDDIA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPgKELVITALPLYHIFALT--MNCLLFielgGQNVLITNPRD 287
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG--LTE-DDNWLCALPLFHISGLSilMRSVIY----GMTVYLVDKFD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 288 IPGLVKELAKYPFTAMTGVNTLFNALLnnKEFQQLDFSTLHLSAGGGMPVQQAVAERwVKLTGQYLLEGYGLTE-CAPLV 366
Cdd:cd05912 154 AEQVLHLINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILLGGGPAPKPLLEQ-CKEKGIPVYQSYGMTEtCSQIV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 367 SVNPHDIDYHSGSIGLPVPSTEAKLVDDEdneVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEG 446
Cdd:cd05912 231 TLSPEDALNKIGSAGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPsLTEDALITFCRRQLTGYKV 526
Cdd:cd05912 308 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYKV 386
|
490 500
....*....|....*....|....*
gi 489956626 527 PKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05912 387 PKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
36-551 |
3.94e-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: 230.65 E-value: 3.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 36 YADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH 115
Cdd:cd12118 17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALA-ALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 116 QLNDSGAAAIVIVSNFAHTlekvvektqvkhviltrmgDQLSTAKGTlvnfvvkyvkrlvPKYHLP----DAISfrralh 191
Cdd:cd12118 96 ILRHSEAKVLFVDREFEYE-------------------DLLAEGDPD-------------FEWIPPadewDPIA------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 192 agyrmqyvkpeivsedlafLQYTGGTTGVAKGAMLTHRN-MLANLEQVnATYGPLLHPGkelVITALPLYH------IFA 264
Cdd:cd12118 138 -------------------LNYTSGTTGRPKGVVYHHRGaYLNALANI-LEWEMKQHPV---YLWTLPMFHcngwcfPWT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 265 LTMncllfieLGGQNVLITNPrDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFS-TLHLSAGGGMPvQQAVAE 343
Cdd:cd12118 195 VAA-------VGGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPP-PAAVLA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RwVKLTGQYLLEGYGLTECAPLVSVNPhdidYHSGSIGLPvPSTEAKL-------------VDDEDNE----VPH-GEP- 404
Cdd:cd12118 266 K-MEELGFDVTHVYGLTETYGPATVCA----WKPEWDELP-TEERARLkarqgvryvgleeVDVLDPEtmkpVPRdGKTi 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 405 GELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVA 484
Cdd:cd12118 340 GEIVFRGNIVMKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAA 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 485 AVGVPSGSSGEAVKIFV-VKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDeLPKSNVGKILRRELRD 551
Cdd:cd12118 420 VVARPDEKWGEVPCAFVeLKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
34-551 |
1.73e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 229.31 E-value: 1.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 34 RRYADQPAFVNM--GEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPR 111
Cdd:PRK09088 6 RLQPQRLAAVDLalGRRWTYAELDALVGRLAAVLR-RRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 112 ELEHQLNDSGAAAIVivsnfahtlekvvektqvkhviltrmGDQLSTAKGTLVnfvvkyvkrlvpkYHLPDAISFRRALH 191
Cdd:PRK09088 85 ELDALLQDAEPRLLL--------------------------GDDAVAAGRTDV-------------EDLAAFIASADALE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 192 AGYRmQYVKPEIVSedlaFLQYTGGTTGVAKGAMLTHRNmlanLEQVNATYGPLLHPGKELVITA-LPLYHIFALTMNCL 270
Cdd:PRK09088 126 PADT-PSIPPERVS----LILFTSGTSGQPKGVMLSERN----LQQTAHNFGVLGRVDAHSSFLCdAPMFHIIGLITSVR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 271 LFIELGGqNVLITNPRDIPGLVKELAKyPFTAMT---GVNTLFNALLNNKEFqqlDFSTL-HLSA--GGGMPvQQAVAER 344
Cdd:PRK09088 197 PVLAVGG-SILVSNGFEPKRTLGRLGD-PALGIThyfCVPQMAQAFRAQPGF---DAAALrHLTAlfTGGAP-HAAEDIL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 WVKLTGQYLLEGYGLTECAPL--VSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRP 422
Cdd:PRK09088 271 GWLDDGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 423 DATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV 501
Cdd:PRK09088 351 QATARAFtGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAI 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489956626 502 VKKDPSLTEDALI-TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK09088 431 VPADGAPLDLERIrSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
21-551 |
3.08e-68 |
|
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: 228.95 E-value: 3.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 21 RYQSLIELFEHSVRR-YADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:TIGR02262 2 KYNAAEDLLDRNVVEgRGGKTAFIDDISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKT-QVKHVILTrmGDQLSTAKgTLVNFVVKYVKRLVPKY 178
Cdd:TIGR02262 81 VPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSpHLEHRVVV--GRPEAGEV-QLAELLATESEQFKPAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 179 HLPDaisfrralhagyrmqyvkpeivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnaTYG-PLLHPGK-ELVITA 256
Cdd:TIGR02262 158 TQAD------------------------DPAFWLYSSGSTGMPKGVVHTHSNPYWTAE----LYArNTLGIREdDVCFSA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 257 LPLYHIFALTmNCLLFIELGGQNVLITNPRDIPGLV-KELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGM 335
Cdd:TIGR02262 210 AKLFFAYGLG-NALTFPMSVGATTVLMGERPTPDAVfDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 336 PVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVN-PHDIDYhsGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQV 414
Cdd:TIGR02262 289 ALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNlPGDVRY--GTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSS 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 415 MLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSG 494
Cdd:TIGR02262 367 ATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 495 EAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:TIGR02262 447 IKPKAFVVlRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
23-552 |
4.01e-68 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 229.64 E-value: 4.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEK-TQVKHVILTRMGDQLSTAKGtlvnfvVKYVKrLVPKYHLP 181
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGdLPLPAVWLLDAPASVSVPAG------WSTAP-LPPLDAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 182 DAISFRRAlhagyrmqyvkpeivseDLAFLQYTGGTTGVAKGAMLTH-------RNMLANLEqvnatygplLHPGkELVI 254
Cdd:PRK06155 173 PAAAVQPG-----------------DTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAEDLE---------IGAD-DVLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 255 TALPLYHIFALTMncllFIE--LGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAG 332
Cdd:PRK06155 226 TTLPLFHTNALNA----FFQalLAGATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 333 GGMPVQQAVA--ERwvklTGQYLLEGYGLTEcAPLVSVNPHDIDyHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR 410
Cdd:PRK06155 302 PGVPAALHAAfrER----FGVDLLDGYGSTE-TNFVIAVTHGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 411 GPQ---VMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:PRK06155 376 ADEpfaFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFP 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 488 VPSGSSGEAVKIFVVKKD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06155 456 VPSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
25-550 |
5.52e-68 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 227.18 E-value: 5.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 25 LIELFEHSVRRYADQPAFVNMGE-VMTFRKLEERSRAFAAylqeglGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVN 103
Cdd:PRK07787 1 LASLNPAAVAAAADIADAVRIGGrVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 104 VNPLYTPRELEHQLNDSGAAAIvivsnfahtlekvvektqvkhviLTRMGDQLSTakgtlvnfvvkyvkrlvpkyhLPdA 183
Cdd:PRK07787 75 VPPDSGVAERRHILADSGAQAW-----------------------LGPAPDDPAG---------------------LP-H 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 184 ISFRraLHAgyRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVITALPLYHIF 263
Cdd:PRK07787 110 VPVR--LHA--RSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQ---WTADDVLVHGLPLFHVH 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 264 ALTMNCLLFIELGGQNVLITNPRdiPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLdFSTLHLSAGGGMPVQQAVAE 343
Cdd:PRK07787 183 GLVLGVLGPLRIGNRFVHTGRPT--PEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFD 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RWVKLTGQYLLEGYGLTECAPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDEDNEVPH-GEP-GELCVRGPQVMLGYWQR 421
Cdd:PRK07787 260 RLAALTGHRPVERYGMTETLITLSTRA-DGERRPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 422 PDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKI 499
Cdd:PRK07787 339 PDATAAAFtADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489956626 500 FVVKKDPSlTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07787 419 YVVGADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-551 |
3.76e-67 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 226.11 E-value: 3.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 33 VRRYADQPAFV--NMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTP 110
Cdd:PRK13391 7 AQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 111 RELEHQLNDSGAAAiVIVSnfAHTLEKVVEKT-QVKHVILTRMGDqlstAKGTLVNFVvkyvkrlvpkyHLPDAISfrra 189
Cdd:PRK13391 86 AEAAYIVDDSGARA-LITS--AAKLDVARALLkQCPGVRHRLVLD----GDGELEGFV-----------GYAEAVA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 190 lhagyrmQYVKPEIVSEDL-AFLQYTGGTTGVAKGAmlthRNMLANLEQVNATygPLLHPGKELV--------ITALPLY 260
Cdd:PRK13391 144 -------GLPATPIADESLgTDMLYSSGTTGRPKGI----KRPLPEQPPDTPL--PLTAFLQRLWgfrsdmvyLSPAPLY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 261 HIfALTMNCLLFIELGGQNVLITN--PRDIPGLVKelaKYPFTAMTGVNTLFNALLNNKEFQQL--DFSTLHLSAGGGMP 336
Cdd:PRK13391 211 HS-APQRAVMLVIRLGGTVIVMEHfdAEQYLALIE---EYGVTHTQLVPTMFSRMLKLPEEVRDkyDLSSLEVAIHAAAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 337 VQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDEDNEVPHGEPGELCVRGPQvML 416
Cdd:PRK13391 287 CPPQVKEQMIDWWGPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGR-PF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 417 GYWQRPDATDEIIKD--GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSG 494
Cdd:PRK13391 365 EYLNDPAKTAEARHPdgTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLG 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 495 EAVKIFVVKKDPSLTEDA----LITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK13391 445 EEVKAVVQPVDGVDPGPAlaaeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
23-550 |
4.21e-67 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 226.10 E-value: 4.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFV---NMGEVMTF--RKL-EERSRAFAAYLQegLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIfesSGGVVRRYsyLELnEEINRTANLFYS--LGIRKGDKVALHLDNCPEFIFCWFGLAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 97 AGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEK--TQVKHVILTRMGdqLSTAKGTlVNFvvkyvKRL 174
Cdd:PRK08008 85 IGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEdaTPLRHICLTRVA--LPADDGV-SSF-----TQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 vpkyhlpdaisfrRALHAGyRMQYVKPeIVSEDLAFLQYTGGTTGVAKGAMLTHRNML-ANLE---QVNATYgpllhpgK 250
Cdd:PRK08008 157 -------------KAQQPA-TLCYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYNLRfAGYYsawQCALRD-------D 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 251 ELVITALPLYHI-FALTMNCLLFiELGGQNVLI-----------------TNPRDIPGLVKELAKYPFTAMTgvntlfna 312
Cdd:PRK08008 215 DVYLTVMPAFHIdCQCTAAMAAF-SAGATFVLLekysarafwgqvckyraTITECIPMMIRTLMVQPPSAND-------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 313 llNNKEFQQLDFsTLHLSAGGgmpvQQAVAERWvkltGQYLLEGYGLTECapLVSV---NPHDiDYHSGSIGLPVPSTEA 389
Cdd:PRK08008 286 --RQHCLREVMF-YLNLSDQE----KDAFEERF----GVRLLTSYGMTET--IVGIigdRPGD-KRRWPSIGRPGFCYEA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 390 KLVDDEDNEVPHGEPGELCVRG---PQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNV 465
Cdd:PRK08008 352 EIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEaDGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENV 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 466 YPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PRK08008 432 SCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKI 511
|
....*.
gi 489956626 545 LRRELR 550
Cdd:PRK08008 512 IKKNLK 517
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
34-551 |
7.87e-67 |
|
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: 226.35 E-value: 7.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 34 RRYADQPAFVNMG---------EVMTFRKLEERSRAFAAYLQEGLGlqKGDRVALMMPNLLQYPVALFGILRAGMIVVnv 104
Cdd:cd05931 1 RRAAARPDRPAYTflddeggreETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 105 nPLYTPRELEHQ------LNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLVnfvvkyvkrlvpky 178
Cdd:cd05931 77 -PLPPPTPGRHAerlaaiLADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADW-------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 179 hlpdaisfrralhagyrmqyVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKELVITALP 258
Cdd:cd05931 142 --------------------PPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG---LDPGDVVVSWLP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 259 LYHIFALTMNCLLFIELGGQNVLITnPRDI---PGL-VKELAKYPFTAMTGVNtlFnAL------LNNKEFQQLDFSTLH 328
Cdd:cd05931 199 LYHDMGLIGGLLTPLYSGGPSVLMS-PAAFlrrPLRwLRLISRYRATISAAPN--F-AYdlcvrrVRDEDLEGLDLSSWR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 LSAGGGMPVQQAVAERWVKLTGQY------LLEGYGLTECAPLVSVNPH---------------------DIDYHSG--- 378
Cdd:cd05931 275 VALNGAEPVRPATLRRFAEAFAPFgfrpeaFRPSYGLAEATLFVSGGPPgtgpvvlrvdrdalagravavAADDPAArel 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 379 -SIGLPVPSTEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYWQRPDATDEIIK-------DGWLHTGDIAVMDDeGFLR 449
Cdd:cd05931 355 vSCGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELY 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE---VAAVGVPSGSSGEAVKIFVVKKDP-SLTEDALITFCRRQL-TGY 524
Cdd:cd05931 434 ITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGAdPADLAAIAAAIRAAVaREH 513
|
570 580 590
....*....|....*....|....*....|.
gi 489956626 525 KVP----KLVEfRDELPKSNVGKILRRELRD 551
Cdd:cd05931 514 GVApadvVLVR-PGSIPRTSSGKIQRRACRA 543
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-551 |
8.69e-66 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 222.65 E-value: 8.69e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 48 VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVI 127
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 128 VSNFAHTLEKVVektqvkhviltrmgdqlstAKGTLVnFVVKYVKRLVPKYHLPDAISFRRALHAGYR--MQYVKP--EI 203
Cdd:PRK12406 90 HADLLHGLASAL-------------------PAGVTV-LSVPTPPEIAAAYRISPALLTPPAGAIDWEgwLAQQEPydGP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 VSEDLAFLQYTGGTTGVAKGamlTHRN-----MLANLEQVNAT-YGplLHPGKELVITAlPLYH----IFALTMncllfI 273
Cdd:PRK12406 150 PVPQPQSMIYTSGTTGHPKG---VRRAaptpeQAAAAEQMRALiYG--LKPGIRALLTG-PLYHsapnAYGLRA-----G 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 274 ELGGqnVLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSTL----HLSAGGGMPVQQAVAERWv 346
Cdd:PRK12406 219 RLGG--VLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLrhviHAAAPCPADVKRAMIEWW- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 347 kltGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVML-GYWQRPDAT 425
Cdd:PRK12406 296 ---GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVkIFVVKKD 505
Cdd:PRK12406 373 AEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL-MAVVEPQ 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489956626 506 P--SLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK12406 452 PgaTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-546 |
2.10e-64 |
|
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: 217.70 E-value: 2.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 vivsnfahtlekvvektqvkhviltrmgdqlstakgtlvnFVVKyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivS 205
Cdd:cd05914 84 ----------------------------------------FVSD-----------------------------------E 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATygPLLHPGkELVITALPLYHIFALTMNCLLFIELGGQNVLITNP 285
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEV--VLLGKG-DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 286 RdiPGLVKELAKYPFTAMTGVNTLF-----------------------NALLNNKEFQQLDFSTLHLSAGG--------G 334
Cdd:cd05914 166 P--SAKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGnikefvigG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 335 MPVQQAVAERWVKLTGQYLlEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKlVDDEDnevPHGEPGELCVRGPQV 414
Cdd:cd05914 244 AKINPDVEEFLRTIGFPYT-IGYGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVR-IDSPD---PATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 415 MLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILV-SGFNVYPNEIEDVVMQHSGVLEvAAVGVPSGS 492
Cdd:cd05914 318 MKGYYKNPEATAEAFdKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEKK 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 493 S---------GEAVKIFVVKKDPSLTEDALITFCRRQLTGY-KVPKLVEFRDELPKSNVGKILR 546
Cdd:cd05914 397 LvalayidpdFLDVKALKQRNIIDAIKWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
34-552 |
7.27e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 217.06 E-value: 7.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 34 RRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPREL 113
Cdd:PRK06145 13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLH-ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 114 EHQLNDSGAAAIVIVSNFAhtlekVVEKTQVKHVILTRMGDQLSTAKGtlvnfvvkyvkrlvpkyhlpdaisfrrALHAG 193
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFD-----AIVALETPKIVIDAAAQADSRRLA---------------------------QGGLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 194 YRMQYVKPEivsEDLAFLQYTGGTTGVAKGAMLTHRNM-LANLEQVNATygPLLHPGKELVITalPLYHIFALTMNCLLF 272
Cdd:PRK06145 140 IPPQAAVAP---TDLVRLMYTSGTTDRPKGVMHSYGNLhWKSIDHVIAL--GLTASERLLVVG--PLYHVGAFDLPGIAV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 273 IELGGQnVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPV-QQAVAERWVKLTGQ 351
Cdd:PRK06145 213 LWVGGT-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 352 YLLEGYGLTE-CAPLVSVNP-HDIDyHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII 429
Cdd:PRK06145 292 RYIDAYGLTEtCSGDTLMEAgREIE-KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 430 KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGE-AVKIFVVKKDPSL 508
Cdd:PRK06145 371 YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGErITAVVVLNPGATL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489956626 509 TEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06145 451 TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
20-551 |
1.45e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 217.49 E-value: 1.45e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 20 DRYQSLIELFEHSVRRYADQPAFVN-MGEvMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK07788 46 RRYGPFAGLVAHAARRAPDRAALIDeRGT-LTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 99 MIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKG--TLVNFVVKYVKRLVP 176
Cdd:PRK07788 124 ARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTdeTLDDLIAGSSTAPLP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 177 KyhlpdaisFRRalHAGyrmqyvkpeivsedlaFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLlhPGKELVITA 256
Cdd:PRK07788 204 K--------PPK--PGG----------------IVILTSGTTGTPKGAPRPEPSPLAPLAGL-LSRVPF--RAGETTLLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 257 LPLYHIFALtMNCLLFIELGgqNVLITNPR-DIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSTLHLSAGG 333
Cdd:PRK07788 255 APMFHATGW-AHLTLAMALG--STVVLRRRfDPEATLEDIAKHKATALVVVPVMLSRILDlgPEVLAKYDTSSLKIIFVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQ 413
Cdd:PRK07788 332 GSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGF 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 414 VMLGYwqrPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSS 493
Cdd:PRK07788 412 PFEGY---TDGRDKQIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 494 GEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK07788 489 GQRLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-549 |
1.26e-62 |
|
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: 212.39 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 37 ADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYtPRE-LEH 115
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRE-RGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 116 QLNDSGAaaivivsnfahtlekvvektqvkHVILTRmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyr 195
Cdd:cd05930 79 ILEDSGA-----------------------KLVLTD-------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 196 mqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVITALP----LYHIFALTMNcll 271
Cdd:cd05930 92 ---------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY-PLTPGDRVLQFTSFSfdvsVWEIFGALLA--- 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 272 fielGGQNVLITN--PRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQqlDFSTLHLSAGGGMPVQQAVAERWVKL- 348
Cdd:cd05930 159 ----GATLVVLPEevRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELl 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 349 TGQYLLEGYGLTECAPLVS---VNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:cd05930 233 PGARLVNLYGPTEATVDATyyrVPPDDEEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DE-IIKD-----GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK 498
Cdd:cd05930 313 AErFVPNpfgpgERMYrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLV 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489956626 499 IFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05930 393 AYVVpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
20-553 |
6.98e-62 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 220.95 E-value: 6.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 20 DRYQSLIELFEHSVRRYADQPAFVN-MGEVMTFRKLEERSRAFAAYLQEGLGLQKgdRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK08633 612 EALPPLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKRELKDEE--NVGILLPPSVAGALANLALLLAG 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 99 MIVVNVNplYTprelehqlndSGAAAivivsnfahtLEKVVEKTQVKHVILTRMGDQLSTAKGTLVNFV----VKYVKRL 174
Cdd:PRK08633 690 KVPVNLN--YT----------ASEAA----------LKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPenvkVIYLEDL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 VPKYHLPDAIsfrRALHAGYRM------QYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtygpLLHP 248
Cdd:PRK08633 748 KAKISKVDKL---TALLAARLLparllkRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISD----VFNL 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 249 GKELVI-TALPLYHIFALTMNCLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTL 327
Cdd:PRK08633 821 RNDDVIlSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASL 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 328 HLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDI---DYHS------GSIGLPVPSTEAKLVDDED-N 397
Cdd:PRK08633 901 RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVlaaDFKRqtgskeGSVGMPLPGVAVRIVDPETfE 980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 398 EVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKD----GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:PRK08633 981 ELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKDidgiGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEE 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 474 VMQ--HSGVLEVAAVGVPSGSSGEavKIFVVKKDPSLTEDALitfcRRQLTGYKVPKLVEFR-----DELPKSNVGKILR 546
Cdd:PRK08633 1061 LAKalGGEEVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEEL----KRAIKESGLPNLWKPSryfkvEALPLLGSGKLDL 1134
|
....*..
gi 489956626 547 RELRDEA 553
Cdd:PRK08633 1135 KGLKELA 1141
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
50-549 |
1.18e-61 |
|
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: 209.61 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGaaaivivs 129
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQ-GIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 nfahtlekvvektqvKHVILTrmgDQLSTAKGTlvnfvvkyvkrlvpkyhlpDAISFRRALHAGYRMQYVKPEIVSEDLA 209
Cdd:TIGR01923 72 ---------------VQLLLT---DSLLEEKDF-------------------QADSLDRIEAAGRYETSLSASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVItALPLYHIFALTMncLLFIELGGQNVLITNPRDip 289
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDNWLL-SLPLYHISGLSI--LFRWLIEGATLRIVDKFN-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 290 GLVKELAKYPFTAMTGVNTLFNALLNnkefQQLDFSTLHLSAGGGMPVQQAVAERWVKLtGQYLLEGYGLTECAPLVSVN 369
Cdd:TIGR01923 188 QLLEMIANERVTHISLVPTQLNRLLD----EGGHNENLRKILLGGSAIPAPLIEEAQQY-GLPIYLSYGMTETCSQVTTA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 370 PHDIDYHSGSIGLPVPSTEAKLVDDEDNEVphgepGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLR 449
Cdd:TIGR01923 263 TPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELTPAFEQQGWFNTGDIGELDGEGFLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEA-VKIFVVKKDPSLTEdaLITFCRRQLTGYKVPK 528
Cdd:TIGR01923 338 VLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVpVAYIVSESDISQAK--LIAYLTEKLAKYKVPI 415
|
490 500
....*....|....*....|.
gi 489956626 529 LVEFRDELPKSNVGKILRREL 549
Cdd:TIGR01923 416 AFEKLDELPYNASGKILRNQL 436
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-550 |
2.67e-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: 208.90 E-value: 2.67e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLYT---PRELEHQLNDSGAAAIV 126
Cdd:cd05969 2 TFAQLKVLSARFANVLKS-LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKVLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 127 ivsnfahTLEKVVEKTQVkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivsE 206
Cdd:cd05969 78 -------TTEELYERTDP-------------------------------------------------------------E 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHPGKELVITALP------LYHIFALTMNcllfielGGQNV 280
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDLHPDDIYWCTADPgwvtgtVYGIWAPWLN-------GVTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 281 LITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF--QQLDFSTLHLSAGGGMPVQQAVAeRW-VKLTGQYLLEGY 357
Cdd:cd05969 161 VYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDElaRKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTW 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 358 GLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRG--PQVMLGYWQRPDATDEIIKDGWLH 435
Cdd:cd05969 240 WQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFIDGWYL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTE---D 511
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlKEGFEPSDelkE 399
|
490 500 510
....*....|....*....|....*....|....*....
gi 489956626 512 ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05969 400 EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-543 |
3.50e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 210.90 E-value: 3.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 28 LFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPL 107
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIA-QGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 108 YTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKT-QVKHVIltRMGDQLSTAkgtlvnfvvkyvkrlvpkyHLPDAISF 186
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLpKLRTLV--VVEDGSGND-------------------LLPGAVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 RRALHAGyrmqyvKPEIV----SEDLAFLQYTGGTTGVAKGAMLTHRNM-LANLEQVNATYGPLLHPGKELVITAL---- 257
Cdd:PRK07798 146 EDALAAG------SPERDfgerSPDDLYLLYTGGTTGMPKGVMWRQEDIfRVLLGGRDFATGEPIEDEEELAKRAAagpg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 258 -------PLYHIFAL--TMNCLLFielGGQNVLITNPR-DIPGLVKELAKYPFTAMTGVN-----TLFNALLNNKEFqql 322
Cdd:PRK07798 220 mrrfpapPLMHGAGQwaAFAALFS---GQTVVLLPDVRfDADEVWRTIEREKVNVITIVGdamarPLLDALEARGPY--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 323 DFSTLHLSAGGGMPVQQAVAERWVKLTGQ-YLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPV-PSTeaKLVDDEDNEVP 400
Cdd:PRK07798 294 DLSSLFAIASGGALFSPSVKEALLELLPNvVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIgPRT--VVLDEDGNPVE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 401 --HGEPGELCVRGPqVMLGYWQRPDATDEIIK--DG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:PRK07798 372 pgSGEIGWIARRGH-IPLGYYKDPEKTAETFPtiDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEAL 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 475 MQHSGVLEVAAVGVPSGSSGEAVkIFVVKKDP--SLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:PRK07798 451 KAHPDVADALVVGVPDERWGQEV-VAVVQLREgaRPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-553 |
5.23e-61 |
|
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: 205.41 E-value: 5.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLE--QVNATYGPllhpgKELVITALPLYHIFALTMNCLLFIELGGQNVLI 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWmlALNSLFDP-----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TnP---RDiPGLVKEL----AKYPFTAMTGVNTLFNALLNNKEfqQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLE 355
Cdd:cd05944 76 G-PagyRN-PGLFDNFwklvERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 356 GYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAK-LVDDEDNEVPH----GEPGELCVRGPQVMLGYWQRPDATDEIIK 430
Cdd:cd05944 152 GYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRiKVLDGVGRLLRdcapDEVGEICVAGPGVFGGYLYTEGNKNAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV-VKKDPSLT 509
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489956626 510 EDALITFCRRQLTGY-KVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05944 312 EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
29-555 |
7.12e-61 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 210.29 E-value: 7.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 29 FEHSVRRYADQPAFVNM----GEV--MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK13295 30 LDACVASCPDKTAVTAVrlgtGAPrrFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVS---NFAHtlEKVVEKTQ-----VKHVILTRMGDQLSTAKgtlvnfvvkyvkrl 174
Cdd:PRK13295 109 PLMPIFRERELSFMLKHAESKVLVVPKtfrGFDH--AAMARRLRpelpaLRHVVVVGGDGADSFEA-------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 vpkyHLPDAiSFRRALHAGYRMQYVKPEivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANleqvNATYGPLLHPGKELVI 254
Cdd:PRK13295 173 ----LLITP-AWEQEPDAPAILARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMAN----IVPYAERLGLGADDVI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 255 -TALPLYHIFALTMNCLLFIELGGQNVL--ITNPRDIPGLVKE------LAKYPFTAmtgvntlfnALLNNKEFQQLDFS 325
Cdd:PRK13295 242 lMASPMAHQTGFMYGLMMPVMLGATAVLqdIWDPARAAELIRTegvtftMASTPFLT---------DLTRAVKESGRPVS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 326 TLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYH-SGSIGLPVPSTEAKLVDDEDNEVPHGEP 404
Cdd:PRK13295 313 SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERaSTTDGCPLPGVEVRVVDADGAPLPAGQI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 405 GELCVRGPQVMLGYWQRPD--ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE 482
Cdd:PRK13295 393 GRLQVRGCSNFGGYLKRPQlnGTDA---DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956626 483 VAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQ-LTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
Cdd:PRK13295 470 VAIVAYPDERLGERACAFVVpRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRG 544
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
23-549 |
1.25e-60 |
|
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: 208.52 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNM--GEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHA-RGLRPGQRVAVVLPNSVEAVIALLALHRLGAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 101 VVNVNPLYTPRELEhQLNDSGAAAIVIVSNFAhtleKVVEKTQVKHVILTRMGDQLSTakGTLVNFvvkyvkrlvpkyhl 180
Cdd:cd05923 80 PALINPRLKAAELA-ELIERGEMTAAVIAVDA----QVMDAIFQSGVRVLALSDLVGL--GEPESA-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 181 PDAISFRralhagyrmqyvKPEIvsEDLAFLQYTGGTTGVAKGAMLTHRnmlANLEQV--NATYGPLLHPGKELVITALP 258
Cdd:cd05923 139 GPLIEDP------------PREP--EQPAFVFYTSGTTGLPKGAVIPQR---AAESRVlfMSTQAGLRHGRHNVVLGLMP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 259 LYHI---FALTMNCLLFielGGQNVLIT--NPRDIPGLVKELAkypFTAMTGVNTLFNALLNNKEFQQLDFSTL-HLS-A 331
Cdd:cd05923 202 LYHVigfFAVLVAALAL---DGTYVVVEefDPADALKLIEQER---VTSLFATPTHLDALAAAAEFAGLKLSSLrHVTfA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 332 GGGMPvqQAVAERWVKLTGQYLLEGYGLTECAPLVsvnpHDIDYHSGSIGLPVPSTEAKLV---DDEDNEVPHGEPGELC 408
Cdd:cd05923 276 GATMP--DAVLERVNQHLPGEKVNIYGTTEAMNSL----YMRDARTGTEMRPGFFSEVRIVrigGSPDEALANGEEGELI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 409 VR--GPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAV 486
Cdd:cd05923 350 VAaaADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 487 GVPSGSSGEAVKIFVVKKDPSLTEDALITFCR-RQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05923 430 GVADERWGQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
12-551 |
1.45e-60 |
|
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: 209.27 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 12 DVPAEINPDRyQSLIELFEHSVRRyadqpafvnmgeVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVAL 91
Cdd:cd05970 24 DAMAKEYPDK-LALVWCDDAGEER------------IFTFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 92 FGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS--NFAHTLEKVVEKTQVKHViLTRMGDQLSTAkgtLVNFVvK 169
Cdd:cd05970 90 LALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAedNIPEEIEKAAPECPSKPK-LVWVGDPVPEG---WIDFR-K 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 170 YVKRLVPKYHLPDAISfrralhagyrmqyvkpEIVSEDLAFLQYTGGTTGVAKgaMLTHrnmlanleqvNATYgPLLHpg 249
Cdd:cd05970 165 LIKNASPDFERPTANS----------------YPCGEDILLVYFSSGTTGMPK--MVEH----------DFTY-PLGH-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 250 kelVITAL--------PLYHIFALT-----MNCLLFIE-LGGQNVLITN-PRDIP-GLVKELAKYPFTAMTGVNTLFNAL 313
Cdd:cd05970 214 ---IVTAKywqnvregGLHLTVADTgwgkaVWGKIYGQwIAGAAVFVYDyDKFDPkALLEKLSKYGVTTFCAPPTIYRFL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 314 LNNKeFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHdIDYHSGSIGLPVPSTEAKLVD 393
Cdd:cd05970 291 IRED-LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPW-MEPKPGSMGKPAPGYEIDLID 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 394 DEDNEVPHGEPGELCVR---GPQVML--GYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPN 468
Cdd:cd05970 369 REGRSCEAGEEGEIVIRtskGKPVGLfgGYYKDAEKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPF 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 469 EIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-----KKDPSLTEDaLITFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:cd05970 449 EVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgyEPSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGK 527
|
....*...
gi 489956626 544 ILRRELRD 551
Cdd:cd05970 528 IRRVEIRE 535
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
18-555 |
3.29e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 205.95 E-value: 3.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 18 NPDRYQSL--IELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGIL 95
Cdd:PRK08162 11 NAANYVPLtpLSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALA-RRGIGRGDTVAVLLPNIPAMVEAHFGVP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 96 RAGMIVVNVNPLYTPRELEHQLnDSGAAAIVIV-SNFAHTLEKVVEKTQVKHVIltrmgdqlstakgtlvnfVVKYVKRL 174
Cdd:PRK08162 90 MAGAVLNTLNTRLDAASIAFML-RHGEAKVLIVdTEFAEVAREALALLPGPKPL------------------VIDVDDPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 VPKYHLPDAISFRRALHAGY-RMQYVKPEIVSEDLAfLQYTGGTTGVAKGAMLTHR----NMLANleQVNATYGPllHPg 249
Cdd:PRK08162 151 YPGGRFIGALDYEAFLASGDpDFAWTLPADEWDAIA-LNYTSGTTGNPKGVVYHHRgaylNALSN--ILAWGMPK--HP- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 250 keLVITALPLYHI----FALTMNCLlfielGGQNVLItnpRDI-PGLVKEL-AKYPFTAMTGVNTLFNALLNN-KEFQQ- 321
Cdd:PRK08162 225 --VYLWTLPMFHCngwcFPWTVAAR-----AGTNVCL---RKVdPKLIFDLiREHGVTHYCGAPIVLSALINApAEWRAg 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 322 LDFSTLHLSAGGGMP--VQQAVAERWVKLTgqyllEGYGLTECAPLVSVNPHDIDYHSGSI----------GLPVPSTEA 389
Cdd:PRK08162 295 IDHPVHAMVAGAAPPaaVIAKMEEIGFDLT-----HVYGLTETYGPATVCAWQPEWDALPLderaqlkarqGVRYPLQEG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 390 KLVDDEDN--EVPH-GEP-GELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNV 465
Cdd:PRK08162 370 VTVLDPDTmqPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENI 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 466 YPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV-VKKDPSLTEDALITFCRRQLTGYKVPKLVEFrDELPKSNVGKI 544
Cdd:PRK08162 450 SSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVeLKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKI 528
|
570
....*....|.
gi 489956626 545 LRRELRDEARA 555
Cdd:PRK08162 529 QKFVLREQAKS 539
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
47-552 |
1.90e-57 |
|
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: 200.77 E-value: 1.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 47 EVM-TFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05928 39 EVKwSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNFAHTLEKVVEKTQvkhviltrmgdQLSTakgtlvnfvvkyvKRLVPKYHLPDAISFRRAL-HAGYRMQYVKPEiv 204
Cdd:cd05928 119 VTSDELAPEVDSVASECP-----------SLKT-------------KLLVSEKSRDGWLNFKELLnEASTEHHCVETG-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYgpllhpgkelvITALPLYHIF--------ALTMNCLLFIE-L 275
Cdd:cd05928 173 SQEPMAIYFTSGTTGSPKMAEHSHSSLGLGL-KVNGRY-----------WLDLTASDIMwntsdtgwIKSAWSSLFEPwI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 276 GGQNVLITN-PR-DIPGLVKELAKYPFTAMTGVNTLFNALLNNkEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYL 353
Cdd:cd05928 241 QGACVFVHHlPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 354 LEGYGLTECApLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR-GPQ----VMLGYWQRPDATDEI 428
Cdd:cd05928 320 YEGYGQTETG-LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSL 508
Cdd:cd05928 399 IRGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 489956626 509 TED------ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:cd05928 479 SHDpeqltkELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-549 |
2.49e-57 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 199.09 E-value: 2.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvKRLVPKYHLPD 182
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYIVP-------------------------------------------DRHAGFDHRAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 183 AISFRRALhagyrmqyvkPEIvsedlAFLQYTGGTTGVAKGAMLTHR----NMLANLEqvnatygpLLHPGKELV-ITAL 257
Cdd:cd05920 131 ARELAESI----------PEV-----ALFLLSGGTTGTPKLIPRTHNdyayNVRASAE--------VCGLDQDTVyLAVL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 258 PLYHIFALT----MNCLLFielGGQNVLITNPRdiPGLVKEL-AKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAG 332
Cdd:cd05920 188 PAAHNFPLAcpgvLGTLLA---GGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 333 GGMPVQQAVAERWVKLTGQYLLEGYGLTEcaPLVSV----NPHDIDYHSGsiGLPV-PSTEAKLVDDEDNEVPHGEPGEL 407
Cdd:cd05920 263 GGARLSPALARRVPPVLGCTLQQVFGMAE--GLLNYtrldDPDEVIIHTQ--GRPMsPDDEIRVVDEEGNPVPPGEEGEL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 408 CVRGPQVMLGYWQRPDA-TDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAV 486
Cdd:cd05920 339 LTRGPYTIRGYYRAPEHnARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 487 GVPSGSSGEAVKIFVVKKDPSLTEDALITFCR-RQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05920 419 AMPDELLGERSCAFVVLRDPPPSAAQLRRFLReRGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
50-550 |
2.45e-56 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 198.58 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVvnvNPLYT---PRELEHQLNDSGAAaiV 126
Cdd:PRK04319 75 TYKELKELSNKFANVLKE-LGVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEafmEEAVRDRLEDSEAK--V 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 127 IVSNFAHTLEKVVEKT-QVKHViltrmgdqlstakgtlvnFVVKYVKRLVPKYhlpdaISFRRALHAG---YRMQYVKPE 202
Cdd:PRK04319 149 LITTPALLERKPADDLpSLKHV------------------LLVGEDVEEGPGT-----LDFNALMEQAsdeFDIEWTDRE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 203 ivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqVNATYGPLLHPGKELVITALP------LYHIFALTMNCLLFIELG 276
Cdd:PRK04319 206 ----DGAILHYTSGSTGKPKGVLHVHNAMLQHY--QTGKYVLDLHEDDVYWCTADPgwvtgtSYGIFAPWLNGATNVIDG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 277 GQnvliTNPRDIPGLvkeLAKYP----FTAMTGVNTLFNAllNNKEFQQLDFSTLHLSAGGGMPVQ-QAVaeRW-VKLTG 350
Cdd:PRK04319 280 GR----FSPERWYRI---LEDYKvtvwYTAPTAIRMLMGA--GDDLVKKYDLSSLRHILSVGEPLNpEVV--RWgMKVFG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 351 QYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRG--PQVMLGYWQRPDATDEI 428
Cdd:PRK04319 349 LPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD--- 505
Cdd:PRK04319 429 FAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPgye 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489956626 506 PS--LTEDaLITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK04319 509 PSeeLKEE-IRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-561 |
2.53e-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: 196.04 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGmiVVNVnplytPR-------ELEHQLNDSGA 122
Cdd:cd17640 7 TYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALG--AVDV-----VRgsdssveELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 123 AAIVIvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpE 202
Cdd:cd17640 79 VALVV--------------------------------------------------------------------------E 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 203 IVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllHPGKElVITALPLYHIFALTmnCLLFIELGGQNVLI 282
Cdd:cd17640 85 NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPP--QPGDR-FLSILPIWHSYERS--AEYFIFACGCSQAY 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNPRDIPglvKELAKYPFTAMTGVNTLFNALLNN--KE------FQQLDFSTL--------HLSAGGGMPVQqavAERWV 346
Cdd:cd17640 160 TSIRTLK---DDLKRVKPHYIVSVPRLWESLYSGiqKQvsksspIKQFLFLFFlsggifkfGISGGGALPPH---VDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 347 KLTGQYLLEGYGLTECAPLVSVNPHDIDYhSGSIGLPVPSTEAKLVDDEDNEV-PHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:cd17640 234 EAIGIEVLNGYGLTETSPVVSARRLKCNV-RGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEAT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQhSGVLEvaavgvpsgssgeavKIFVVK 503
Cdd:cd17640 313 SKVLdSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMR-SPFIE---------------QIMVVG 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 504 KDPSlTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDNKA 561
Cdd:cd17640 377 QDQK-RLGALIVPNFEELEKWAKESGVKLANDRSQLLASKKVLKLYKNEIKDEISNRP 433
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-486 |
5.65e-56 |
|
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: 193.64 E-value: 5.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 NFAHTLEKVVEktqvkhVILTRMGDQLSTAKGTLVNFVvkyvkrlvpkyhlPDAISfrralhagyrmqyvkpeiVSEDLA 209
Cdd:TIGR01733 81 ALASRLAGLVL------PVILLDPLELAALDDAPAPPP-------------PDAPS------------------GPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhpGKELVITALPLYH-------IFAltmnCLLFielGGQNVLI 282
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL----DPDDRVLQFASLSfdasveeIFG----ALLA---GATLVVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNP--RDIPGLVKEL-AKYPFTAMTGVNTLFNALLnnkEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQ-YLLEGYG 358
Cdd:TIGR01733 193 PEDeeRDDAALLAALiAEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGaRLINLYG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 359 LTECAPLVSVNPHDIDYHSG----SIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKDG- 432
Cdd:TIGR01733 270 PTETTVWSTATLVDPDDAPRespvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErFVPDPf 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 433 -------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVlEVAAV 486
Cdd:TIGR01733 350 aggdgarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
201-551 |
5.87e-56 |
|
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: 195.29 E-value: 5.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 201 PEIVSEDLA---FLQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLL---HPGKELVITALPLYHI--FALTMNCLLf 272
Cdd:cd05929 117 PETPIEDEAagwKMLYSGGTTGRPKGIK---RGLPGGPPDNDTLMAAALgfgPGADSVYLSPAPLYHAapFRWSMTALF- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 273 ieLGGQNVLITN--PRDIPGLVKelaKYPFTAMTGVNTLFNALLNNKEFQQ--LDFSTL----HlsAGGGMPVQqaVAER 344
Cdd:cd05929 193 --MGGTLVLMEKfdPEEFLRLIE---RYRVTFAQFVPTMFVRLLKLPEAVRnaYDLSSLkrviH--AAAPCPPW--VKEQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 WVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPStEAKLVDDEDNEVPHGEPGELCVRGPQVMLgYWQRPDA 424
Cdd:cd05929 264 WIDWGGPIIWEYYGGTEGQGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 425 TDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIfVVK 503
Cdd:cd05929 342 TAAaRNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA-VVQ 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 504 KDPS-----LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd05929 421 PAPGadagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-549 |
9.32e-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: 195.11 E-value: 9.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRA-AGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVIvsnfAHTLEKVVEKTQVKHVILtrmgDQLSTAkgtlvnfvvkyvkrlvpkyhlpDAISF 186
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLEVAVVID----EALDAG----------------------PAGNP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 RRALHAgyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvNATYGPLlhPGKELVITALPL------Y 260
Cdd:cd12117 130 AVPVSP-------------DDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTL--GPDDRVLQTSPLafdastF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 261 HIFAltmnCLLFielGGQNVLIT--NPRDIPGLVKELAKYPFTAMTGVNTLFNALLnnkefqQLD---FSTL-HLSAGG- 333
Cdd:cd12117 193 EIWG----ALLN---GARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQLA------DEDpecFAGLrELLTGGe 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GMPVQQ--AVAERWVKLTgqyLLEGYGLTE---CAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELC 408
Cdd:cd12117 260 VVSPPHvrRVLAACPGLR---LVNGYGPTEnttFTTSHVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 409 VRGPQVMLGYWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVL 481
Cdd:cd12117 337 VGGDGLALGYLNRPALTAErFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVR 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 482 EVAAVGVPSGSSGEAVKIFVVkKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12117 417 EAVVVVREDAGGDKRLVAYVV-AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
213-538 |
1.60e-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: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 213 YTGGTTGVAKGAMLTHRN------MLANLEQVNATYGPLlhpgkelviTALPLYHIFALtMNCLLFIELGGQNVLI--TN 284
Cdd:cd17636 7 YTAAFSGRPNGALLSHQAllaqalVLAVLQAIDEGTVFL---------NSGPLFHIGTL-MFTLATFHAGGTNVFVrrVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 285 PRDIPGLV-KELAKYPFTAMTGVNTLFNAllnNKEFQqLDFSTLHlsAGGGMPVQQAVAERWVKLTGQYLlEGYGLTECA 363
Cdd:cd17636 77 AEEVLELIeAERCTHAFLLPPTIDQIVEL---NADGL-YDLSSLR--SSPAAPEWNDMATVDTSPWGRKP-GGYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 364 PLVSVNPHDIDYHSGSiGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMD 443
Cdd:cd17636 150 GLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRGGWHHTNDLGRRE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK-IFVVKKDPSLTEDALITFCRRQLT 522
Cdd:cd17636 229 PDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKaIVVLKPGASVTEAELIEHCRARIA 308
|
330
....*....|....*.
gi 489956626 523 GYKVPKLVEFRDELPK 538
Cdd:cd17636 309 SYKKPKSVEFADALPR 324
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
14-558 |
6.51e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 194.19 E-value: 6.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 14 PAEINPDRYQSLIElfEHsVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK06164 4 DAAPRADTLASLLD--AH-ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 94 ILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFaHTLEKVVEKTQVKHviltrmgDQLSTAKGTLVnfvvkyVKR 173
Cdd:PRK06164 80 CARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGF-KGIDFAAILAAVPP-------DALPPLRAIAV------VDD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 174 LVPKyhLPDAISFRR----ALHAGYRMQYVKPEIVSEDLAFLQYT-GGTTGVAKGAMLTHRNMLANLEQVNATYGplLHP 248
Cdd:PRK06164 146 AADA--TPAPAPGARvqlfALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYG--YDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 249 GkELVITALPLYHIFALTMncLLFIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNnKEFQQLDFSTLH 328
Cdd:PRK06164 222 G-AVLLAALPFCGVFGFST--LLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILD-TAGERADFPSAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 LS-----AGGGMPVQQAVAERWVKLTGQYllegyGLTECAPLVSVNPHDIDY---HSGSiGLPV-PSTEAKLVDDEDNEV 399
Cdd:PRK06164 298 LFgfasfAPALGELAALARARGVPLTGLY-----GSSEVQALVALQPATDPVsvrIEGG-GRPAsPEARVRARDPQDGAL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 400 -PHGEPGELCVRGPQVMLGYWQRPDAT-DEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:PRK06164 372 lPDGESGEIEIRAPSLMRGYLDNPDATaRALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEAL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 478 SGVLEVAAVGVPSGSSGEAVKiFVVKKD-PSLTEDALITFCRRQLTGYKVPKLVEFRDELP---KSNVGKILRRELRDEA 553
Cdd:PRK06164 452 PGVAAAQVVGATRDGKTVPVA-FVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPvteSANGAKIQKHRLREMA 530
|
....*
gi 489956626 554 RAKVD 558
Cdd:PRK06164 531 QARLA 535
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
11-551 |
7.31e-55 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 193.82 E-value: 7.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 11 ADVPAEINPDRY-----------QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVAL 79
Cdd:PRK13382 20 AGLIAPMRPDRYlrivaamrregMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQ-ALPIGEPRVVGI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 80 MMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKhvilTRMGDQLSTA 159
Cdd:PRK13382 99 MCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCPQA----TRIVAWTDED 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 160 KGTLVNFVVkyvkrlvpkyhlpdaisfrrALHAGYRMQyvkPEIVSEDLAFLqyTGGTTGVAKGAMlthrnmlanlEQVN 239
Cdd:PRK13382 175 HDLTVEVLI--------------------AAHAGQRPE---PTGRKGRVILL--TSGTTGTPKGAR----------RSGP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 240 ATYGPL--------LHPGKELVITAlPLYH-------IFALTMNCllfielggqnVLITNPR-DIPGLVKELAKYPFTAM 303
Cdd:PRK13382 220 GGIGTLkaildrtpWRAEEPTVIVA-PMFHawgfsqlVLAASLAC----------TIVTRRRfDPEATLDLIDRHRATGL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 304 TGVNTLFNALLN--NKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIG 381
Cdd:PRK13382 289 AVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 382 LPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYwqRPDATDEIIkDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PRK13382 369 RPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFH-DGFMASGDVGYLDENGRLFVVGRDDEMIVSG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 462 GFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSN 540
Cdd:PRK13382 446 GENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGA 525
|
570
....*....|.
gi 489956626 541 VGKILRRELRD 551
Cdd:PRK13382 526 TGKILRRELQA 536
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
33-549 |
8.02e-54 |
|
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: 189.00 E-value: 8.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 33 VRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRE 112
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALAS-LGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 113 LEHQLNDSGAAAIVIVsnfahtlekvvektqvkhviltrmGDqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralha 192
Cdd:cd05945 80 IREILDAAKPALLIAD------------------------GD-------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 193 gyrmqyvkpeivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtYGPLlhpGKELVITALPLYHiFAL-TMNclL 271
Cdd:cd05945 98 --------------DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLS-DFPL---GPGDVFLNQAPFS-FDLsVMD--L 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 272 FIELGGQNVLITNPRDIPG----LVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLS--AGGGMPVQQAvaERW 345
Cdd:cd05945 157 YPALASGATLVPVPRDATAdpkqLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFlfCGEVLPHKTA--RAL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKLT-GQYLLEGYGLTECAPLVS---VNPHDID-YHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQ 420
Cdd:cd05945 235 QQRFpDARIYNTYGPTEATVAVTyieVTPEVLDgYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLN 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 421 RPDATDE----IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEA 496
Cdd:cd05945 315 NPEKTAAaffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTE 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489956626 497 VKIFVVKKDPSLTED--ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd05945 395 LIAFVVPKPGAEAGLtkAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-550 |
3.90e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 188.29 E-value: 3.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFV--NMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH 115
Cdd:PRK13390 12 DRPAVIvaETGEQVSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 116 QLNDSGAAAIVIVSnfahTLEKVVEKTQVKHVILTRMGdqlstakGTLVNFVvkyvkrlvpkyhlpdaiSFRRALHAGyr 195
Cdd:PRK13390 91 IVGDSGARVLVASA----ALDGLAAKVGADLPLRLSFG-------GEIDGFG-----------------SFEAALAGA-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 196 mqyvKPEIVSEDL-AFLQYTGGTTGVAKGAM--LTHRNMLANLEQVNATYGPLLH-PGKELVITALPLYHIFALTMnCLL 271
Cdd:PRK13390 141 ----GPRLTEQPCgAVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDiSESDIYYSSAPIYHAAPLRW-CSM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 272 FIELGGqNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALL--NNKEFQQLDFSTL----HLSAGGGMPVQQAVAErW 345
Cdd:PRK13390 216 VHALGG-TVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLraviHAAAPCPVDVKHAMID-W 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VkltGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTeAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:PRK13390 294 L---GPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DEIIKDG---WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV- 501
Cdd:PRK13390 370 AAAQHPAhpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIq 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 502 ----VKKDPSLTEDaLITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK13390 450 lvegIRGSDELARE-LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
14-551 |
1.10e-51 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 185.18 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 14 PAEINPDRYQSLIELFEHSVRRYADQ-PAFVNM---GEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPV 89
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKgITYIDAdgsEEFQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 90 ALFGILRAGMIVVNVNPLYTPRELEHQLNDsgaaaiviVSNFAHTLEKVVektqvkhvILT--RMGDQLSTAKGTLVnfv 167
Cdd:cd05906 80 AFWACVLAGFVPAPLTVPPTYDEPNARLRK--------LRHIWQLLGSPV--------VLTdaELVAEFAGLETLSG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 168 vkyvkrlvpkyHLPDAISFRRALHAGYRmQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllH 247
Cdd:cd05906 141 -----------LPGIRVLSIEELLDTAA-DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNG---L 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 248 PGKELVITALPLYHIFALTMNCLLFIELGGQNV------LITNPRDIPGLVKelaKYPFTAMTGVNTLFnALLNNK---- 317
Cdd:cd05906 206 TPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVhvpteeILADPLRWLDLID---RYRVTITWAPNFAF-ALLNDLleei 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 318 EFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLE------GYGLTE-CAPLV-----SVNPHDIDYHSGSIGLPVP 385
Cdd:cd05906 282 EDGTWDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPpdairpAFGMTEtCSGVIysrsfPTYDHSQALEFVSLGRPIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 386 STEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFN 464
Cdd:cd05906 362 GVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFtEDGWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVN 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 465 VYPNEIEDVVMQHSGVLE--VAAVGV--PSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLT---GYKVPKLVEF-RDEL 536
Cdd:cd05906 441 YYSHEIEAAVEEVPGVEPsfTAAFAVrdPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSrevGVSPAYLIPLpKEEI 520
|
570
....*....|....*
gi 489956626 537 PKSNVGKILRRELRD 551
Cdd:cd05906 521 PKTSLGKIQRSKLKA 535
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-555 |
1.41e-51 |
|
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: 190.84 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 4 VWLNRYPADVPAEinpdryQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPN 83
Cdd:COG1020 463 AEWNATAAPYPAD------ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLER 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 84 LLQYPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGAAAIVIVSNFAHTLEKvvekTQVKHVILtrmgDQLSTAkgt 162
Cdd:COG1020 536 SLEMVVALLAVLKAGAAYVPLDPAY-PAErLAYMLEDAGARLVLTQSALAARLPE----LGVPVLAL----DALALA--- 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 163 lvnfvvkyvkrlvpkyHLPDAisfrralhagyrmqYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:COG1020 604 ----------------AEPAT--------------NPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 243 GplLHPG-KELVITAL----PLYHIFAltmnCLLFielGGQNVLITN--PRDIPGLVKELAKYPFTAMTGVNTLFNALLn 315
Cdd:COG1020 654 G--LGPGdRVLQFASLsfdaSVWEIFG----ALLS---GATLVLAPPeaRRDPAALAELLARHRVTVLNLTPSLLRALL- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 316 nkEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQY-LLEGYGLTECAPLVS---VNPHDIDYHSGSIGLPVPSTEAKL 391
Cdd:COG1020 724 --DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGArLVNLYGPTETTVDSTyyeVTPPDADGGSVPIGRPIANTRVYV 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 392 VDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDE------IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGF 463
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKIRGF 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 464 NVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALITFC-RRQLTGYKVPKLVEFRDELPKSNVG 542
Cdd:COG1020 882 RIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGNG 961
|
570
....*....|...
gi 489956626 543 KILRRELRDEARA 555
Cdd:COG1020 962 KLDRLALPAPAAA 974
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-551 |
5.85e-51 |
|
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: 177.91 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtygpLLHPGKELV-ITALPLYHI--FALTMNCLLfieLGGQNVLIT 283
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHS----RLGFGGGDSwLLSLPLYHVggLAILVRSLL---AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 284 NPRDipgLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGmPVQQAVAERWVKLtGQYLLEGYGLTECA 363
Cdd:cd17630 74 RNQA---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGA-PIPPELLERAADR-GIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 364 PLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDednevphgepGELCVRGPQVMLGYWqRPDATDEIIKDGWLHTGDIAVMD 443
Cdd:cd17630 149 SQVATKRPD-GFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL-RGQLVPEFNEDGWFTTKDLGELH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 444 DEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVkIFVVKKDPSLTEDALITFCRRQLTG 523
Cdd:cd17630 217 ADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLAR 295
|
330 340
....*....|....*....|....*...
gi 489956626 524 YKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17630 296 FKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-549 |
1.12e-47 |
|
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: 172.86 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYtPRE-LEHQ 116
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 117 LNDSGAAAIVIVSNFAHTLekvvektqvkHVILTRMGDQLSTAKGTLVNfvvkyvkrlvpkyhlpdaisfrralhagyrm 196
Cdd:cd12116 80 LEDAEPALVLTDDALPDRL----------PAGLPVLLLALAAAAAAPAA------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 197 qyVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITALPLYHIFALTMncLLFIELG 276
Cdd:cd12116 119 --PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLG--LGPGDRLLAVTTYAFDISLLEL--LLPLLAG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 277 GQNVLI--TNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNkEFQQLDfsTLHLSAGGgMPVQQAVAERWVKLTGQyLL 354
Cdd:cd12116 193 ARVVIAprETQRDPEALARLIEAHSITVMQATPATWRMLLDA-GWQGRA--GLTALCGG-EALPPDLAARLLSRVGS-LW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 355 EGYGLTE-----CAPLVSVNPHDIDyhsgsIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII 429
Cdd:cd12116 268 NLYGPTEttiwsTAARVTAAAGPIP-----IGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 430 KDG--------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV 501
Cdd:cd12116 343 VPDpfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVV 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489956626 502 VKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12116 423 LKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-550 |
1.15e-47 |
|
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: 175.37 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRA-LGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 102 VNVNPLYTPRELEHQLNDSGAAAIVIVSNFAH---------TLEKVVEKT-QVKHVILTRMGDQLSTAkgTLVNFVvkyv 171
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADGFTRrgrevnlkeEADKACAQCpTVEKVVVVRHLGNDFTP--AKGRDL---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 172 krlvpKYHLPDAISFRRALHAGyrmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMlanleqvnatygpllhPGKe 251
Cdd:cd05968 218 -----SYDEEKETAGDGAERTE-----------SEDPLMIIYTSGTTGKPKGTVHVHAGF----------------PLK- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 252 lviTALPLYHIFALTMNCLLF-----------------IELGGQNVLITNPRDIPG---LVKELAKYPFTAMTGVNTLFN 311
Cdd:cd05968 265 ---AAQDMYFQFDLKPGDLLTwftdlgwmmgpwlifggLILGATMVLYDGAPDHPKadrLWRMVEDHEITHLGLSPTLIR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 312 ALLNNKE--FQQLDFSTLHLSAGGGMPVQqavAERWvkltgQYLLEGYGLTECaPLvsvnphdIDYHSG----------- 378
Cdd:cd05968 342 ALKPRGDapVNAHDLSSLRVLGSTGEPWN---PEPW-----NWLFETVGKGRN-PI-------INYSGGteisggilgnv 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 379 --------SIGLPVPSTEAKLVDDEDNEVPhGEPGELCVRGPQVML--GYWQRPDATDEI----IKDGWLHtGDIAVMDD 444
Cdd:cd05968 406 likpikpsSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAPWPGMtrGFWRDEDRYLETywsrFDNVWVH-GDFAYYDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 445 EGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD----PSLTEDALITFCRRQ 520
Cdd:cd05968 484 EGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtpTEALAEELMERVADE 563
|
570 580 590
....*....|....*....|....*....|
gi 489956626 521 LTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05968 564 LGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-547 |
3.91e-47 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 172.76 E-value: 3.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAFVNMGE--VMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 102 VNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHtleKVVEKTQVKHVILTRMGDQLSTAKGTLvnfvvkyvkrlvpKYHLP 181
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPH---DRAEPTTRWWPLTVNVGGDSGPSGGTL-------------SVHLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 182 DAISFRRALHAgyrmqyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITaLPLYH 261
Cdd:PRK05852 160 AATEPTPATST--------PEGLRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR--LSPRDATVAV-MPLYH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 262 IFALtMNCLLFIELGGQNVLItnprdiPGLVK--------ELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSTLHLSA 331
Cdd:PRK05852 229 GHGL-IAALLATLASGGAVLL------PARGRfsahtfwdDIKAVGATWYTAVPTIHQILLEraATEPSGRKPAALRFIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 332 GGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHS----GSIGLPVPSTEA--KLVDDEDNEVPHGEPG 405
Cdd:PRK05852 302 SCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvVSTGLVGRSTGAqiRIVGSDGLPLPAGAVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 406 ELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAA 485
Cdd:PRK05852 382 EVWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956626 486 VGVPSGSSGEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRR 547
Cdd:PRK05852 462 FGVPDQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-551 |
4.07e-47 |
|
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: 170.18 E-value: 4.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQ-LGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVivsnfahtlekvvektqvkhviltrmgdqlSTAKGtlvnfvvkyvkrlvpkyhlpdaisf 186
Cdd:cd17653 80 KLPSARIQAILRTSGATLLL------------------------------TTDSP------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITALPLYHIFALT 266
Cdd:cd17653 105 -------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLD--VGPGSRVAQVLSIAFDACIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 267 M-NCLLFielGGQNVLITNPRDIPGLVKELAKYPFTAMtgvntlFNALLNNKEFQQLDFSTLhlsagGGMPVQQAVAERW 345
Cdd:cd17653 164 IfSTLCN---GGTLVLADPSDPFAHVARTVDALMSTPS------ILSTLSPQDFPNLKTIFL-----GGEAVPPSLLDRW 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKltGQYLLEGYGLTECApLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:cd17653 230 SP--GRRLYNAYGPTECT-ISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALT 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DEIIK-----DGWLH--TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVpsgsSGEAVK 498
Cdd:cd17653 307 ASKFVpdpfwPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV----VNGRLV 382
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 499 IFVVKKdpSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:cd17653 383 AFVTPE--TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
27-549 |
7.24e-47 |
|
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: 170.92 E-value: 7.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRA-RGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDqlstakgtlvnfvvkyvkrlvpkyHLPDaisf 186
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPA------------------------TPPL---- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgPLLHPGKELVITALPlyhiFALT 266
Cdd:cd17646 133 --------------VPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY-PLGPGDRVLQKTPLS----FDVS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 267 MNCLLFIELGGQNVLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDfsTLHLSAGGGMPVQQAVAE 343
Cdd:cd17646 194 VWELFWPLVAGARLVVARPgghRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSCA--SLRRVFCSGEALPPELAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RWVKLTGQYLLEGYGLTECAplVSVNPH----DIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYW 419
Cdd:cd17646 272 RFLALPGAELHNLYGPTEAA--IDVTHWpvrgPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDEIIKDGWL-------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGS 492
Cdd:cd17646 350 GRPALTAERFVPDPFgpgsrmyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPA 429
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 493 SGEAVKIFVVKKD--PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17646 430 GAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-476 |
2.21e-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: 170.86 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFA-AYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLY---TPRELEHQLNDSGAAA 124
Cdd:cd05927 6 ISYKEVAERADNIGsALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 125 IVIVSNFAHTLEKVVEKtqvkhviltrMGDqlstakgtlvnfvvKYVKRLVPKyhlpdaisfrralhagyrmqyvKPEiv 204
Cdd:cd05927 83 VFCDAGVKVYSLEEFEK----------LGK--------------KNKVPPPPP----------------------KPE-- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 seDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELV-ITALPLYHIF-ALTMNCLLFIelGGQnvlI 282
Cdd:cd05927 115 --DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyISYLPLAHIFeRVVEALFLYH--GAK---I 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNPR-DIPGLVKELAKYPFTAMTGV----------------------NTLFNALLNNKE-------------FQQLDFST 326
Cdd:cd05927 188 GFYSgDIRLLLDDIKALKPTVFPGVprvlnriydkifnkvqakgplkRKLFNFALNYKLaelrsgvvraspfWDKLVFNK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 327 LHLSAG--------GGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVD----- 393
Cdd:cd05927 268 IKQALGgnvrlmltGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPG-DTSVGHVGGPLPCAEVKLVDvpemn 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 394 -DEDNEVPHGEpgeLCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYPNEI 470
Cdd:cd05927 347 yDAKDPNPRGE---VCIRGPNVFSGYYKDPEKTAEALdEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKI 423
|
....*.
gi 489956626 471 EDVVMQ 476
Cdd:cd05927 424 ENIYAR 429
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
1.44e-45 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 166.15 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVnvnPLYT---PRELEHQLNDSGAaai 125
Cdd:cd05973 1 LTFGELRALSARFANALQE-LGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 vivsnfahtlekvvektqvkHVILTRMgDQLSTakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeiVS 205
Cdd:cd05973 74 --------------------RLVVTDA-ANRHK---------------------------------------------LD 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLAnlEQVNATYGPLLHPGKELVITALP--LYHIFALTMNCLLfieLGGQNVLIT 283
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAVDLRPEDSFWNAADPgwAYGLYYAITGPLA---LGHPTILLE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 284 NPRDIPGLVKELAKYPFTAMTGVNTLFNALL-NNKEFQQLDFSTLHLSAGGGMPVQQAVAeRWVKLT-GQYLLEGYGLTE 361
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTAYRLLMaAGAEVPARPKGRLRRVSSAGEPLTPEVI-RWFDAAlGVPIHDHYGQTE 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 362 CApLVSVNPHDIDY--HSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCV---RGPQVML-GYWQRPDATdeiIKDGWLH 435
Cdd:cd05973 242 LG-MVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMWFrGYQLPDTPA---IDGGYYL 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-----KKDPSLtE 510
Cdd:cd05973 318 TGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlrgghEGTPAL-A 396
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489956626 511 DALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05973 397 DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
28-554 |
5.07e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 164.11 E-value: 5.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 28 LFEHSVRRYADqpafvnmGEVM-----------TFRKLEERSRAFAAYLqEGLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK07008 15 LIAHAARHAGD-------TEIVsrrvegdihryTYRDCERRAKQLAQAL-AALGVEPGDRVGTLAWNGYRHLEAYYGVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 97 AGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEK-TQVKHVILtrMGDqlstakgtlvnfvvkyvkrlv 175
Cdd:PRK07008 87 SGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQcPNVKGWVA--MTD--------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 176 pKYHLP-DAISFR--RALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNmlanleQVNATYGPLLhP---- 248
Cdd:PRK07008 144 -AAHLPaGSTPLLcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHRS------TVLHAYGAAL-Pdamg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 249 --GKELVITALPLYHIFA--LTMNCLLfieLGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDF 324
Cdd:PRK07008 216 lsARDAVLPVVPMFHVNAwgLPYSAPL---TGAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 325 STLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSV----NPHDIDYHSGSI------GLPVPSTEAKLVDD 394
Cdd:PRK07008 293 STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLcklkWKHSQLPLDEQRkllekqGRVIYGVDMKIVGD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 395 EDNEVPH-GEP-GELCVRGPQVMLGYWQRpdaTDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIED 472
Cdd:PRK07008 373 DGRELPWdGKAfGDLQVRGPWVIDRYFRG---DASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIEN 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 473 VVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKK-DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK07008 450 VAVAHPAVAEAACIACAHPKWDERPLLVVVKRpGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
...
gi 489956626 552 EAR 554
Cdd:PRK07008 530 QFR 532
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-550 |
1.01e-43 |
|
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: 162.51 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 29 FEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLqEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLY 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRL-RARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 109 TPRELEHQLNDSGAAAIVIVSNFAHTLEkvvektqVKHVILTRMGDQLSTAKGTLvnfvvkyvkrlvpkyhlpdaiSFRR 188
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELA-------VELVAVTLLDQPGAAAGADA---------------------EPDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 189 ALHAGyrmqyvkpeivseDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQVNATYGPLlHPGKELVITALPLYHIFALTmn 268
Cdd:cd17651 132 ALDAD-------------DLAYVIYTSGSTGRPKGVVMPHR-SLANLVAWQARASSL-GPGARTLQFAGLGFDVSVQE-- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 269 clLFIEL--GGQNVLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLH--LSAGGGMPVQQAVA 342
Cdd:cd17651 195 --IFSTLcaGATLVLPPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRylLTGGEQLVLTEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 343 ERWVKLTGQYLLEGYGLTEcAPLVS--VNPHDIDYH--SGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGY 418
Cdd:cd17651 273 EFCAGLPGLRLHNHYGPTE-THVVTalSLPGDPAAWpaPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGY 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 419 WQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSG 491
Cdd:cd17651 352 LNRPELTAErFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDR 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 492 SSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17651 432 PGEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
31-553 |
3.23e-43 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 162.28 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 31 HSVRRYADQPAFVNmgEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTP 110
Cdd:PLN02860 17 ATLRGNAVVTISGN--RRRTGHEFVDGVLSLAAGLLR-LGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 111 RELEHQLNDSGAAAIVIVSNFAHTLEKVvEKTQVKHVILTRMGDQLSTAKGT-LVNFV-VKYVKRLVPKYHLPDaisfrr 188
Cdd:PLN02860 94 EEAKSAMLLVRPVMLVTDETCSSWYEEL-QNDRLPSLMWQVFLESPSSSVFIfLNSFLtTEMLKQRALGTTELD------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 189 alhagyrmqyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNM----LANLEQVNatYGP---LLHpgkelviTAlPLYH 261
Cdd:PLN02860 167 ------------YAWAPDDAVLICFTSGTTGRPKGVTISHSALivqsLAKIAIVG--YGEddvYLH-------TA-PLCH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 262 IFALTmNCLLFIELGGQNVLItnPR-DIPGLVKELAKYPFTAMTGVNTLFNALL-------NNKEFQQLdfsTLHLSAGG 333
Cdd:PLN02860 225 IGGLS-SALAMLMVGACHVLL--PKfDAKAALQAIKQHNVTSMITVPAMMADLIsltrksmTWKVFPSV---RKILNGGG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GMPVQqaVAERWVKL-TGQYLLEGYGLTE-CAPLVSVNPHDID---------------------YHSGSIGLPVPSTEAK 390
Cdd:PLN02860 299 SLSSR--LLPDAKKLfPNAKLFSAYGMTEaCSSLTFMTLHDPTlespkqtlqtvnqtksssvhqPQGVCVGKPAPHVELK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 391 LVDDEDNEVphgepGELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PLN02860 377 IGLDESSRV-----GRILTRGPHVMLGYWGQNSETASVLsNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 470 IEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV---------------VKKDPSLTEDALITFCRRQ-LTGYKVPKL-VEF 532
Cdd:PLN02860 452 VEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdnekenAKKNLTLSSETLRHHCREKnLSRFKIPKLfVQW 531
|
570 580
....*....|....*....|.
gi 489956626 533 RDELPKSNVGKILRRELRDEA 553
Cdd:PLN02860 532 RKPFPLTTTGKIRRDEVRREV 552
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-544 |
6.85e-43 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 164.75 E-value: 6.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEGLGLqkGDRVALMMPNLLQYPVALFGILRAGMIVVNVNplYTprelehqlndSGAAAI 125
Cdd:PRK06814 656 NGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FS----------AGIANI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNFAhtlekvvektQVKHVILTR-------MGDqLSTAKGTLVNFVvkYVKRLVPKYHLPDAIsfrRALHAGYRMQY 198
Cdd:PRK06814 722 LSACKAA----------QVKTVLTSRafiekarLGP-LIEALEFGIRII--YLEDVRAQIGLADKI---KGLLAGRFPLV 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 199 VKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGkELVITALPLYHIFALTMNCLLFIELGGQ 278
Cdd:PRK06814 786 YFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--FSPE-DKVFNALPVFHSFGLTGGLVLPLLSGVK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 279 NVLITNP---RDIPGLVKELAKypfTAMTGVNTLFNALLNNKefQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLE 355
Cdd:PRK06814 863 VFLYPSPlhyRIIPELIYDTNA---TILFGTDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILE 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 356 GYGLTECAPLVSVN-P-HDidyHSGSIGLPVPSTEAKLVddednEVPhG--EPGELCVRGPQVMLGYWqRPDA--TDEII 429
Cdd:PRK06814 938 GYGVTETAPVIALNtPmHN---KAGTVGRLLPGIEYRLE-----PVP-GidEGGRLFVRGPNVMLGYL-RAENpgVLEPP 1007
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 430 KDGWLHTGDIAVMDDEGFLRIVDRKK-------DMILVSGFNVYPNEIeDVVMQHsgvlevAAVGVPSGSSGEavKIFVV 502
Cdd:PRK06814 1008 ADGWYDTGDIVTIDEEGFITIKGRAKrfakiagEMISLAAVEELAAEL-WPDALH------AAVSIPDARKGE--RIILL 1078
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489956626 503 KKDPSLTEDALITFCR-RQLTGYKVPKLVEFRDELPKSNVGKI 544
Cdd:PRK06814 1079 TTASDATRAAFLAHAKaAGASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-546 |
2.13e-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: 155.11 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLE-----QVNATYGpllhpgkELVITALPLYHIFAL--TMNCLLFielGGQ 278
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDilqkeGLNWVVG-------DVTYLPLPATHIGGLwwILTCLIH---GGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 279 NVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLN-----NKEFQQLDFstlhLSAGGGMPVQQ--AVAErWVKLTGq 351
Cdd:cd17635 71 CVTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSelksaNATVPSLRL----IGYGGSRAIAAdvRFIE-ATGLTN- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 352 yLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKD 431
Cdd:cd17635 145 -TAQVYGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 432 GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVK---KDPSL 508
Cdd:cd17635 224 GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENA 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 489956626 509 TEdALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:cd17635 304 IR-ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
27-549 |
2.15e-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: 158.64 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVIVSNFAHTLEkvvektQVKHVILTrmgDQLSTAKGTLVNFvvkyvkrlvpkyhlpdaisf 186
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHLQPPIA------FIGLIDLL---DEDTIYHEESENL-------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHPGKELVITALPLYHiFALT 266
Cdd:cd17655 131 -------------EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI----YQGEHLRVALFASIS-FDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 267 MNCLLFIELGGqNVLITNPR----DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLhLSAGGGMPVQqaVA 342
Cdd:cd17655 193 VTEIFASLLSG-NTLYIVRKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL-IVGGEALSTE--LA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 343 ERWVKLTGQ--YLLEGYGLTE---CAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLG 417
Cdd:cd17655 269 KKIIELFGTnpTITNAYGPTEttvDASIYQYEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 418 YWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEvAAVGVPS 490
Cdd:cd17655 349 YLNRPELTAEkFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKE-AVVIARK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 491 GSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17655 428 DEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
6-473 |
2.55e-42 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 161.04 E-value: 2.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 6 LNRYPaDVPaEInpdryQSLIELFEHSVRRYADQPAFVN-------MGEV--MTFRKL-EERSRAFAAYLQegLGLQKGD 75
Cdd:PLN02736 34 VSRFP-DHP-EI-----GTLHDNFVYAVETFRDYKYLGTrirvdgtVGEYkwMTYGEAgTARTAIGSGLVQ--HGIPKGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 76 RVALMMPNLLQYPVALFGILRAGMIVVnvnPLYtprelehqlnDS-GAAAIVIVSNFAhtlekVVEKTQVKHVILTRMGD 154
Cdd:PLN02736 105 CVGLYFINRPEWLIVDHACSAYSYVSV---PLY----------DTlGPDAVKFIVNHA-----EVAAIFCVPQTLNTLLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 155 QLSTAKGTLVNFVVKYVKRLVPKyhLPDA-----ISFRRALHAGYRMQ--YVKPEivSEDLAFLQYTGGTTGVAKGAMLT 227
Cdd:PLN02736 167 CLSEIPSVRLIVVVGGADEPLPS--LPSGtgveiVTYSKLLAQGRSSPqpFRPPK--PEDVATICYTSGTTGTPKGVVLT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 228 HRNMLANLeqVNATYGPLLHPGkELVITALPLYHIFAlTMNCLLFIELG-------GQN-------------VLITNPR- 286
Cdd:PLN02736 243 HGNLIANV--AGSSLSTKFYPS-DVHISYLPLAHIYE-RVNQIVMLHYGvavgfyqGDNlklmddlaalrptIFCSVPRl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 ------DIPGLVKE---LAKYPFTAmtGVNTLFNALLNNKE----FQQLDFSTLHLSAGGGM--------PVQQAVAERW 345
Cdd:PLN02736 319 ynriydGITNAVKEsggLKERLFNA--AYNAKKQALENGKNpspmWDRLVFNKIKAKLGGRVrfmssgasPLSPDVMEFL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKLTGQYLLEGYGLTECAPLVSvNPHDIDYHSGSIGLPVPSTEAKLVD-------DEDNEVPHGEpgeLCVRGPQVMLGY 418
Cdd:PLN02736 397 RICFGGRVLEGYGMTETSCVIS-GMDEGDNLSGHVGSPNPACEVKLVDvpemnytSEDQPYPRGE---ICVRGPIIFKGY 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 419 WQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMI-LVSGFNVYPNEIEDV 473
Cdd:PLN02736 473 YKDEVQTREVIdEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENV 529
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
27-549 |
2.58e-42 |
|
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: 157.48 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAaivivsnfahtlekvvektqvkhVILTRmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisf 186
Cdd:cd12115 82 AYPPERLRFILEDAQAR-----------------------LVLTD----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllhPGKEL--VITA------LP 258
Cdd:cd12115 104 ------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAF-----SAEELagVLAStsicfdLS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 259 LYHIFAlTMNCllfielGGQNVLITNPRDIPGLVkelAKYPFTAMTGVNTLFNALLNNKEFQQlDFSTLHLsAGGGMPvQ 338
Cdd:cd12115 161 VFELFG-PLAT------GGKVVLADNVLALPDLP---AAAEVTLINTVPSAAAELLRHDALPA-SVRVVNL-AGEPLP-R 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 339 QAVAERWVKLTGQYLLEGYGLTEC---APLVSVNPHDIDyhSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVM 415
Cdd:cd12115 228 DLVQRLYARLQVERVVNLYGPSEDttySTVAPVPPGASG--EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVA 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 416 LGYWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGV 488
Cdd:cd12115 306 RGYLGRPGLTAErFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAI 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956626 489 PSGSSGEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12115 386 GDAAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-546 |
2.62e-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: 154.10 E-value: 2.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 213 YTGGTTGVAKGAMLTHRNMLANLEqVNATygpLLHPGKELVITAL-PLYHifALTMNCLLFIELGGQNVLITNPRDIPGL 291
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFV-CNED---LFNISGEDAILAPgPLSH--SLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 292 VKELAKYPFTAMTGVNTLFNALLNNkEFQQLDFSTLhLSAGGGMP--VQQAVAERWVKLTgqyLLEGYGLTEcAPLVSVN 369
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFesTKKKLKNIFPKAN---LIEFYGTSE-LSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 370 PHDIDYHSGSIGLPVPSTEAKLVDDEDNEVphgepGELCVRGPQVMLGYWQrpdaTDEIIKDGWLHTGDIAVMDDEGFLR 449
Cdd:cd17633 155 FNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVR----GGFSNPDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVkIFVVKKDpSLTEDALITFCRRQLTGYKVPKL 529
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*..
gi 489956626 530 VEFRDELPKSNVGKILR 546
Cdd:cd17633 304 IIFVDSLPYTSSGKIAR 320
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-552 |
1.98e-41 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 156.84 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLqEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:PRK06018 41 TYAQIHDRALKVSQAL-DRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 NFAHTLEKVVektqvkhviltrmgDQLSTAKgtlvNFVVKYVKRLVPKYHLPDAISFRRALhAGYRMQYVKPEIVSEDLA 209
Cdd:PRK06018 120 TFVPILEKIA--------------DKLPSVE----RYVVLTDAAHMPQTTLKNAVAYEEWI-AEADGDFAWKTFDENTAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHR-NMLANLEQVNAtyGPLLHPGKELVITALPLYHIFA--LTMNCllfiELGGQNVLITNPR 286
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHRsNVLHALMANNG--DALGTSAADTMLPVVPLFHANSwgIAFSA----PSMGTKLVMPGAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKEL---AKYPFTAmtGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLtGQYLLEGYGLTECA 363
Cdd:PRK06018 255 LDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 364 PL--VSVNPHDIDYHSGSI--------GLPVPSTEAKLVDDEDNEVPHG--EPGELCVRGPQVMLGYWQrpdATDEII-K 430
Cdd:PRK06018 332 PLgtLAALKPPFSKLPGDArldvlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYR---VDGEILdD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 431 DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGE-AVKIFVVKKDPSLT 509
Cdd:PRK06018 409 DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErPLLIVQLKPGETAT 488
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489956626 510 EDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDE 552
Cdd:PRK06018 489 REEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
49-458 |
5.78e-41 |
|
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: 155.07 E-value: 5.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVnplY-TPRE--LEHQLNDSGAAAI 125
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVE-LGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTV---YaTLGEdaLIHSLNETECSAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivS 205
Cdd:cd17639 82 FTDGK--------------------------------------------------------------------------P 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVITALPLYHIFALTM-NCLLFIelggqNVLI-- 282
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAeNVCLYR-----GGTIgy 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNPRDIPGLVK-----ELAKYPFTAMTGV----------------------NTLFNALLNNKEFQQLD-----------F 324
Cdd:cd17639 162 GSPRTLTDKSKrgckgDLTEFKPTLMVGVpaiwdtirkgvlaklnpmgglkRTLFWTAYQSKLKALKEgpgtplldelvF 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 325 STLHLSAG--------GGMPVQQAvAERWVKLTGQYLLEGYGLTE-CAPLVSVNPHDIDYhsGSIGLPVPSTEAKLVD-D 394
Cdd:cd17639 242 KKVRAALGgrlrymlsGGAPLSAD-TQEFLNIVLCPVIQGYGLTEtCAGGTVQDPGDLET--GRVGPPLPCCEIKLVDwE 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 395 EDNEVPHGEP--GELCVRGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMI 458
Cdd:cd17639 319 EGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDgDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-555 |
7.93e-41 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 155.77 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 12 DVPAeiNPDRYQSLIELF--EHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYL-QEGLGLqkGDRVALMMPNLLQYP 88
Cdd:PLN02479 9 DLPK--NAANYTALTPLWflERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALaKRSIGP--GSTVAVIAPNIPAMY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 89 VALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVE------KTQVKHVILTRMGDQLSTAKGT 162
Cdd:PLN02479 85 EAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKilaekkKSSFKPPLLIVIGDPTCDPKSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 163 lvnfvvkyvkrlvpKYHLPD-AISFRRALHAG-YRMQYVKPEIVSEDLAfLQYTGGTTGVAKGAMLTHRNMLanleqVNA 240
Cdd:PLN02479 165 --------------QYALGKgAIEYEKFLETGdPEFAWKPPADEWQSIA-LGYTSGTTASPKGVVLHHRGAY-----LMA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 241 TYGPLL--HPGKELVITALPLYHI----FALTMNCLLfielgGQNVLItnpRDIP--GLVKELAKYPFTAMTGVNTLFNA 312
Cdd:PLN02479 225 LSNALIwgMNEGAVYLWTLPMFHCngwcFTWTLAALC-----GTNICL---RQVTakAIYSAIANYGVTHFCAAPVVLNT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 313 LLNN-KEFQQLDFS-TLHLSAGGGMP---VQQAVAERWVKLTGQY-LLEGYG-LTECA--------PLVS---------- 367
Cdd:PLN02479 297 IVNApKSETILPLPrVVHVMTAGAAPppsVLFAMSEKGFRVTHTYgLSETYGpSTVCAwkpewdslPPEEqarlnarqgv 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 368 --VNPHDIDYHSGSIGLPVPSTEAKLvddednevphgepGELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDE 445
Cdd:PLN02479 377 ryIGLEGLDVVDTKTMKPVPADGKTM-------------GEIVMRGNMVMKGYLKNPKANEEAFANGWFHSGDLGVKHPD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 446 GFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-------PSLTEDaLITFCR 518
Cdd:PLN02479 444 GYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPgvdksdeAALAED-IMKFCR 522
|
570 580 590
....*....|....*....|....*....|....*..
gi 489956626 519 RQLTGYKVPKLVEFrDELPKSNVGKILRRELRDEARA 555
Cdd:PLN02479 523 ERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKAKE 558
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
211-557 |
8.86e-41 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 155.56 E-value: 8.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 211 LQYTGGTTGVAKGAMLTHRNmlANLEQVNATYGPLLHPGKELVITaLPLYHIFALTMNCLLFIElGGQNVLITNPrDIPG 290
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGTCPVYLWT-LPMFHCNGWTFTWGTAAR-GGTSVCMRHV-TAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 291 LVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFST-LHLSAGGGMPvqQAVAERWVKLTGQYLLEGYGLTEC-APLVSV 368
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGpVHVLTGGSPP--PAALVKKVQRLGFQVMHAYGLTEAtGPVLFC 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 369 NPHD------------IDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEP-GELCVRGPQVMLGYWQRPDATDEIIKDGWLH 435
Cdd:PLN03102 344 EWQDewnrlpenqqmeLKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAFKHGWLN 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLT------ 509
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTkedrvd 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489956626 510 -----EDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKV 557
Cdd:PLN03102 504 klvtrERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLV 556
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
38-550 |
1.20e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 153.78 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKgdRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVIvsnfahtlekvvektqvkhviLTRMGDQLSTAKGTLVNfvVKYVKRLVPKYhLPDAISFRRALHAGYRMQ 197
Cdd:PRK07638 94 AISNADMIVT---------------------ERYKLNDLPDEEGRVIE--IDEWKRMIEKY-LPTYAPIENVQNAPFYMG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 YvkpeivsedlaflqyTGGTTGVAKGAMLTHRNMLANLeQVNATYGPLLHPGKELVITALpLYHIFALTMNCLLFIelgG 277
Cdd:PRK07638 150 F---------------TSGSTGKPKAFLRAQQSWLHSF-DCNVHDFHMKREDSVLIAGTL-VHSLFLYGAISTLYV---G 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 QNVLITnPRDIPGLVKE-LAKYPFTAMTGVNTLFNALLNNKEFqqLDFSTLHLSAGG--GMPVQQAVAERWVKLTgqyLL 354
Cdd:PRK07638 210 QTVHLM-RKFIPNQVLDkLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGAkwEAEAKEKIKNIFPYAK---LY 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 355 EGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGWL 434
Cdd:PRK07638 284 EFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARELNADGWM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 435 HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEavkIFVVKKDPSLTEDALI 514
Cdd:PRK07638 364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE---KPVAIIKGSATKQQLK 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 489956626 515 TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07638 441 SFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-553 |
6.46e-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: 151.54 E-value: 6.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRS-LGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYtPRE-LEHQLNDSGAAaIVIVSNfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdais 185
Cdd:cd05918 82 SH-PLQrLQEILQDTGAK-VVLTSS------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 186 frralhagyrmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQvnatYGPLLHPGKE---LVITA----LP 258
Cdd:cd05918 105 -------------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALA----HGRALGLTSEsrvLQFASytfdVS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 259 LYHIFAlTMNCllfielGGqNVLITNPRDIPGlvkELAKYpFTAMtGVNTLF-----NALLNNKEFQQLdfSTLHLsagG 333
Cdd:cd05918 162 ILEIFT-TLAA------GG-CLCIPSEEDRLN---DLAGF-INRL-RVTWAFltpsvARLLDPEDVPSL--RTLVL---G 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GMPVQQAVAERWVKLTGqyLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTeAKLVD--DEDNEVPHGEPGELCVRG 411
Cdd:cd05918 224 GEALTQSDVDTWADRVR--LINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEG 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 412 PQVMLGYWQRPDATDEI-IKD-GWLH------------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:cd05918 301 PILARGYLNDPEKTAAAfIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQS 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 478 SGVLEVAAVGV--PSGSSGEAVKI-FVVKKDPSLTED------------------ALITFCRRQLTGYKVPKLVEFRDEL 536
Cdd:cd05918 381 LPGAKEVVVEVvkPKDGSSSPQLVaFVVLDGSSSGSGdgdslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHL 460
|
570
....*....|....*..
gi 489956626 537 PKSNVGKILRRELRDEA 553
Cdd:cd05918 461 PLTASGKIDRRALRELA 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-549 |
2.41e-39 |
|
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: 149.73 E-value: 2.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvVEKTQVKHVILTrmgdqlstakgtlvnfvvkyvkrlvpkyhlPDAISFRRALHAGYRMQ 197
Cdd:cd12114 81 ADAGARLVL------------TDGPDAQLDVAV------------------------------FDVLILDLDALAAPAPP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYgpllHPGKELVITA-------LPLYHIFALTmncl 270
Cdd:cd12114 119 -PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF----AVGPDDRVLAlsslsfdLSVYDIFGAL---- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 271 lfiELGGQNVLITNPRDI-PGLVKELA-KYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKL 348
Cdd:cd12114 190 ---SAGATLVLPDEARRRdPAHWAELIeRHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 349 TGQYLLEGYG-LTECA------PLVSVNPHDidyhsGSI--GLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYW 419
Cdd:cd12114 267 APDARLISLGgATEASiwsiyhPIDEVPPDW-----RSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDE---IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGsSG 494
Cdd:cd12114 342 GDPELTAArfvTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GG 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 495 EAVKIFVV--KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd12114 421 KRLAAFVVpdNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-549 |
2.62e-39 |
|
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: 149.38 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRA-EGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmq 197
Cdd:cd17643 81 ADSGPSLLL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yVKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY------------------------GPLLHpGKELV 253
Cdd:cd17643 90 -TDPD----DLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFgfneddvwtlfhsyafdfsvweiwGALLH-GGRLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 254 ItalPLYHIfALTmncllfielggqnvlitnPRDIPGLVKELAkypFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGG 333
Cdd:cd17643 164 V---VPYEV-ARS------------------PEDFARLLRDEG---VTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GMPVQQAVAERWVK---LTGQYLLEGYGLTECAPLVS---VNPHDIDYHSGS-IGLPVPSTEAKLVDDEDNEVPHGEPGE 406
Cdd:cd17643 219 GEALEAAMLRPWAGrfgLDRPQLVNMYGITETTVHVTfrpLDAADLPAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGE 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 407 LCVRGPQVMLGYWQRPDATDEIIKDG--------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:cd17643 299 LYVSGAGVARGYLGRPELTAERFVANpfggpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHP 378
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956626 479 GVLEvAAVGVPSGSSGEA--VKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17643 379 SVRD-AAVIVREDEPGDTrlVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
34-501 |
2.05e-38 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 149.00 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 34 RRYADQPAFV--------------------NMGEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFG 93
Cdd:PRK09192 15 RRYADFPTLVealdyaalgeagmnfydrrgQLEEALPYQTLRARAEAGARRLL-ALGLKPGDRVALIAETDGDFVEAFFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 94 ILRAGMIVVnvnPLYTP-----RE-----LEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHViltrmgdqlstakGTL 163
Cdd:PRK09192 94 CQYAGLVPV---PLPLPmgfggREsyiaqLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHV-------------LSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 164 VNFvvkyvkrlvpkYHLPDAISfrrALhagyrmqyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeQVNATYG 243
Cdd:PRK09192 158 AWF-----------KALPEADV---AL----------PRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL-RAISHDG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 244 PLLHPGkELVITALPLYHIFALtMNCLLFIeLGGQ---NVLITNprdipglvkELAKYPF---------TAMTGVNTLFN 311
Cdd:PRK09192 213 LKVRPG-DRCVSWLPFYHDMGL-VGFLLTP-VATQlsvDYLPTR---------DFARRPLqwldlisrnRGTISYSPPFG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 312 ALLNNKEFQQLDFSTLHLS----AGGG-----MPVQQAVAERW--VKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSI 380
Cdd:PRK09192 281 YELCARRVNSKDLAELDLScwrvAGIGadmirPDVLHQFAEAFapAGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 381 ---------------------------GLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIKDGW 433
Cdd:PRK09192 361 drdrleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGW 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 434 LHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVL--EVAAVGVPSGsSGEAVKIFV 501
Cdd:PRK09192 441 LDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE-NGEKIVLLV 508
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-545 |
3.34e-38 |
|
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: 148.49 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 33 VRRYADQPAFVNMGE------VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17634 63 LRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVIVSNFahtlekvVEKTQVkhVILTRMGDQLSTAKGTLVNFVVKYVKRLVPKYHLPDAISF 186
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLITADGG-------VRAGRS--VPLKKNVDDALNPNVTSVEHVIVLKRTGSDIDWQEGRDLW 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 RRALHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAtYGPLLHPGkELVITALPL------- 259
Cdd:cd17634 213 WRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMK-YVFDYGPG-DIYWCTADVgwvtghs 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 260 ---YHIFALTMNCLLF---------------IELGGQNVLITNPRDIPGLVKElakypftamtgvntlfnallNNKEFQQ 321
Cdd:cd17634 291 yllYGPLACGATTLLYegvpnwptparmwqvVDKHGVNILYTAPTAIRALMAA--------------------GDDAIEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 322 LDFSTLHLSAGGGMPVQQAVAERWVKLTGQY---LLEGYGLTECA-PLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDN 397
Cdd:cd17634 351 TDRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGgFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGH 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 398 EVPHGEPGELCVRG--PQVMLGYWQRPDATDEIIK---DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIED 472
Cdd:cd17634 431 PQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYFstfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIES 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 473 VVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKK----DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:cd17634 511 VLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
24-552 |
5.31e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 148.34 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPA--FVNM-----GEV--MTFRKLEERSRAFAAYLQEGLglQKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAyrFLDFsterdGVArdLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLYTPRELEHqlndsgaaaivivsnfAHTLEKVVEKTQVKhVILTRMGdqlsTAKGtlvnfVVKYVKRL 174
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDDCTPS-AILTTTD----SAEG-----VRKFFRAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 VPKYH--------LPDAISfrralhagyrMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV-NATYGPL 245
Cdd:PRK07769 151 PAKERprviavdaVPDEVG----------ATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQViDALEGQE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 246 LHPGkelvITALPLYHIFALTMncLLFIELGGQNVLITNPRDI---PG-LVKELAKYPftamTGVNTLFNALLN------ 315
Cdd:PRK07769 221 GDRG----VSWLPFFHDMGLIT--VLLPALLGHYITFMSPAAFvrrPGrWIRELARKP----GGTGGTFSAAPNfafeha 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 316 -----NKEFQQ-LDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLE------GYGLTECAPLVSVNPHD-------IDYH 376
Cdd:PRK07769 291 aarglPKDGEPpLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVSTTPMDeeptviyVDRD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 377 SGSIG--LPVPSTE-----------------AKLVDDE-DNEVPHGEPGELCVRGPQVMLGYWQRPDATDEIIK------ 430
Cdd:PRK07769 371 ELNAGrfVEVPADApnavaqvsagkvgvsewAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksr 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 431 ------------DGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE---VAAVGVPSGSSGE 495
Cdd:PRK07769 451 lseshaegapddALWVRTGDYGVYFD-GELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRtgyVAAFSVPANQLPQ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 496 AV---KIFVVKKDPSLTEDALITFCRRQLTGYK---------------VPKLVEFRDEL-------PKSNVGKILRRELR 550
Cdd:PRK07769 530 VVfddSHAGLKFDPEDTSEQLVIVAERAPGAHKldpqpiaddiraaiaVRHGVTVRDVLlvpagsiPRTSSGKIARRACR 609
|
..
gi 489956626 551 DE 552
Cdd:PRK07769 610 AA 611
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
36-556 |
5.68e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 149.03 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 36 YADQPAFVnMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH 115
Cdd:PRK06060 19 WYDRPAFY-AADVVTHGQIHDGAARLGEVLRN-RGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 116 QLNDSgAAAIVIVSNfahtleKVVEKTQVKHVIltRMGDQLSTAKgtlvnfvvkyvkrlvpkyhlpdaisfrRALHAGYr 195
Cdd:PRK06060 97 AARNT-EPALVVTSD------ALRDRFQPSRVA--EAAELMSEAA---------------------------RVAPGGY- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 196 mqyvkpEIVSED-LAFLQYTGGTTGVAKGAMLTHRNMLANLEQV--NATYgplLHPgKELVITALPLYHIFALTMNCLLF 272
Cdd:PRK06060 140 ------EPMGGDaLAYATYTSGTTGPPKAAIHRHADPLTFVDAMcrKALR---LTP-EDTGLCSARMYFAYGLGNSVWFP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 273 IELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQldFSTLHLSAGGGMPVQQAVAERWVKLTGQY 352
Cdd:PRK06060 210 LATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFARVIDSCSPDS--FRSLRCVVSAGEALELGLAERLMEFFGGI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 -LLEGYGLTECAPLVSVNPHDiDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDA--TDEii 429
Cdd:PRK06060 288 pILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSpvANE-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 430 kdGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLT 509
Cdd:PRK06060 365 --GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATI 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489956626 510 EDALITFCRR----QLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
Cdd:PRK06060 443 DGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-487 |
1.00e-36 |
|
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: 142.99 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIvivs 129
Cdd:cd05932 8 TWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 nfahtlekvvektqvkhvILTRMGDQLSTAKGtlvnfvvkyVKRLVPKYHLP--DAISFRR---ALHAGYRMQYVKPEIV 204
Cdd:cd05932 83 ------------------FVGKLDDWKAMAPG---------VPEGLISISLPppSAANCQYqwdDLIAQHPPLEERPTRF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhPGKELVITALPLYHIFALTmncllFIELGG--QNVLI 282
Cdd:cd05932 136 PEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGT---EENDRMLSYLPLAHVTERV-----FVEGGSlyGGVLV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 TNPRDIPGLVKELAKYPFTAMTGVN---TLF----------------------NALLNNKEFQQLDFSTLHLSAGGGMPV 337
Cdd:cd05932 208 AFAESLDTFVEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkipvvNSLVKRKVLKGLGLDQCRLAGCGSAPV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 338 QQAVAErWVKLTGQYLLEGYGLTE-CAplVSVNPHDIDYHSGSIGLPVPSTEAKLVDDednevphgepGELCVRGPQVML 416
Cdd:cd05932 288 PPALLE-WYRSLGLNILEAYGMTEnFA--YSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMM 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489956626 417 GYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:cd05932 355 GYYKDPEATAEAFtADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
47-474 |
1.44e-36 |
|
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: 143.65 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 47 EVMTFRKLEERSRAFA-AYLQegLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSgAAAI 125
Cdd:cd05933 7 HTLTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNfAHTLEKVvekTQVKhviltrmgDQLSTAKGtlvnfVVKYvkRLVPKYHLPDAISFRRALHAGY---------RM 196
Cdd:cd05933 84 LVVEN-QKQLQKI---LQIQ--------DKLPHLKA-----IIQY--KEPLKEKEPNLYSWDEFMELGRsipdeqldaII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 197 QYVKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHP-GKELVITALPLYHIFALTMNCLLFIEL 275
Cdd:cd05933 145 SSQKPN----QCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvGQESVVSYLPLSHIAAQILDIWLPIKV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 276 GGQnVLITNPRDIPG-LVKELAKYPFTAMTGV------------------------------------------------ 306
Cdd:cd05933 221 GGQ-VYFAQPDALKGtLVKTLREVRPTAFMGVprvwekiqekmkavgaksgtlkrkiaswakgvgletnlklmggespsp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 307 --NTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQyLLEGYGLTECAPLVSVNpHDIDYHSGSIGLPV 384
Cdd:cd05933 300 lfYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLSLNIP-IMELYGMSETSGPHTIS-NPQAYRLLSCGKAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 385 PSTEAKLVDDEDNEVphgepGELCVRGPQVMLGYWQRPDATDEIIK-DGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-G 462
Cdd:cd05933 378 PGCKTKIHNPDADGI-----GEICFWGRHVFMGYLNMEDKTEEAIDeDGWLHSGDLGKLDEDGFLYITGRIKELIITAgG 452
|
490
....*....|..
gi 489956626 463 FNVYPNEIEDVV 474
Cdd:cd05933 453 ENVPPVPIEDAV 464
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
27-549 |
8.20e-36 |
|
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: 139.23 E-value: 8.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGK-GVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAaiVIVSNfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisf 186
Cdd:cd17645 81 DYPGERIAYMLADSSAK--ILLTN-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLHPGKELVITALPlYHIFALT 266
Cdd:cd17645 103 ------------------PDDLAYVIYTSGSTGLPKGVMIEHHN-LVNLCEWHRPYFGVTPADKSLVYASFS-FDASAWE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 267 MncllFIELGGQNVLITNPRDIPGLVKELAKYPFTamTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAErwv 346
Cdd:cd17645 163 I----FPHLTAGAALHVVPSERRLDLDALNDYFNQ--EGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK--- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 347 kltGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAkLVDDEDNEV-PHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:cd17645 234 ---GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRV-YILDEALQLqPIGVAGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 DE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVK 498
Cdd:cd17645 310 AEkFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489956626 499 IFVVKKDPSLTEdALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17645 390 AYVTAPEEIPHE-ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-549 |
1.13e-35 |
|
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: 138.54 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAA-RGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvvekTQVkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmq 197
Cdd:cd17652 81 ADARPALLL---------------TTP----------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLlHPGKELVITALPLYHIFALTMnCLLFIElGG 277
Cdd:cd17652 93 --------DNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDV-GPGSRVLQFASPSFDASVWEL-LMALLA-GA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 QNVLITNPRDIPG--LVKELAKYPFTAMTGVNTLFNALlnnKEFQQLDFSTLHLsagGGMPVQQAVAERWVKltGQYLLE 355
Cdd:cd17652 161 TLVLAPAEELLPGepLADLLREHRITHVTLPPAALAAL---PPDDLPDLRTLVV---AGEACPAELVDRWAP--GRRMIN 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 356 GYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKD--- 431
Cdd:cd17652 233 AYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErFVADpfg 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 432 ---GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEvAAVGVPSGSSGEA--VKIFVVKKD 505
Cdd:cd17652 313 apgSRMYrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKrlVAYVVPAPG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 489956626 506 PSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17652 392 AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
23-543 |
1.40e-35 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 141.77 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRY-ADQPAF--VNMGEvMTFRKLEERSRAFAAYLQEGLglQKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:PRK08043 204 ETLYEALLSAQYRYgAGKPCIedVNFTP-DSYRKLLKKTLFVGRILEKYS--VEGERIGLMLPNATISAAVIFGASLRRR 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNplYTP--RELEHQLNDSGAAAIVIVSNF------AHTLEKVvekTQVKHVILTRMGDQLSTAKGTLVNFvvkyv 171
Cdd:PRK08043 281 IPAMMN--YTAgvKGLTSAITAAEIKTIFTSRQFldkgklWHLPEQL---TQVRWVYLEDLKDDVTTADKLWIFA----- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 172 KRLVPkyhlpdaisfRRAlhagyrMQYVKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVN--ATYGPllhpg 249
Cdd:PRK08043 351 HLLMP----------RLA------QVKQQPE----DAALILFTSGSEGHPKGVVHSHKSLLANVEQIKtiADFTP----- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 250 KELVITALPLYHIFALTMNCLLFIELGGQNVLITNP---RDIPGLVKELAkypFTAMTGVNTLfnaLLNNKEFQQ-LDFS 325
Cdd:PRK08043 406 NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSPlhyRIVPELVYDRN---CTVLFGTSTF---LGNYARFANpYDFA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 326 TLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVN-PhdIDYHSGSIGLPVPSTEAKLVddednEVP---H 401
Cdd:PRK08043 480 RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINvP--MAAKPGTVGRILPGMDARLL-----SVPgieQ 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 402 GepGELCVRGPQVMLGY--------WQRPDATDE--IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIE 471
Cdd:PRK08043 553 G--GRLQLKGPNIMNGYlrvekpgvLEVPTAENArgEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVE 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 472 DVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVkkDPSLTEDALITFCRR----QLTgykVPKLVEFRDELPKSNVGK 543
Cdd:PRK08043 631 QLALGVSPDKQHATAIKSDASKGEALVLFTT--DSELTREKLQQYAREhgvpELA---VPRDIRYLKQLPLLGSGK 701
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-543 |
3.65e-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: 135.59 E-value: 3.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 SEDLAFLQYTGGTTGVAKGAMLTH---RNML---ANLEQVNATYGPLLHPGKE-----LVITALPLYHifALTMNCLLFI 273
Cdd:cd05924 2 SADDLYILYTGGTTGMPKGVMWRQediFRMLmggADFGTGEFTPSEDAHKAAAaaagtVMFPAPPLMH--GTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 274 ELGGQNVLITNPR-DIPGLVKELAKYPFTAMTGVNT-----LFNALLNNKEFqqlDFSTLHLSAGGGMPVQQAVAERWVK 347
Cdd:cd05924 80 LLGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVGDamarpLIDALRDAGPY---DLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 348 LTGQ-YLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTeaKLVDDEDNEVP--HGEPGELCVRGpQVMLGYWQRPDA 424
Cdd:cd05924 157 LVPNiTLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPpgSGGVGWIARRG-HIPLGYYGDEAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 425 TDEIIK--DG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVkIF 500
Cdd:cd05924 234 TAETFPevDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV-VA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489956626 501 VVKKDP--SLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:cd05924 313 VVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
47-550 |
3.89e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 139.53 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 47 EVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIV 126
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 127 IVSNFAHTLEKVVEKT-QVKHVILTRMGDQLSTAKgtlvnfvvkyvkrlvpkyHLPDAISFR--RALHAGYRMQYVKPEI 203
Cdd:PRK05620 117 ADPRLAEQLGEILKECpCVRAVVFIGPSDADSAAA------------------HMPEGIKVYsyEALLDGRSTVYDWPEL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 VSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkELVITALPLYHIFALTMNCLLFieLGGQNVLIT 283
Cdd:PRK05620 179 DETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHG-ESFLCCVPIYHVLSWGVPLAAF--MSGTPLVFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 284 NPRDIPglvKELAKYPFTAMT----GVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGL 359
Cdd:PRK05620 256 GPDLSA---PTLAKIIATAMPrvahGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 360 TECAPL--VSVNPHDID------YHSGSIGLPVpSTEAKLVDD-------EDNEvphgepGELCVRGPQVMLGYWQRP-- 422
Cdd:PRK05620 333 TETSPVgtVARPPSGVSgearwaYRVSQGRFPA-SLEYRIVNDgqvmestDRNE------GEIQVRGNWVTASYYHSPte 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 423 ---------------DATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:PRK05620 406 egggaastfrgedveDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 488 VPSGSSGE---AVKIFVVKKDPSL-TEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK05620 486 YPDDKWGErplAVTVLAPGIEPTReTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
50-556 |
4.10e-35 |
|
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: 139.76 E-value: 4.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd05967 84 TYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTAS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 ---------NFAHTLEKVVEKTQVK--HVILTRMGDqlstakgtlvnfvvkyvKRLVPKYHLPDaISFRRALHAGYRMQY 198
Cdd:cd05967 163 cgiepgkvvPYKPLLDKALELSGHKphHVLVLNRPQ-----------------VPADLTKPGRD-LDWSELLAKAEPVDC 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 199 VKpeIVSEDLAFLQYTGGTTGVAKG--------AMLTHRNMlANLEQVNA-------------------TYGPLLHPGKE 251
Cdd:cd05967 225 VP--VAATDPLYILYTSGTTGKPKGvvrdngghAVALNWSM-RNIYGIKPgdvwwaasdvgwvvghsyiVYGPLLHGATT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 252 LVITALPLYhifalTMNCLLF---IELGGQNVLITNPRDIPGLVKE------LAKYPFTAMTgvnTLFNAllnnkeFQQL 322
Cdd:cd05967 302 VLYEGKPVG-----TPDPGAFwrvIEKYQVNALFTAPTAIRAIRKEdpdgkyIKKYDLSSLR---TLFLA------GERL 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 323 DFSTLHlsagggmpvqqavaerWV-KLTGQYLLEGYGLTE-----CAPLVSVNPHDIdyHSGSIGLPVPSTEAKLVDDED 396
Cdd:cd05967 368 DPPTLE----------------WAeNTLGVPVIDHWWQTEtgwpiTANPVGLEPLPI--KAGSPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 397 NEVPHGEPGELCVRGP---QVMLGYWQRPDATDEII---KDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEI 470
Cdd:cd05967 430 EPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYlskFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEM 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 471 EDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTED----ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:cd05967 510 EESVLSHPAVAECAVVGVRDELKGQVPLGLVVlKEGVKITAEelekELVALVREQIGPVAAFRLVIFVKRLPKTRSGKIL 589
|
570
....*....|.
gi 489956626 546 RRELRDEARAK 556
Cdd:cd05967 590 RRTLRKIADGE 600
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-549 |
4.22e-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: 137.99 E-value: 4.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvvekTQVKHViltrmgDQLSTAKGTlvnfvvkyvkrlvpkyHLPDAISFRRALHagyrmQ 197
Cdd:cd17656 82 LDSGVRVVL---------------TQRHLK------SKLSFNKST----------------ILLEDPSISQEDT-----S 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 YVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMlANLEQVNATYGPLLHPGKELVITALPL---YH-IFAltmnCLLFi 273
Cdd:cd17656 120 NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM-VNLLHFEREKTNINFSDKVLQFATCSFdvcYQeIFS----TLLS- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 274 elGGQNVLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTL-HLSAGGGMPVQQAVAERWVKLTG 350
Cdd:cd17656 194 --GGTLYIIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVkHIITAGEQLVITNEFKEMLHEHN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 351 QYLLEGYGLTEcAPLVS---VNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDAT-D 426
Cdd:cd17656 272 VHLHNHYGPSE-THVVTtytINPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTaE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 427 EIIKDGW------LHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEvAAVGVPSGSSGEAVKIF 500
Cdd:cd17656 351 KFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEKYLCA 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489956626 501 VVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17656 430 YFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
5.05e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.63 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 7 NRYPADVPAEinpdryQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQ 86
Cdd:PRK12316 4541 NRTDAGYPAT------RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIA-RGVGPEVLVGIAMERSAE 4613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 87 YPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGAAAIVivsnfahtlekvvekTQvkhvilTRMGDQLSTAKGTlvn 165
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEY-PRErLAYMMEDSGAALLL---------------TQ------SHLLQRLPIPDGL--- 4668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 166 fvvkyvkrlvpkyhlpDAISFRRALH-AGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGp 244
Cdd:PRK12316 4669 ----------------ASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE- 4731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 245 LLHPGKELVITALPlyhiFALTMNCLLFIELGGQNVLITNPR--DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEfQQL 322
Cdd:PRK12316 4732 LTPDDRVLQFMSFS----FDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDG 4806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 323 DFSTLHLSAGGGMPVQQAVAER-WVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDEDN 397
Cdd:PRK12316 4807 EPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQLN 4886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 398 EVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK12316 4887 PLPVGVAGELYLGGEGVARGYLERPALTAErFVPDpfgapgGRLYrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGE 4966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 470 IEDVVMQHSGVLEVAAVGVPsGSSGEAVKIFVVKKDPSLTE---------DALITFCRRQLTGYKVPKLVEFRDELPKSN 540
Cdd:PRK12316 4967 IEARLREHPAVREAVVIAQE-GAVGKQLVGYVVPQDPALADadeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTP 5045
|
....*....
gi 489956626 541 VGKILRREL 549
Cdd:PRK12316 5046 NGKLDRKAL 5054
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-552 |
1.63e-34 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 136.46 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQV-NATYGPLlhpgKELVITALPLYHIFALtMNCLLFIELGGQNVLITN 284
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAIlNSTEWKT----KDRILSWMPLTHDMGL-IAFHLAPLIAGMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 285 PRDI---PGL-VKELAKYPFTAMTGVN---TLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQY----- 352
Cdd:cd05908 181 TRLFirrPILwLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYglkrn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 -LLEGYGLTECAPLVSVNPHDIDY------HSG---------------------SIGLPVPSTEAKLVDDEDNEVPHGEP 404
Cdd:cd05908 261 aILPVYGLAEASVGASLPKAQSPFktitlgRRHvthgepepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDGYI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 405 GELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVL-- 481
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFtDDGWLKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElg 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 482 EVAAVGV-PSGSSGEAVKIFVVKKDpslTEDALITFCRR------QLTGYKVPKLVEFRdELPKSNVGKILRRELRDE 552
Cdd:cd05908 420 RVVACGVnNSNTRNEEIFCFIEHRK---SEDDFYPLGKKikkhlnKRGGWQINEVLPIR-RIPKTTSGKVKRYELAQR 493
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-553 |
2.48e-34 |
|
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: 137.31 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 33 VRRYADQPAF------VNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd05966 63 LKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKS-LGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYTPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVEK-----TQVKHVIltrmgdqlstakgtlvnfVVKYVKRLVP 176
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGGyrggkVIPLKEIVDEalekcPSVEKVL------------------VVKRTGGEVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 177 K-------YHlpDAIsfrralhAGYRMqYVKPEIV-SEDLAFLQYTGGTTGVAKG-----------AMLTHRNML----- 232
Cdd:cd05966 204 MtegrdlwWH--DLM-------AKQSP-ECEPEWMdSEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKYVFdyhpd 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 233 ------ANLEQVNA----TYGPLLHPGKELVITALPLYHIFALTMNcllFIELGGQNVLITNPRDIPGLVKELAKYPfta 302
Cdd:cd05966 274 diywctADIGWITGhsyiVYGPLANGATTVMFEGTPTYPDPGRYWD---IVEKHKVTIFYTAPTAIRALMKFGDEWV--- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 303 mtgvntlfnallnnkefQQLDFSTLHLSAGGGMPVQqavAERWvkltgQYLLEGYGLTEC----------------APLv 366
Cdd:cd05966 348 -----------------KKHDLSSLRVLGSVGEPIN---PEAW-----MWYYEVIGKERCpivdtwwqtetggimiTPL- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 367 svnPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGP-QVML------------GYWQR-PdatdeiikdG 432
Cdd:cd05966 402 ---PGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwPGMArtiygdheryedTYFSKfP---------G 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKD-----PS 507
Cdd:cd05966 470 YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepsDE 549
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 489956626 508 LTEDaLITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05966 550 LRKE-LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKIA 594
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
24-548 |
3.12e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 136.61 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAFVNM---------GEVMTFRKLEERSRAFAAYLQEgLGlQKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIdyeqdpagvAETLTWSQLYRRTLNVAEELRR-HG-STGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLYTPRELEHQ------LNDSGAAAIvivsnfahtlekvvektqvkhviltrmgdqLSTAKgtLVNFVV 168
Cdd:PRK05850 80 LQAGLIAV---PLSVPQGGAHDervsavLRDTSPSVV------------------------------LTTSA--VVDDVT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 169 KYVKRL----VPKYHLPDAISFRRALhagyrmqyvKPEIVSEDL---AFLQYTGGTTGVAKGAMLTHRNMLANLEQVNAT 241
Cdd:PRK05850 125 EYVAPQpgqsAPPVIEVDLLDLDSPR---------GSDARPRDLpstAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 242 YgpLLHPGKEL-----VITALPLYHIFALTMNCLLFIeLGGQNVLITNP--------RdipgLVKELAKYP--FTA---- 302
Cdd:PRK05850 196 Y--FGDTGGVPppdttVVSWLPFYHDMGLVLGVCAPI-LGGCPAVLTSPvaflqrpaR----WMQLLASNPhaFSAapnf 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 303 -------------MTGvntlfnallnnkefqqLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLE------GYGLTECA 363
Cdd:PRK05850 269 afelavrktsdddMAG----------------LDLGGVLGIISGSERVHPATLKRFADRFAPFNLRetairpSYGLAEAT 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 364 PLVSVNPH-------DIDYHSGSIGLPVP----------------STEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYW 419
Cdd:PRK05850 333 VYVATREPgqppesvRFDYEKLSAGHAKRcetgggtplvsygsprSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYW 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDEI-----------IKDG-WLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVlEVAAVG 487
Cdd:PRK05850 413 QKPEETERTfgatlvdpspgTPEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGG-RVAAIS 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 488 VPSGSSGEAVKIFVVKKDPSLTEDALITFC--RRQLT-------GYKVPKLVEF-RDELPKSNVGKILRRE 548
Cdd:PRK05850 491 VPDDGTEKLVAIIELKKRGDSDEEAMDRLRtvKREVTsaiskshGLSVADLVLVaPGSIPITTSGKIRRAA 561
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-549 |
3.83e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 138.76 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK12467 512 DCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYV 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYtPRE-LEHQLNDSGAAAIVIVSnfaHTLEKVVEKTQVKHVILTRMGDQLSTAKGtlvnfvvkyvkrlvpkyHLP 181
Cdd:PRK12467 591 PLDPEY-PQDrLAYMLDDSGVRLLLTQS---HLLAQLPVPAGLRSLCLDEPADLLCGYSG-----------------HNP 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 182 DaisfrralhagyrmqyvkPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQVNATYGPLLhpgkelVITALPLYH 261
Cdd:PRK12467 650 E------------------VALDPDNLAYVIYTSGSTGQPKGVAISHGA-LANYVCVIAERLQLA------ADDSMLMVS 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 262 IFALTMNCL-LFIELG-GQNVLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ-LDFSTLHLsagGGM 335
Cdd:PRK12467 705 TFAFDLGVTeLFGALAsGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALpRPQRALVC---GGE 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 336 PVQQAVAERWVKLT-GQYLLEGYGLTECAPLVSVNP---HDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRG 411
Cdd:PRK12467 782 ALQVDLLARVRALGpGARLINHYGPTETTVGVSTYElsdEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGG 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 412 PQVMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEv 483
Cdd:PRK12467 862 AGLARGYHRRPALTAErFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE- 940
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956626 484 AAVGVPSGSSGEAVKIFVVKK------DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12467 941 AVVLAQPGDAGLQLVAYLVPAavadgaEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
49-509 |
1.20e-33 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 134.64 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAA-IVI 127
Cdd:PRK09274 42 LSFAELDARSDAIAHGLNA-AGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAfIGI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 128 vsnfahtlekvvEKTQVKHVILTRmgdqlstAKGTlvnfvvkyVKRLVP--KYHLPDAISFRRALH----AGYRMQYVKP 201
Cdd:PRK09274 121 ------------PKAHLARRLFGW-------GKPS--------VRRLVTvgGRLLWGGTTLATLLRdgaaAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 202 EivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVitALPLYHIFALTmncllfieLGGQNVL 281
Cdd:PRK09274 174 D----DMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYG-IEPGEIDLP--TFPLFALFGPA--------LGMTSVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 282 --------IT-NPRDIpglVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKL--TG 350
Cdd:PRK09274 239 pdmdptrpATvDPAKL---FAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlpPD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 351 QYLLEGYGLTECAPLVSVNPHDI--------DYHSGS-IGLPVPSTEAKLVD---------DEDNEVPHGEPGELCVRGP 412
Cdd:PRK09274 316 AEILTPYGATEALPISSIESREIlfatraatDNGAGIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 413 QVMLGYWQRPDATDEI-IKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:PRK09274 396 MVTRSYYNRPEATRLAkIPDGqgdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG 475
|
490 500
....*....|....*....|..
gi 489956626 488 VPSGssGEAVKIFVVKKDPSLT 509
Cdd:PRK09274 476 VGVP--GAQRPVLCVELEPGVA 495
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
38-557 |
2.99e-33 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 133.19 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGmiVVNVNPLYTPRELEhqL 117
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRSE--L 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 N---DSGAAAIVIVSNfahtlekvvektqvKHVILT--RMGDQLSTAKGTLvnfvvkyvkRLVPKYHLPDAISFRRALHA 192
Cdd:PRK10946 113 NayaSQIEPALLIADR--------------QHALFSddDFLNTLVAEHSSL---------RVVLLLNDDGEHSLDDAINH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 193 GYRMQYVKPEIVSEdLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELvITALPLYHIFALTM-NCLL 271
Cdd:PRK10946 170 PAEDFTATPSPADE-VAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICG--FTPQTRY-LCALPAAHNYPMSSpGALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 272 FIELGGQNVLITNPRdiPGLVKEL-AKYPFTaMT-----GVNTLFNALLNNKEFQQLdfSTLHLSAGGGMPVQQAVAERW 345
Cdd:PRK10946 246 VFLAGGTVVLAPDPS--ATLCFPLiEKHQVN-VTalvppAVSLWLQAIAEGGSRAQL--ASLKLLQVGGARLSETLARRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKLTGQYLLEGYGLTEcaPLVSV----NPHDIDYHSGsiGLPV-PSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQ 420
Cdd:PRK10946 321 PAELGCQLQQVFGMAE--GLVNYtrldDSDERIFTTQ--GRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 421 RPD----ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEA 496
Cdd:PRK10946 397 SPQhnasAFDA---NGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEK 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956626 497 VKIFVVKKDPsLTEDALITFCRRQ-LTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKV 557
Cdd:PRK10946 474 SCAFLVVKEP-LKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRA 534
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
47-457 |
3.38e-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: 133.70 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 47 EVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLlqyPVALFGILRAGMIVVNVNPLYT---PRELEHQLNDSGAA 123
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 124 AIVivsnfahtlekVVEKTQVKHVIltRMGDQLStakgtLVNFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEI 203
Cdd:cd17641 86 VVI-----------AEDEEQVDKLL--EIADRIP-----SVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 VS--------EDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYGPLlHPGKElVITALPL----YHIFALTM---- 267
Cdd:cd17641 148 YErevaagkgEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-CAAYLAADPL-GPGDE-YVSVLPLpwigEQMYSVGQalvc 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 268 -NCLLFIELG----------GQNVLITNPRDIPGLVKEL-------------------------------AKYPFTAMTG 305
Cdd:cd17641 225 gFIVNFPEEPetmmedlreiGPTFVLLPPRVWEGIAADVrarmmdatpfkrfmfelgmklglraldrgkrGRPVSLWLRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 306 VNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAeRWVKLTGQYLLEGYGLTECAPLVSVNP-HDIDYHSgsIGLPV 384
Cdd:cd17641 305 ASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRdGDVDPDT--VGVPF 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 385 PSTEAKLVddednevphgEPGELCVRGPQVMLGYWQRPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDM 457
Cdd:cd17641 382 PGTEVRID----------EVGEILVRSPGVFVGYYKNPEATAEdFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-550 |
9.45e-33 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 134.53 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 15 AEINPDRYqslielfehSVRRYADQPafvNMGEVMTFRKLEERSRAFAAYLQEGLGLqkGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK05691 19 AAQTPDRL---------ALRFLADDP---GEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLYTPREL--EHQLNdsgaaaivIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLVNfvvkyVK 172
Cdd:PRK05691 85 LYAGVIAV---PAYPPESArrHHQER--------LLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLC-----VD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 173 RLVPkyhlpdaisfrrALHAGYRmqyvKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKEL 252
Cdd:PRK05691 149 TLDP------------ALAEAWQ----EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP-DDV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 253 VITALPLYHIFALTMNCLLFIELGGQNVLITnprdiPGL--------VKELAKYPFTAMTGVN---TLFNALLNNKEFQQ 321
Cdd:PRK05691 212 IVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS-----PAYflerplrwLEAISEYGGTISGGPDfayRLCSERVSESALER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 322 LDFSTLHLSAGGGMPVQQ----AVAERWVK--LTGQYLLEGYGLTECAPLVSVNPH-------DIDYHS----------G 378
Cdd:PRK05691 287 LDLSRWRVAYSGSEPIRQdsleRFAEKFAAcgFDPDSFFASYGLAEATLFVSGGRRgqgipalELDAEAlarnraepgtG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 379 SI----GLPVPSTEAKLVDDEDNEV-PHGEPGELCVRGPQVMLGYWQRPDATDEII--KDG--WLHTGDIAVMDDeGFLR 449
Cdd:PRK05691 367 SVlmscGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFveHDGrtWLRTGDLGFLRD-GELF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 450 IVDRKKDMILVSGFNVYPNEIEDVVMQHSGVL---EVAAVGVP-SGSSGEAVKIFVVKK-DPSLTEDALITFCRRQLTG- 523
Cdd:PRK05691 446 VTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkgRVAAFAVNhQGEEGIGIAAEISRSvQKILPPQALIKSIRQAVAEa 525
|
570 580 590
....*....|....*....|....*....|
gi 489956626 524 -YKVPKLVEFRD--ELPKSNVGKILRRELR 550
Cdd:PRK05691 526 cQEAPSVVLLLNpgALPKTSSGKLQRSACR 555
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
24-552 |
1.54e-32 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 132.17 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAF-------VNMGEV--MTFRKLEERSRAFAAYLQEGLglQKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYryldhshSAAGCAveLTWTQLGVRLRAVGARLQQVA--GPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLYTPRELEHqlndsgaaaivivsnfAHTLEKVVEKTQvKHVILTRmgdqlSTAKGTLVNFVVKYVKRL 174
Cdd:PRK12476 113 IKAGTIAV---PLFAPELPGH----------------AERLDTALRDAE-PTVVLTT-----TAAAEAVEGFLRNLPRLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 VPKYHLPDAISFRRAlhagyrMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKELVi 254
Cdd:PRK12476 168 RPRVIAIDAIPDSAG------ESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSID-LLDRNTHGV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 255 TALPLYHIFALTMncLLFIELGGQNVLITNP----RDIPGLVKELAK---------------YPFTAMTGVntlfnalln 315
Cdd:PRK12476 240 SWLPLYHDMGLSM--IGFPAVYGGHSTLMSPtafvRRPQRWIKALSEgsrtgrvvtaapnfaYEWAAQRGL--------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 316 NKEFQQLDFSTLHLsAGGGMPVQQAVAERWVKLTGQYLLE------GYGLTECAPLVSVNPHD-------IDYH---SG- 378
Cdd:PRK12476 309 PAEGDDIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPrtafkpSYGIAEATLFVATIAPDaepsvvyLDREqlgAGr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 379 ---------------SIGLPVPSTEAKLVD-DEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEI-------------- 428
Cdd:PRK12476 388 avrvaadapnavahvSCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTfgaklqsrlaegsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 -----IKDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE---VAAVGVPSGSSGEAVKIF 500
Cdd:PRK12476 468 adgaaDDGTWLRTGDLGVYLD-GELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAEDNERLVIVA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 501 -----VVKKDPSLTEDAL-ITFCRRQLTGYKVPKLVEfRDELPKSNVGKILRRELRDE 552
Cdd:PRK12476 547 eraagTSRADPAPAIDAIrAAVSRRHGLAVADVRLVP-AGAIPRTTSGKLARRACRAQ 603
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-550 |
1.64e-32 |
|
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: 129.80 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAaaivivsnfahtlekvvektqvkHVILTRMGDQLstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmq 197
Cdd:cd17649 81 EDSGA-----------------------GLLLTHHPRQL----------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivsedlAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELvitaLPLYHI-FALTMNCLLFIELG 276
Cdd:cd17649 97 -----------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG--LTPGDRE----LQFASFnFDGAHEQLLPPLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 277 GQNVLI------TNPRDIPGLVKELakypftamtGVNT-------LFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAE 343
Cdd:cd17649 160 GACVVLrpdelwASADELAEMVREL---------GVTVldlppayLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLR 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 344 RWVKlTGQYLLEGYGLTEC--APLVSVNPHDIDYHSGS--IGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYW 419
Cdd:cd17649 231 RWLK-APVRLFNAYGPTEAtvTPLVWKCEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDE-IIKDG-------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSG 491
Cdd:cd17649 310 GRPELTAErFVPDPfgapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 492 SSGEAVKIFVVKKDPSLTED--ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd17649 390 GGKQLVAYVVLRAAAAQPELraQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
17-553 |
5.66e-32 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 130.38 E-value: 5.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 17 INPDRYQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAA-RGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 97 AGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLsTAKGTLVNFvvkyvkrlvp 176
Cdd:PRK08279 110 LGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTL-DDPEGYEDL---------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 177 KYHLPDAISFRRALHAGyrmqyvkpeIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqvnATYGPLLHPGKELVI-T 255
Cdd:PRK08279 179 AAAAAGAPTTNPASRSG---------VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAM----GGFGGLLRLTPDDVLyC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 256 ALPLYHIFALT--MNCLLfieLGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGG 333
Cdd:PRK08279 246 CLPLYHNTGGTvaWSSVL---AAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPPKPTDRDHRLRLMIGN 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 334 GM-PvqqAVAERWVKLTG-QYLLEGYGLTECaplvSVNPHDIDYHSGSIGLpVPSTEAK---LVD-DEDNE--------- 398
Cdd:PRK08279 323 GLrP---DIWDEFQQRFGiPRILEFYAASEG----NVGFINVFNFDGTVGR-VPLWLAHpyaIVKyDVDTGepvrdadgr 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 399 ---VPHGEPGELC--VRGPQVMLGYWQrPDATDE-IIKDG------WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVY 466
Cdd:PRK08279 395 cikVKPGEVGLLIgrITDRGPFDGYTD-PEASEKkILRDVfkkgdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 467 PNEIEDVVMQHSGVLEVAAVGVP-SGSSGEA--VKIfVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:PRK08279 474 TTEVENALSGFPGVEEAVVYGVEvPGTDGRAgmAAI-VLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFK 552
|
570
....*....|
gi 489956626 544 ILRRELRDEA 553
Cdd:PRK08279 553 YRKVDLRKEG 562
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
181-549 |
7.71e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 127.46 E-value: 7.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 181 PDAISFRRALHAG-YRMQYVKPEIVSEDL--------AFLQYTGGTTGVAKgamlTHRNMLANLEQVNATYGPLLH-PGK 250
Cdd:PRK08308 67 PKEAAIRMAKRAGcHGLLYGESDFTKLEAvnylaeepSLLQYSSGTTGEPK----LIRRSWTEIDREIEAYNEALNcEQD 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 251 ELVITALPLYHIFALTMNCLLFIELGGQNVLIT--NPRDIpglVKELAKYPFTAMTGVNTLFNALlnnKEFQQLDFsTLH 328
Cdd:PRK08308 143 ETPIVACPVTHSYGLICGVLAALTRGSKPVIITnkNPKFA---LNILRNTPQHILYAVPLMLHIL---GRLLPGTF-QFH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 --LSAGGGMPvqqavaERW---VKLTGQYLLEGYGLTEcAPLVSVNPHDIDyhSGSIGLPVPSTEAKLVDDEDNevphge 403
Cdd:PRK08308 216 avMTSGTPLP------EAWfykLRERTTYMMQQYGCSE-AGCVSICPDMKS--HLDLGNPLPHVSVSAGSDENA------ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 404 PGELCVRgpqvmlgywqrpdatdeiIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEV 483
Cdd:PRK08308 281 PEEIVVK------------------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEA 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 484 AAVGVPSGSSGEAVKIFVVkKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK08308 343 VVYRGKDPVAGERVKAKVI-SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-549 |
2.00e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.46 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 24 SLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVN 103
Cdd:PRK12316 512 GVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE-RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 104 VNPLYTPRELEHQLNDSGAAAIVivsnfahtlekvvekTQvkhvilTRMGDQLSTAKGtlvnfvvkyVKRLVpkyhLPDA 183
Cdd:PRK12316 591 LDPEYPAERLAYMLEDSGVQLLL---------------SQ------SHLGRKLPLAAG---------VQVLD----LDRP 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 184 ISFRralhAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGkelVITALPLYHIF 263
Cdd:PRK12316 637 AAWL----EGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT---VLQKTPFSFDV 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 264 ALTMnclLFIELGGQNVLITNPrdiPGLVKELAKYP-FTAMTGVNTL------FNALLNNKEFQQLDFSTLHLSAGGGMP 336
Cdd:PRK12316 710 SVWE---FFWPLMSGARLVVAA---PGDHRDPAKLVeLINREGVDTLhfvpsmLQAFLQDEDVASCTSLRRIVCSGEALP 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 337 ---VQQAVAERWVklTGQYLLegYGLTECAPLVSvnpHDIDYHSG----SIGLPVPSTEAKLVDDEDNEVPHGEPGELCV 409
Cdd:PRK12316 784 adaQEQVFAKLPQ--AGLYNL--YGPTEAAIDVT---HWTCVEEGgdsvPIGRPIANLACYILDANLEPVPVGVLGELYL 856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 410 RGPQVMLGYWQRPDATDE-----IIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE 482
Cdd:PRK12316 857 AGRGLARGYHGRPGLTAErfvpsPFVAGerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE 936
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 483 VAAVGVpsgsSGEAVKIFVVKKDPS-LTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 937 AAVLAV----DGKQLVGYVVLESEGgDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
49-455 |
3.51e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 128.56 E-value: 3.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIV 128
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAE-LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 129 SNFAHTLEKVVEKTQVKHVILTRMGD---QLSTAKGTLVNF--VVkyvkrlvpkyhlpdAISFRRALHAGYRMQYVKpei 203
Cdd:PTZ00216 201 GKNVPNLLRLMKSGGMPNTTIIYLDSlpaSVDTEGCRLVAWtdVV--------------AKGHSAGSHHPLNIPENN--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 vsEDLAFLQYTGGTTGVAKGAMLTHRNMLANL----EQVNATYGPLlHPGkELVITALPLYHIFALT-MNCLLFielggQ 278
Cdd:PTZ00216 264 --DDLALIMYTSGTTGDPKGVMHTHGSLTAGIlaleDRLNDLIGPP-EED-ETYCSYLPLAHIMEFGvTNIFLA-----R 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 279 NVLIT--NPRDIPGLVK----ELAKYPFTAMTGVNTLFN------------------------------ALLNNKE---F 319
Cdd:PTZ00216 335 GALIGfgSPRTLTDTFArphgDLTEFRPVFLIGVPRIFDtikkaveaklppvgslkrrvfdhayqsrlrALKEGKDtpyW 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 320 QQLDFST--------LHLSAGGGMPVQQAVAErWVKLTGQYLLEGYGLTECaplVSVNPHDI--DYHSGSIGLPVPSTEA 389
Cdd:PTZ00216 415 NEKVFSApravlggrVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTET---VCCGGIQRtgDLEPNAVGQLLKGVEM 490
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 390 KLVDDEdnEVPHG---EP-GELCVRGPQVMLGYWQRPDATDEII-KDGWLHTGDIAVMDDEGFLRIVDRKK 455
Cdd:PTZ00216 491 KLLDTE--EYKHTdtpEPrGEILLRGPFLFKGYYKQEELTREVLdEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-553 |
1.04e-30 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 124.88 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIViv 128
Cdd:cd05910 3 LSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 129 snfahtlekvvektqvkhviltrmgdqlstakGtlvnfvvkyvkrlVPKYHLPDAISFrralhagyrmqyvkpeivsedl 208
Cdd:cd05910 80 --------------------------------G-------------IPKADEPAAILF---------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 209 aflqyTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllHPGkELVITALPLYHIFALTMNCLLFI-ELGGQNVLITNPRD 287
Cdd:cd05910 93 -----TSGSTGTPKGVVYRHGTFAAQIDALRQLYGI--RPG-EVDLATFPLFALFGPALGLTSVIpDMDPTRPARADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 288 ipgLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLH--LSAGGgmPVQQAVAERWVKLT--GQYLLEGYGLTECA 363
Cdd:cd05910 165 ---LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGA--PVPIALAARLRKMLsdEAEILTPYGATEAL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 364 PLVSVNPHDI--------DYHSGS-IGLPVPSTEAKLV--DDED-------NEVPHGEPGELCVRGPQVMLGYWQRPDAT 425
Cdd:cd05910 240 PVSSIGSRELlatttaatSGGAGTcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVAT 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 426 D-EIIKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVpsGSSGEAVKIF 500
Cdd:cd05910 320 AlAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQLPVL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489956626 501 VVKKDPSLTED------ALITFCRRQLTGYKVPKLVeFRDELP---KSNvGKILRRELRDEA 553
Cdd:cd05910 398 CVEPLPGTITPrarleqELRALAKDYPHTQRIGRFL-IHPSFPvdiRHN-AKIFREKLAVWA 457
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
2.23e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.38 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 7 NRYPADVPAEInpdryqSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQ 86
Cdd:PRK12316 1993 DRTPEAYPRGP------GVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFE 2065
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 87 YPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGAAAIVIVSnfaHTLEKVVEKTQVKHVILTRMGDQlstakgtlvn 165
Cdd:PRK12316 2066 LVVALLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLLTQR---HLLERLPLPAGVARLPLDRDAEW---------- 2131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 166 fvvkyvkrlvpkyhlpdaisfrralhAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpl 245
Cdd:PRK12316 2132 --------------------------ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE-- 2183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 246 LHPGK-ELVITALPlyhiFALTMNCLLFIELGGQNVLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQ-- 320
Cdd:PRK12316 2184 LSPADcELQFMSFS----FDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDgr 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 321 QLDFSTLHLsagGGMPVQQAVAER-WVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDE 395
Cdd:PRK12316 2260 PPAVRVYCF---GGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayvpIGRALGNRRAYILDAD 2336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 396 DNEVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKDGWLH-------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYP 467
Cdd:PRK12316 2337 LNLLAPGMAGELYLGGEGLARGYLNRPGLTAErFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIEL 2416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 468 NEIEDVVMQHSGVLEvAAVGVPSGSSGEAVKIFVVKKDP-SLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:PRK12316 2417 GEIEARLQAHPAVRE-AVVVAQDGASGKQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDR 2495
|
...
gi 489956626 547 REL 549
Cdd:PRK12316 2496 KAL 2498
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
201-548 |
2.90e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 124.72 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 201 PEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITALPLYH------IFALTMNCllfie 274
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVETDVMVSWLPLFHdmgmvgFLTVPMYF----- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 275 lGGQNVLITnPRDI---PGLVKEL-AKYPFTAMTGVN---TLFNALLNNK-EFQQLDFSTLHLSAGGGMPVQQAVAERWV 346
Cdd:PRK07768 220 -GAELVKVT-PMDFlrdPLLWAELiSKYRGTMTAAPNfayALLARRLRRQaKPGAFDLSSLRFALNGAEPIDPADVEDLL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 347 ------KLTGQYLLEGYGLTECAPLVSVNPHD----IDY---------------HSG------SIGLPVPSTEAKLVDDE 395
Cdd:PRK07768 298 dagarfGLRPEAILPAYGMAEATLAVSFSPCGaglvVDEvdadllaalrravpaTKGntrrlaTLGPPLPGLEVRVVDED 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 396 DNEVPHGEPGELCVRGPQVMLGYwQRPD----ATDEiikDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIE 471
Cdd:PRK07768 378 GQVLPPRGVGVIELRGESVTPGY-LTMDgfipAQDA---DGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 472 DVVMQHSGVLE--VAAVGVPSGSSGEAVKIFVVKKDPSltEDALITFCRRQLTgYKVPKLVEFRDE---------LPKSN 540
Cdd:PRK07768 454 RAAARVEGVRPgnAVAVRLDAGHSREGFAVAVESNAFE--DPAEVRRIRHQVA-HEVVAEVGVRPRnvvvlgpgsIPKTP 530
|
....*...
gi 489956626 541 VGKiLRRE 548
Cdd:PRK07768 531 SGK-LRRA 537
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
5-549 |
2.97e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 126.81 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 5 WlNRYPADVPAEinpdryQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNL 84
Cdd:PRK12467 1563 W-NATHTGYPLA------RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIA-LGVGPEVLVGIAVERS 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 85 LQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVSnfaHTLEKVVEKTQVKHVILTRMGDQLstakgtlv 164
Cdd:PRK12467 1635 LEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS---HLQARLPLPDGLRSLVLDQEDDWL-------- 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 165 nfvvkyvkrlvpkyhlpdaisfrralhAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGp 244
Cdd:PRK12467 1704 ---------------------------EGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ- 1755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 245 lLHPGKelvitALPLYHIFALTMNC--LLFIELGGQNVLITNP---RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEF 319
Cdd:PRK12467 1756 -LSAAD-----VVLQFTSFAFDVSVweLFWPLINGARLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQ 1829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 320 QQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDE 395
Cdd:PRK12467 1830 VEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILDAS 1909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 396 DNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII-------KDGWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYP 467
Cdd:PRK12467 1910 LNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgtVGSRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIEL 1989
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 468 NEIEDVVMQHSGVLEvAAVGVPSGSSGEAVKIFVVKKDPSLTEDAL-ITFCRRQLTG--------YKVPKLVEFRDELPK 538
Cdd:PRK12467 1990 GEIEARLREQGGVRE-AVVIAQDGANGKQLVAYVVPTDPGLVDDDEaQVALRAILKNhlkaslpeYMVPAHLVFLARMPL 2068
|
570
....*....|.
gi 489956626 539 SNVGKILRREL 549
Cdd:PRK12467 2069 TPNGKLDRKAL 2079
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
200-549 |
4.59e-30 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 123.97 E-value: 4.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 200 KPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLA--------NLEQVNATYGpllhpgkELVITALPLYHIFAL--TMNC 269
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpdilqkeGLNWVTWVVG-------ETTYSPLPATHIGGLwwILTC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 270 LLFielGGqnVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGmpvQQAVAE--RWVK 347
Cdd:PRK05857 236 LMH---GG--LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAAdvRFIE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 348 LTGQYLLEGYGLTE------CAPLVSVNPHDIDyhSGSIGLPVPSTEAKLVDDE--DNEVPHGEP----GELCVRGPQVM 415
Cdd:PRK05857 308 ATGVRTAQVYGLSEtgctalCLPTDDGSIVKIE--AGAVGRPYPGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANM 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 416 LGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGE 495
Cdd:PRK05857 386 LGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGA 465
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 496 AVKIFVVKKdPSLTEDALITFCRRQLTGYK-------VPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05857 466 LVGLAVVAS-AELDESAARALKHTIAARFRresepmaRPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
23-549 |
4.77e-30 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 125.93 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK10252 458 TTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRE-RGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVSNFAHTLekvvektqvkhviltrMGDQLSTakgtlvnfvvkyvkrlVPKYHLPD 182
Cdd:PRK10252 537 PLDTGYPDDRLKMMLEDARPSLLITTADQLPRF----------------ADVPDLT----------------SLCYNAPL 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 183 AISFRRALHAGyrmqyvKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYG------------------- 243
Cdd:PRK10252 585 APQGAAPLQLS------QPH----HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPltaddvvlqktpcsfdvsv 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 244 -----PLLhPGKELVItALPLYHifaltmncllfielggqnvlitnpRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKE 318
Cdd:PRK10252 655 weffwPFI-AGAKLVM-AEPEAH------------------------RDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLT 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 319 FQQLDFSTLHLS----AGGGMPVQQAvaERWVKLTGQYLLEGYGLTECAPLVSVNP---HDIDYHSGS---IGLPVPSTE 388
Cdd:PRK10252 709 PEGARQSCASLRqvfcSGEALPADLC--REWQQLTGAPLHNLYGPTEAAVDVSWYPafgEELAAVRGSsvpIGYPVWNTG 786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 389 AKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKDGWL------HTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PRK10252 787 LRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASrFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIR 866
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 462 GFNVYPNEIEDVVMQHSGVLEVAAVGV-------PSGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRD 534
Cdd:PRK10252 867 GQRIELGEIDRAMQALPDVEQAVTHACvinqaaaTGGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLD 946
|
570
....*....|....*
gi 489956626 535 ELPKSNVGKILRREL 549
Cdd:PRK10252 947 QLPLSANGKLDRKAL 961
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-553 |
1.61e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 122.48 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAKGTLVNFVVkyvkrlvpkyhlPDAisfrralhagyrmq 197
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRV------------ADP-------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivsEDLAFLQYTGGTTGVAKGAMLTHR------NMLAnleqvnATYGplLHPGkELVITALPLYHIFALtMNCLL 271
Cdd:PRK07867 152 --------DDLFMLIFTSGTSGDPKAVRCTHRkvasagVMLA------QRFG--LGPD-DVCYVSMPLFHSNAV-MAGWA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 272 FIELGGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAG--GGMPVQQAVAERWvklt 349
Cdd:PRK07867 214 VALAAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGneGAPGDIARFARRF---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 350 GQYLLEGYGLTECAPLVSVNPhdiDYHSGSIGLPVPSTeaKLVD-DEDNEVPHGEP------------GELC-VRGPQVM 415
Cdd:PRK07867 290 GCVVVDGFGSTEGGVAITRTP---DTPPGALGPLPPGV--AIVDpDTGTECPPAEDadgrllnadeaiGELVnTAGPGGF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 416 LGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGE 495
Cdd:PRK07867 365 EGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGD 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 496 AVKIFVV-KKDPSLTEDALITFCRRQ--LTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK07867 445 QVMAALVlAPGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEG 505
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-550 |
4.87e-29 |
|
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: 119.59 E-value: 4.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLnDSGAAAIVIV 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRV-DRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 129 SNFAHtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivSEDL 208
Cdd:cd05974 79 DENTH-----------------------------------------------------------------------ADDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 209 AFLQYTGGTTGVAKGAMLTHRNMLANleQVNATYGPLLHPGKELVITALPLYHIFALTmnCLLFIELGGQNVLITN-PR- 286
Cdd:cd05974 88 MLLYFTSGTTSKPKLVEHTHRSYPVG--HLSTMYWIGLKPGDVHWNISSPGWAKHAWS--CFFAPWNAGATVFLFNyARf 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKELAKYPFTAMTGVNTLFNALLnnkefqQLDFSTLHLS----AGGGMPVQQAVAERWVKLTGQYLLEGYGLTEC 362
Cdd:cd05974 164 DAKRVLAALVRYGVTTLCAPPTVWRMLI------QQDLASFDVKlrevVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTET 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 363 APLVSVNPHDIdYHSGSIGLPVPSTEAKLVDDEDNEVphgEPGELCV-----RGPQVMLGYWQRPDATDEIIKDGWLHTG 437
Cdd:cd05974 238 TALVGNSPGQP-VKAGSMGRPLPGYRVALLDPDGAPA---TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAMRGGYYRTG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 438 DIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-----KKDPSLTEDa 512
Cdd:cd05974 314 DIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragyEPSPETALE- 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 489956626 513 LITFCRRQLTGYKVPKLVEFRdELPKSNVGKILRRELR 550
Cdd:cd05974 393 IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
27-549 |
1.83e-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: 118.31 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 27 ELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNP 106
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 107 LYtPRElehqlndsgaaaivivsnfahTLEKVVEKTQVKhVILTRmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisf 186
Cdd:cd17644 83 NY-PQE---------------------RLTYILEDAQIS-VLLTQ----------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 187 rralhagyrmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMlanleqVNATYGPLlhpgKELVITAlplyhifalT 266
Cdd:cd17644 105 ------------------PENLAYVIYTSGSTGKPKGVMIEHQSL------VNLSHGLI----KEYGITS---------S 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 267 MNCLLFIEL---------------GGQNVLITNP--RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDF-STLH 328
Cdd:cd17644 148 DRVLQFASIafdvaaeeiyvtllsGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLR 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 LSAGGGMPVQQAVAERWVKLTGQY--LLEGYGLTECAPLVSV----NPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHG 402
Cdd:cd17644 228 LVIVGGEAVQPELVRQWQKNVGNFiqLINVYGPTEATIAATVcrltQLTERNITSVPIGRPIANTQVYILDENLQPVPVG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 403 EPGELCVRGPQVMLGYWQRPDATDE-IIKDGWLH--------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
Cdd:cd17644 308 VPGELHIGGVGLARGYLNRPELTAEkFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAV 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 474 VMQHSGVlEVAAVGVPSGSSGEA--VKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17644 388 LSQHNDV-KTAVVIVREDQPGNKrlVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-551 |
2.35e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 121.04 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 7 NRYPADVPAEinpdryQSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFA-AYLQEGLGlqkGDR-VALMMPNL 84
Cdd:PRK12467 3085 NATAAAYPSE------RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAhRLIAIGVG---PDVlVGVAVERS 3155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 85 LQYPVALFGILRAGMIVVNVNPLYtPRE-LEHQLNDSGAAAIVivsnfahTLEKVVEKTQVKHVILTRMGDQLSTAkgtl 163
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEY-PRErLAYMIEDSGVKLLL-------TQAHLLEQLPAPAGDTALTLDRLDLN---- 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 164 vnfvvkyvkrlvpkyhlpdaisfrralhaGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHrNMLANLEQVNATYG 243
Cdd:PRK12467 3224 -----------------------------GYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRH-GALANHLCWIAEAY 3273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 244 PLLHPGKELVITALPlyhiFALTMNCLLFIEL-GGQNVLITNP-RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQ 321
Cdd:PRK12467 3274 ELDANDRVLLFMSFS----FDGAQERFLWTLIcGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGAD 3349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 322 LDFSTLHLSAGGGMPVQqAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDEDN 397
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPA-AFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDGQLN 3428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 398 EVPHGEPGELCVRGPQVMLGYWQRPDATDE-IIKD------GWLH-TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNE 469
Cdd:PRK12467 3429 PVPVGVAGELYIGGVGLARGYHQRPSLTAErFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGE 3508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 470 IEDVVMQHSGVLEVAAVGVPsGSSGEAVKIFVVKKDPSLT-EDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARD-GAGGKQLVAYVVPADPQGDwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKA 3587
|
...
gi 489956626 549 LRD 551
Cdd:PRK12467 3588 LPD 3590
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-550 |
6.58e-28 |
|
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: 117.53 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAIVIVS 129
Cdd:cd05915 26 TYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 NFAHTLEKVVEktqvkhvILTRMGDQLSTAKgtlvnfvvkyvkrlvpKYHlpdaiSFRRALHAGY-RMQYVKPEIVSEDL 208
Cdd:cd05915 105 NLLPLVEAIRG-------ELKTVQHFVVMDE----------------KAP-----EGYLAYEEALgEEADPVRVPERAAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 209 AfLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPgKELVITALPLYHIFALtmnCLLFI--ELGGQNVLITNPR 286
Cdd:cd05915 157 G-MAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSE-KDVVLPVVPMFHVNAW---CLPYAatLVGAKQVLPGPRL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 287 DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFS-TLHLSAGGGMPVQqaVAERWVKLTGQYLLEGYGLTEC--- 362
Cdd:cd05915 232 DPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKtLRRLVVGGSAAPR--SLIARFERMGVEVRQGYGLTETspv 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 363 ------APLVSVNPHDIDYH-SGSIGLPVPSTEAKLVDDEDNEVPHGEPG--ELCVRGPQVMLGYWQRPDATDEI-IKDG 432
Cdd:cd05915 310 vvqnfvKSHLESLSEEEKLTlKAKTGLPIPLVRLRVADEEGRPVPKDGKAlgEVQLKGPWITGGYYGNEEATRSAlTPDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDA 512
Cdd:cd05915 390 FFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEE 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 489956626 513 LITFCRRQLTGYK-VPKLVEFRDELPKSNVGKILRRELR 550
Cdd:cd05915 470 LNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-549 |
1.11e-27 |
|
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: 116.03 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVIvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhLPdaisfrralhagyrmq 197
Cdd:cd17650 81 EDSGAKLLLT----------------------------------------------------QP---------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVITALPLYHIFALTMNCLLFielGG 277
Cdd:cd17650 93 --------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLN---GG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 QNVLITNPR--DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGG--GMPVQQAVAERWVKLTGQYL 353
Cdd:cd17650 162 TLVICPDEVklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGsdGCKAQDFKTLAARFGQGMRI 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 354 LEGYGLTECAPLVSVNPHDIDYHSGS----IGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEII 429
Cdd:cd17650 242 INSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 430 KDGWL-------HTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEvAAVGVPSGSSGEAVKIFVV 502
Cdd:cd17650 322 VENPFapgermyRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEARLCAYV 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489956626 503 KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17650 401 VAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-550 |
1.36e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 113.99 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 175 VPKYHLPDAISFRRALHAGyrmqyvkpEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEqvnATYGPLLHPGKELVi 254
Cdd:PRK07824 12 VPAQDERRAALLRDALRVG--------EPIDDDVALVVATSGTTGTPKGAMLTAAALTASAD---ATHDRLGGPGQWLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 255 tALPLYHIFAltMNCLLFIELGGQNVLIT------NPRDIPGLVKELA---KYpfTAMTGVNtLFNALLNNKEFQQLDFS 325
Cdd:PRK07824 80 -ALPAHHIAG--LQVLVRSVIAGSEPVELdvsagfDPTALPRAVAELGggrRY--TSLVPMQ-LAKALDDPAATAALAEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 326 TLHLSAGGGMPVQqaVAERWVKLtGQYLLEGYGLTECAplvsvnphdidyhSGSI--GLPVPSTEAKLVDdednevphge 403
Cdd:PRK07824 154 DAVLVGGGPAPAP--VLDAAAAA-GINVVRTYGMSETS-------------GGCVydGVPLDGVRVRVED---------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 404 pGELCVRGPQVMLGYwQRPDATDEIIKDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEV 483
Cdd:PRK07824 208 -GRIALGGPTLAKGY-RNPVDPDPFAEPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 484 AAVGVPSGSSGEAVKIFVVKK-DPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK07824 285 AVFGLPDDRLGQRVVAAVVGDgGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-553 |
2.92e-27 |
|
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: 114.76 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05940 1 DEALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIvsnfahtlekvvektqvkhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmqyvkpeivs 205
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 eDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnatYGPLLHPGKELVITALPLYHIFALTMnCLLFIELGGQNVLITNP 285
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAWRGGAFF---AGSGGALPSDVLYTCLPLYHSTALIV-GWSACLASGATLVIRKK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 286 RDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPvqqavAERWVKLTGQY----LLEGYGLTE 361
Cdd:cd05940 157 FSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLR-----PDIWEEFKERFgvprIAEFYAATE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 362 CApLVSVNphdIDYHSGSIG----LPVPSTEAKLVD-DEDN------------EVPHGEPGELCVR--GPQVMLGYWQrP 422
Cdd:cd05940 232 GN-SGFIN---FFGKPGAIGrnpsLLRKVAPLALVKyDLESgepirdaegrciKVPRGEPGLLISRinPLEPFDGYTD-P 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 423 DATDEIIK-------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVP-SGSSG 494
Cdd:cd05940 307 AATEKKILrdvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvPGTDG 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 495 EA-VKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05940 387 RAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-553 |
2.78e-26 |
|
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: 112.13 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQeGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VivsnfahtlekvvektqvkhvilTRMGDQLSTAKGTlvnfvvkyvkrlvpkyHLP--DAISFRRALhagyrmqyvkpei 203
Cdd:cd05939 80 I-----------------------FNLLDPLLTQSST----------------EPPsqDDVNFRDKL------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 vsedlaFLQYTGGTTGVAKGAMLTHRNMLanLEQVNATYGPLLHPgKELVITALPLYHIFALTM---NCLLFielgGQNV 280
Cdd:cd05939 108 ------FYIYTSGTTGLPKAAVIVHSRYY--RIAAGAYYAFGMRP-EDVVYDCLPLYHSAGGIMgvgQALLH----GSTV 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 281 LITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPvqqavAERWVKLTGQY----LLEG 356
Cdd:cd05939 175 VIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR-----PQIWEQFVRRFgipqIGEF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 357 YGLTECaplvSVNPHDIDYHSGSIGLpVPSTEAKL-------VDDEDNE------------VPhGEPGELCVRGPQ---- 413
Cdd:cd05939 250 YGATEG----NSSLVNIDNHVGACGF-NSRILPSVypirlikVDEDTGElirdsdglcipcQP-GEPGLLVGKIIQndpl 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 414 -VMLGYWQRPDATDEIIKDGWLH------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAV 486
Cdd:cd05939 324 rRFDGYVNEGATNKKIARDVFKKgdsaflSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVY 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 487 GVP-SGSSGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:cd05939 404 GVEvPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
35-549 |
4.54e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 112.01 E-value: 4.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 35 RYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEGlGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTprele 114
Cdd:PRK13383 47 RWPGRTAIIDDDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFR----- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 115 hqlNDSGAAAIVivsnfAHTLEKVVEKTQvkhviltrMGDQLSTAKgtlvnfvvkyvkrlvpkyhlpDAISFRRALHAGY 194
Cdd:PRK13383 121 ---SDALAAALR-----AHHISTVVADNE--------FAERIAGAD---------------------DAVAVIDPATAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 195 RMQYVKPEIVSEDLAFLqYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVItALPLYHIFALTMnCLLFIE 274
Cdd:PRK13383 164 EESGGRPAVAAPGRIVL-LTSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISV-AMPMFHGLGLGM-LMLTIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 275 LGGqNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLN--NKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQY 352
Cdd:PRK13383 241 LGG-TVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYwqrPDATDEIIKDG 432
Cdd:PRK13383 320 LYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVVDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 433 WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPS-LTED 511
Cdd:PRK13383 397 MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSgVDAA 476
|
490 500 510
....*....|....*....|....*....|....*...
gi 489956626 512 ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK13383 477 QLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-458 |
2.41e-25 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 110.59 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 2 KKVWLNRYPADVPAE----INPDRYQSLIE-----------LFEHSVRRYADQP----------AFVNMGEVMTFRKLE- 55
Cdd:PLN02387 22 KKGKKRGVPVDVGGEpgyaIRNARFPELVEtpwegattlaaLFEQSCKKYSDKRllgtrklisrEFETSSDGRKFEKLHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 56 ------------ERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAA 123
Cdd:PLN02387 102 geyewitygqvfERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 124 AIVIVSNFAHTLEKVVEK-TQVKHVI-LTRMGDQLSTAKGTLVNFVVkyvkrlvpkyhlpdaISFRRALHAGyRMQYVKP 201
Cdd:PLN02387 181 TVICDSKQLKKLIDISSQlETVKRVIyMDDEGVDSDSSLSGSSNWTV---------------SSFSEVEKLG-KENPVDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 202 EI-VSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVnATYGPLLHPgKELVITALPLYHIFALTMNCLLF-----IEL 275
Cdd:PLN02387 245 DLpSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGV-MTVVPKLGK-NDVYLAYLPLAHILELAAESVMAavgaaIGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 276 GGQNVLITNPRDIP----GLVKELAKypfTAMTGV----------------------NTLFN-------ALLNNKEF--- 319
Cdd:PLN02387 323 GSPLTLTDTSNKIKkgtkGDASALKP---TLMTAVpaildrvrdgvrkkvdakgglaKKLFDiaykrrlAAIEGSWFgaw 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 320 -------QQLDFSTLHLSAG--------GGMPVQqAVAERWVKLT-GQYLLEGYGLTE-CAPLVSVNPHDIDYhsGSIGL 382
Cdd:PLN02387 400 glekllwDALVFKKIRAVLGgrirfmlsGGAPLS-GDTQRFINIClGAPIGQGYGLTEtCAGATFSEWDDTSV--GRVGP 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 383 PVPSTEAKLVDDE-------DNEVPHGEpgeLCVRGPQVMLGYWQRPDATDEIIKDG-----WLHTGDIAVMDDEGFLRI 450
Cdd:PLN02387 477 PLPCCYVKLVSWEeggylisDKPMPRGE---IVIGGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEI 553
|
....*...
gi 489956626 451 VDRKKDMI 458
Cdd:PLN02387 554 IDRKKDIV 561
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-549 |
3.22e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.20 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 7 NRYPADVPAEINPDRyqslieLFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQ 86
Cdd:PRK12316 3047 NATAAEYPLERGVHR------LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLE 3119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 87 YPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAaaivivsnfahtlekvvektqvkHVILTRMGDQLSTAKGtlvnf 166
Cdd:PRK12316 3120 MVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA-----------------------QLLLSQSHLRLPLAQG----- 3171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 167 vvkyVKRLVPKYHLPDAISFRRALHagyrmqyvkpeIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplL 246
Cdd:PRK12316 3172 ----VQVLDLDRGDENYAEANPAIR-----------TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG--L 3234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 247 HPGKELVITALPLYHIFALTMNCLLfieLGGQNVLITNPR---DIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLD 323
Cdd:PRK12316 3235 GVGDRVLQFTTFSFDVFVEELFWPL---MSGARVVLAGPEdwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRCT 3311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 324 FSTLHLSAGGGMPVQqaVAERWVklTGQYLLEGYGLTECAPLVSVNPHDIDYHSGS-IGLPVPSTEAKLVDDEDNEVPHG 402
Cdd:PRK12316 3312 SLKRIVCGGEALPAD--LQQQVF--AGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYILDGSLEPVPVG 3387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 403 EPGELCVRGPQVMLGYWQRPDATDE-------IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PRK12316 3388 ALGELYLGGEGLARGYHNRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLL 3467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489956626 476 QHSGVLEVAAVGVpsgsSGEAVKIFVVKKDPSLT-EDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK12316 3468 EHPWVREAVVLAV----DGRQLVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
190-476 |
1.48e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 108.18 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 190 LHAGYRMQYVKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLA-------NLEQVNATYGPllhpgKELVITALPLYHI 262
Cdd:PLN02614 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTliagvirLLKSANAALTV-----KDVYLSYLPLAHI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 263 FALTMN-CllFIELGGQ--------NVLITN------------PRDI----PGLVKELA--------------KYPFTAM 303
Cdd:PLN02614 282 FDRVIEeC--FIQHGAAigfwrgdvKLLIEDlgelkptifcavPRVLdrvySGLQKKLSdggflkkfvfdsafSYKFGNM 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 304 ------TGVNTLFNALLNNKEFQQLDfSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTE-CAPLVSVNPHDIDYh 376
Cdd:PLN02614 360 kkgqshVEASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDELDM- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 377 SGSIGLPVPSTEAKL--VDDEDNEVPHGEP-GELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDR 453
Cdd:PLN02614 438 LGTVGPPVPNVDIRLesVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDR 517
|
330 340
....*....|....*....|....
gi 489956626 454 KKDMI-LVSGFNVYPNEIEDVVMQ 476
Cdd:PLN02614 518 KKNIFkLSQGEYVAVENIENIYGE 541
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
69-452 |
1.63e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 107.82 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 69 LGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEH----QLNDSGAAAIVIVSN---FAHTLEkVVEK 141
Cdd:PRK12582 100 LGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHaklkHLFDLVKPRVVFAQSgapFARALA-ALDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 142 TQVKHVILTRMGD-QLSTAKGTLVNFVVKyvkrlvpkyhlpDAIsfrRALHAGyrmqyVKPEIVSEDLaflqYTGGTTGV 220
Cdd:PRK12582 179 LDVTVVHVTGPGEgIASIAFADLAATPPT------------AAV---AAAIAA-----ITPDTVAKYL----FTSGSTGM 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 221 AKGAMLTHRNMLANLEQVNATYGPLLHPGKELVITALPLYHIFA--LTMNCLLFielGGQNVLITNPRDIPGLVKELAK- 297
Cdd:PRK12582 235 PKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnANFNGLLW---GGGTLYIDDGKPLPGMFEETIRn 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 298 -------YPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERW----VKLTGQY--LLEGYGLTECAP 364
Cdd:PRK12582 312 lreisptVYGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMqalaVRTTGHRipFYTGYGATETAP 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 365 lVSVNPHDIDYHSGSIGLPVPSTEAKLvddedneVPHGEPGELCVRGPQVMLGYWQRPDATDeiikdgwlhtgdiAVMDD 444
Cdd:PRK12582 392 -TTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELTA-------------AAFDE 450
|
....*...
gi 489956626 445 EGFLRIVD 452
Cdd:PRK12582 451 EGFYRLGD 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
2.60e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 108.33 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVV 102
Cdd:PRK05691 1131 AWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 103 NVNPLYTPRELEHQLNDSGAAAIVIVSnfaHTLEKVVEKTQVKHVILtrmgDQLStakgtLVNFVVKyvkrlVPKYHLPD 182
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQS---HLLERLPQAEGVSAIAL----DSLH-----LDSWPSQ-----APGLHLHG 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 183 aisfrralhagyrmqyvkpeivsEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITA-----L 257
Cdd:PRK05691 1273 -----------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDSDVLMQKApisfdV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 258 PLYHIF-ALTMNCLLFIELGGQNvliTNPRDIPGLVKElakYPFTAMTGVNTLFNALLNnkEFQQLDFSTLHLSAGGGMP 336
Cdd:PRK05691 1328 SVWECFwPLITGCRLVLAGPGEH---RDPQRIAELVQQ---YGVTTLHFVPPLLQLFID--EPLAAACTSLRRLFSGGEA 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 337 VQQAVAERWVKLTGQYLLEG-YGLTECAPLVSvnpH----DIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRG 411
Cdd:PRK05691 1400 LPAELRNRVLQRLPQVQLHNrYGPTETAINVT---HwqcqAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGG 1476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 412 PQVMLGYWQRPDAT------DEIIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVlEV 483
Cdd:PRK05691 1477 AGLARGYLGRPALTaerfvpDPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV-AQ 1555
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 484 AAVGVPSGSSG-EAVKIFVVKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 1556 AAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
23-452 |
3.47e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 106.89 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMG-----EVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRA 97
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAMYA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 98 GMIVVNVNPLYT-----PRELEHQLN---------DSGAA---AIVIVSnFAHTlEKVVEKTQVKHVILTRMGDQLSTAK 160
Cdd:PRK08180 118 GVPYAPVSPAYSlvsqdFGKLRHVLElltpglvfaDDGAAfarALAAVV-PADV-EVVAVRGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 161 GTLVNfvvkyvkrlvpkyhlpdaisfrrALHAGyrmqyVKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA 240
Cdd:PRK08180 196 TAAVD-----------------------AAHAA-----VGPD----TIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 241 TYgPLLHPGKELVITALPLYHIFALTMNCLLFIELGGqNVLITNPRDIPGLVKE----LAKYPFTAMTGVNTLFNALLN- 315
Cdd:PRK08180 244 TF-PFLAEEPPVLVDWLPWNHTFGGNHNLGIVLYNGG-TLYIDDGKPTPGGFDEtlrnLREISPTVYFNVPKGWEMLVPa 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 316 ---NKEFQQLDFSTLHLS--AGGGMPvqQAVAERWVKLTGQYLLE------GYGLTECAPLVSvNPHDIDYHSGSIGLPV 384
Cdd:PRK08180 322 lerDAALRRRFFSRLKLLfyAGAALS--QDVWDRLDRVAEATCGErirmmtGLGMTETAPSAT-FTTGPLSRAGNIGLPA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 385 PSTEAKLVddednevPHGEPGELCVRGPQVMLGYWQRPDATDEiikdgwlhtgdiaVMDDEGFLRIVD 452
Cdd:PRK08180 399 PGCEVKLV-------PVGGKLEVRVKGPNVTPGYWRAPELTAE-------------AFDEEGYYRSGD 446
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
353-553 |
3.97e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 106.26 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPLVSVNPhdiDYHSGSIGLPVPSTE----------AKLVDDEDNEVPHGEP--GELCVR-GPQVMLGYW 419
Cdd:PRK13388 291 VEDGYGSSEGAVIVVREP---GTPPGSIGRGAPGVAiynpetltecAVARFDAHGALLNADEaiGELVNTaGAGFFEGYY 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKI 499
Cdd:PRK13388 368 NNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489956626 500 FVVKKDP-SLTEDALITFCRRQ--LTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK13388 448 ALVLRDGaTFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
74-499 |
1.10e-23 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 104.90 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 74 GDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGaaaivivsnfahtlekvvektqVKHVILTR-M 152
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVG----------------------VTHVLTSKqL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 153 GDQLSTAKGtlvnFVVKYVKRLVPKYHLPDAISFRRALHAGYRMQYVKPEIV---------SEDLAFLQYTGGTTGVAKG 223
Cdd:PRK06334 125 MQHLAQTHG----EDAEYPFSLIYMEEVRKELSFWEKCRIGIYMSIPFEWLMrwfgvsdkdPEDVAVILFTSGTEKLPKG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 224 AMLTHRNMLANLEQVNATYGPLlhpGKELVITALPLYHIFALTmNCLLFIELGGQNVLIT-NPRDIPGLVKELAKYPFTA 302
Cdd:PRK06334 201 VPLTHANLLANQRACLKFFSPK---EDDVMMSFLPPFHAYGFN-SCTLFPLLSGVPVVFAyNPLYPKKIVEMIDEAKVTF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 303 MTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERWVKLTGQYLL-EGYGLTECAPLVSVNPHDIDYHSGSIG 381
Cdd:PRK06334 277 LGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLrQGYGTTECSPVITINTVNSPKHESCVG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 382 LPVPSTEAKLVDDEDN-EVPHGEPGELCVRGPQVMLGYWQRpDATDEIIK---DGWLHTGDIAVMDDEGFLRIVDRKKDM 457
Cdd:PRK06334 357 MPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGE-DFGQGFVElggETWYVTGDLGYVDRHGELFLKGRLSRF 435
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 489956626 458 ILVSGFNVYPNEIEDVVMQHSGVLEVAAVG--VPSGSSGEAVKI 499
Cdd:PRK06334 436 VKIGAEMVSLEALESILMEGFGQNAADHAGplVVCGLPGEKVRL 479
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
201-452 |
2.01e-23 |
|
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: 104.05 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 201 PEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpllHPGKE--LVITALPLYHIFALTMNCLLFIELGGq 278
Cdd:cd05921 160 AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYP---FFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGG- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 279 NVLITNPRDIPGLVKELAK--------YPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPVQQAVAERW----V 346
Cdd:cd05921 236 TLYIDDGKPMPGGFEETLRnlreisptVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLqalaV 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 347 KLTGQY--LLEGYGLTECAPLvSVNPHDIDYHSGSIGLPVPSTEAKLVddednevPHGEPGELCVRGPQVMLGYWQRPDA 424
Cdd:cd05921 316 ATVGERipMMAGLGATETAPT-ATFTHWPTERSGLIGLPAPGTELKLV-------PSGGKYEVRVKGPNVTPGYWRQPEL 387
|
250 260
....*....|....*....|....*...
gi 489956626 425 TdeiikdgwlhtgdIAVMDDEGFLRIVD 452
Cdd:cd05921 388 T-------------AQAFDEEGFYCLGD 402
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
201-549 |
2.63e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 105.25 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 201 PEIVS--EDLAFLQYTGGTTGVAKGAMLTHRNMLAN-LEQVnatygPLLHPGKELVItALPLYHIFALTMNCLLFIELGG 277
Cdd:PRK05691 3862 PGIYSgpDNLAYVIYTSGSTGLPKGVMVEQRGMLNNqLSKV-----PYLALSEADVI-AQTASQSFDISVWQFLAAPLFG 3935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 QNVLITnPRDIP----GLVKELAKYPFTAMTGVNTLFNALLNNKEfQQLDFSTLHLSAGGGMPVQqaVAERWVKLTGQY- 352
Cdd:PRK05691 3936 ARVEIV-PNAIAhdpqGLLAHVQAQGITVLESVPSLIQGMLAEDR-QALDGLRWMLPTGEAMPPE--LARQWLQRYPQIg 4011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 LLEGYGLTECAPLVSVNPHDIDYHSGS---IGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQRPDATDEI- 428
Cdd:PRK05691 4012 LVNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAf 4091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 429 -------IKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEvAAVGVPSGSSGEAVKIFV 501
Cdd:PRK05691 4092 vphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYL 4170
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489956626 502 VKKDPSLTEDALITFCRRQLTG----YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 4171 VPHQTVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
205-550 |
1.42e-22 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 101.38 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 SEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITALPLYHIFALTMncLLFIELGGQnvlitn 284
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG--LDAATDVGCSWLPLYHDMGLAF--LLTAALAGA------ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 285 prdipglvkELAKYPFTA-----------MTGVNTLFNALLN---------NKEFQQLDFSTLHLSAGGGMPVQQAVAER 344
Cdd:PRK05851 221 ---------PLWLAPTTAfsaspfrwlswLSDSRATLTAAPNfaynligkyARRVSDVDLGALRVALNGGEPVDCDGFER 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 345 WVKLTGQY------LLEGYGLTE--CAPLVSVnP------HDIDYHSGS-------IGLPVPSTEAKLV-DDEDNEVPHG 402
Cdd:PRK05851 292 FATAMAPFgfdagaAAPSYGLAEstCAVTVPV-PgiglrvDEVTTDDGSgarrhavLGNPIPGMEVRISpGDGAAGVAGR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 403 EPGELCVRGPQVMLGYWqrpdATDEIIKDGWLHTGDIAVMDDEGfLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLE 482
Cdd:PRK05851 371 EIGEIEIRGASMMSGYL----GQAPIDPDDWFPTGDLGYLVDGG-LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVRE 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 483 --VAAVGVPSGS--SGEAVKIFVVKKDPSLTEDALITFCRRQlTGYkVPKLVEFRD--ELPKSNVGKILRRELR 550
Cdd:PRK05851 446 gaVVAVGTGEGSarPGLVIAAEFRGPDEAGARSEVVQRVASE-CGV-VPSDVVFVApgSLPRTSSGKLRRLAVK 517
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
37-553 |
2.25e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 101.37 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 37 ADQPAFVNMGE------VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMI--VVNVNplY 108
Cdd:PRK00174 81 GDKVAIIWEGDdpgdsrKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsVVFGG--F 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 109 TPRELEHQLNDSGAAAIVIVSNF-----AHTLEKVVEK-----TQVKHVIltrmgdqlstakgtlvnfVVKYVKRLVP-- 176
Cdd:PRK00174 158 SAEALADRIIDAGAKLVITADEGvrggkPIPLKANVDEalancPSVEKVI------------------VVRRTGGDVDwv 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 177 -----KYHlpDAISFRRAlhagyrmqYVKPEIV-SEDLAFLQYTGGTTGVAKG-----------AMLTHRNML------- 232
Cdd:PRK00174 220 egrdlWWH--ELVAGASD--------ECEPEPMdAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVFdykdgdv 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 233 ----ANLEQVNA----TYGPLLHPGKELVITALPLY-------HIfaltmncllfIELGGQNVLITNPRDIPGLVKELAK 297
Cdd:PRK00174 290 ywctADVGWVTGhsyiVYGPLANGATTLMFEGVPNYpdpgrfwEV----------IDKHKVTIFYTAPTAIRALMKEGDE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 298 YPftamtgvntlfnallnnkefQQLDFSTLHLSAGGGMPV--------QQAV-AER-------WVKLTGQYLLegyglte 361
Cdd:PRK00174 360 HP--------------------KKYDLSSLRLLGSVGEPInpeawewyYKVVgGERcpivdtwWQTETGGIMI------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 362 cAPLvsvnPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRG--PQVMLGYWQRPD-------ATdeiIKDG 432
Cdd:PRK00174 413 -TPL----PGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHErfvktyfST---FKGM 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 433 WLhTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDA 512
Cdd:PRK00174 485 YF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE 563
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 489956626 513 LIT----FCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PRK00174 564 LRKelrnWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIA 608
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-549 |
3.02e-22 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 99.78 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 38 DQPAFVNMGEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQL 117
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 118 NDSGAAAIVivsnfahtlekvvekTQVKhviltrmgdqlstakgtlvnfvvkyvkrlvpkyhlpdaisfrralhagyrmq 197
Cdd:cd17648 82 EDTGARVVI---------------TNST---------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 198 yvkpeivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGpLLHPGKElVITALPLYhIFALTMNCLLFIELGG 277
Cdd:cd17648 95 ---------DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDE-AVLFFSNY-VFDFFVEQMTLALLNG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 QNVLITNPR---DIPGLVKELAKYPFTAMTGVNTLFnallnnkefQQLDFSTL-HL----SAGggmpvQQAVAERWVKLT 349
Cdd:cd17648 163 QKLVVPPDEmrfDPDRFYAYINREKVTYLSGTPSVL---------QQYDLARLpHLkrvdAAG-----EEFTAPVFEKLR 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 350 GQY---LLEGYGLTEcaplVSVNPHDIDYHSG-----SIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGPQVMLGYWQR 421
Cdd:cd17648 229 SRFaglIINAYGPTE----TTVTNHKRFFPGDqrfdkSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNR 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 422 PD-----------ATDEIIKDG----WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAV 486
Cdd:cd17648 305 PEltaerflpnpfQTEQERARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVV 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489956626 487 G--VPSGSSGEAVKIFV---VKKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17648 385 AkeDASQAQSRIQKYLVgyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
31-550 |
7.01e-22 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 99.64 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 31 HSVRRyADQPAFV------NMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:PRK10524 62 HLAKR-PEQLALIavstetDEERTYTFRQLHDEVNRMAAMLRS-LGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 105 NPLYTPRELEHQLNDsgAAAIVIVS-----------NFAHTLEKVVEKTQVK--HVILTRMGdqlsTAKGTLVNfvvkyv 171
Cdd:PRK10524 140 FGGFASHSLAARIDD--AKPVLIVSadagsrggkvvPYKPLLDEAIALAQHKprHVLLVDRG----LAPMARVA------ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 172 KRLVPKYHLpdaisfrRALHAGYRmqyVKPEIV-SEDLAFLQYTGGTTGVAKGAmltHRNMlanleqvnatygpllhpGK 250
Cdd:PRK10524 208 GRDVDYATL-------RAQHLGAR---VPVEWLeSNEPSYILYTSGTTGKPKGV---QRDT-----------------GG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 251 ELVITALPLYHIF----ALTMNCLLFIE-------------LGGQNVLI---TNPRDIPGLVKEL-AKYpftamtGVNTL 309
Cdd:PRK10524 258 YAVALATSMDTIFggkaGETFFCASDIGwvvghsyivyaplLAGMATIMyegLPTRPDAGIWWRIvEKY------KVNRM 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 310 FNA-----LLNNKEFQQL---DFSTLHLSAGGGMPVQQAVAeRWVKLT-GQYLLEGYGLTECA-PLVSVNP--HDIDYHS 377
Cdd:PRK10524 332 FSAptairVLKKQDPALLrkhDLSSLRALFLAGEPLDEPTA-SWISEAlGVPVIDNYWQTETGwPILAIARgvEDRPTRL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 378 GSIGLPVPSTEAKLVDDEDNE-VPHGEPGELCVRGP---QVMLGYWqRPDatDEIIKDGWLH-------TGDIAVMDDEG 446
Cdd:PRK10524 411 GSPGVPMYGYNVKLLNEVTGEpCGPNEKGVLVIEGPlppGCMQTVW-GDD--DRFVKTYWSLfgrqvysTFDWGIRDADG 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 447 FLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDA---------LITFC 517
Cdd:PRK10524 488 YYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlalekeIMALV 567
|
570 580 590
....*....|....*....|....*....|...
gi 489956626 518 RRQLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
Cdd:PRK10524 568 DSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
327-461 |
7.08e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 99.89 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 327 LHLSAGGGMPVQQAVaERWVKLTG-QYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLvdDEDNEV---PHG 402
Cdd:PLN02430 385 LRLLISGGAPLSTEI-EEFLRVTScAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELRL--EEVPEMgydPLG 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 403 EP--GELCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PLN02430 462 EPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-536 |
7.28e-22 |
|
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: 99.29 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 46 GEVMTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 VIVSNFAHTLEKVVEKTQVKHVILTRMGDQLSTAK-GTLVNFVVKYVKRLVPKYhLPDAISFRralhagyrmqyvkpeiv 204
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGvISLLDKVDAASDEPVPAS-LRAHVTIK----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 205 seDLAFLQYTGGTTGVAKGAMLTHRNMLanleQVNATYgPLLHPGKELVI-TALPLYHIFALTMNCLLFIELGGQNVLIT 283
Cdd:cd05938 145 --SPALYIYTSGTTGLPKAARISHLRVL----QCSGFL-SLCGVTADDVIyITLPLYHSSGFLLGIGGCIELGATCVLKP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 284 nprdipglvK--------ELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGmpVQQAVAERWVKLTGQ-YLL 354
Cdd:cd05938 218 ---------KfsasqfwdDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNG--LRADVWREFLRRFGPiRIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 355 EGYGLTECaplvsvNPHDIDY--HSGSIG-------LPVP-------STEAKLVDDEDN---EVPHGEPGELC--VRGPQ 413
Cdd:cd05938 287 EFYGSTEG------NIGFFNYtgKIGAVGrvsylykLLFPfelikfdVEKEEPVRDAQGfciPVAKGEPGLLVakITQQS 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 414 VMLGYWQRPDATD-----EIIKDG--WLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAV 486
Cdd:cd05938 361 PFLGYAGDKEQTEkkllrDVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVY 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489956626 487 GVP-SGSSGEAVKIFVVKKDP-SLTEDALITFCRRQLTGYKVPKLVEFRDEL 536
Cdd:cd05938 441 GVTvPGHEGRIGMAAVKLKPGhEFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
23-549 |
2.54e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.09 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQE-GLGLQKgdRVALMMPNLLQYPVALFGILRAGMIV 101
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRErGVGPQV--RVGLALERSLEMVVGLLAILKAGGAY 2265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 102 VNVNPLYTPRELEHQLNDSGaaaIVIVSNFAHTLEKVVE-KTQVKHVILTRMGDQLSTakgtlvnfvvkYVKRLVPKYHL 180
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSG---IGLLLSDRALFEALGElPAGVARWCLEDDAAALAA-----------YSDAPLPFLSL 2331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 181 PDaisfrralhagyrmqyvkpeivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKelviTALPLY 260
Cdd:PRK05691 2332 PQ------------------------HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFG--MRADD----CELHFY 2381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 261 HI-FALTMNCLLFIELGGQNVLIT-----NPRDIPGLVKELAkypfTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGG 334
Cdd:PRK05691 2382 SInFDAASERLLVPLLCGARVVLRaqgqwGAEEICQLIREQQ----VSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGG 2457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 335 mpvQQAVAERWVKLTG----QYLLEGYGLTECA--PLVSVNPHDIDYHSGS--IGLPVPSTEAKLVDDEDNEVPHGEPGE 406
Cdd:PRK05691 2458 ---EALTGEHLQRIRQafapQLFFNAYGPTETVvmPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGE 2534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 407 LCVRGPQVMLGYWQRPDATDE-IIKDGWLH-------TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:PRK05691 2535 LYVGGAGLAQGYHDRPGLTAErFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 479 GVLE--VAAVGVPsgsSGEAVKIFVVKKDPSLTED-------ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:PRK05691 2615 AVREavVLALDTP---SGKQLAGYLVSAVAGQDDEaqaalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
23-555 |
1.23e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 95.35 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 23 QSLIELFEHSVRRYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVAL---MMPNLLqypVALFGILRAGM 99
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDS-LKLPDKSPIIVfghMSPEML---ATFLGAVKAGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 100 IVVNVNpLYTPRELEHQLNDSGAAAIVIvsnfaHTLEKVVEKTQVKHVILtrmgDQLSTAKGTLVNFVVKyvkrlvpkyh 179
Cdd:PRK04813 78 AYIPVD-VSSPAERIEMIIEVAKPSLII-----ATEELPLEILGIPVITL----DELKDIFATGNPYDFD---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 180 lpdaisfrralhagyrmQYVKPEivseDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPllhpGKELVITALPL 259
Cdd:PRK04813 138 -----------------HAVKGD----DNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL----PEGPQFLNQAP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 260 YHiFALT-MN---CLLfieLGGQNV-----LITNPRDipgLVKELAKYPFTAMTGVNTLFNALLNNKEF--QQLDFSTLH 328
Cdd:PRK04813 193 YS-FDLSvMDlypTLA---SGGTLValpkdMTANFKQ---LFETLPQLPINVWVSTPSFADMCLLDPSFneEHLPNLTHF 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 329 LSAGGGMPVQ--QAVAERWVKLTgqyLLEGYGLTECAPLVS---VNPHDID-YHSGSIGLPVPSTEAKLVDDEDNEVPHG 402
Cdd:PRK04813 266 LFCGEELPHKtaKKLLERFPSAT---IYNTYGPTEATVAVTsieITDEMLDqYKRLPIGYAKPDSPLLIIDEEGTKLPDG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 403 EPGELCVRGPQVMLGYWQRPDATDEIIK--DGW--LHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHS 478
Cdd:PRK04813 343 EQGEIVISGPSVSKGYLNNPEKTAEAFFtfDGQpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSS 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 479 GVLEvaAVGVPSGSSGEAVKI--FVVKKDPSLTEDALITFCRRQ-----LTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
Cdd:PRK04813 422 YVES--AVVVPYNKDHKVQYLiaYVVPKEEDFEREFELTKAIKKelkerLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
....
gi 489956626 552 EARA 555
Cdd:PRK04813 500 EVNK 503
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
207-511 |
5.66e-20 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 93.75 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 207 DLAFLQYTGGTTGVAKGAMLTHRNMLAnleQVNATYGPLLHPGK-----ELVITALPLYHIFALTMNcLLFIELGG---- 277
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIA---EVLSTDHLLKVTDRvateeDSYFSYLPLAHVYDQVIE-TYCISKGAsigf 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 278 ---------QNVLITNPR---DIP------------------GLVKELAKYPFTAMTG----------VNTLFNALLNNK 317
Cdd:PLN02861 297 wqgdirylmEDVQALKPTifcGVPrvydriytgimqkissggMLRKKLFDFAYNYKLGnlrkglkqeeASPRLDRLVFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 318 EFQQLDfSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGYGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVD---- 393
Cdd:PLN02861 377 IKEGLG-GRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTTIEARLESvpem 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 394 --DEDNEVPHGEpgeLCVRGPQVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS-GFNVYPNEI 470
Cdd:PLN02861 456 gyDALSDVPRGE---ICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENL 532
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489956626 471 EDVVMQHSgvlEVAAVGVpSGSSGEAVKIFVVKKDPSLTED 511
Cdd:PLN02861 533 ENTYSRCP---LIASIWV-YGNSFESFLVAVVVPDRQALED 569
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
357-551 |
1.24e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 91.59 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 357 YGLTECAPLVSV-NPHDIDYHSGSIGLPVPstEAKLvddednEVPHGEPGELCVRGPQVMLGYWqrPDATDeiiKDGWLH 435
Cdd:PRK07445 261 YGMTETASQIATlKPDDFLAGNNSSGQVLP--HAQI------TIPANQTGNITIQAQSLALGYY--PQILD---SQGIFE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 436 TGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVVKKDPSLTEDALIT 515
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKT 407
|
170 180 190
....*....|....*....|....*....|....*....
gi 489956626 516 FCRRQLTGYKVPK---LVEfrdELPKSNVGKILRRELRD 551
Cdd:PRK07445 408 AIKDQLSPFKQPKhwiPVP---QLPRNPQGKINRQQLQQ 443
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
35-560 |
6.16e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 89.55 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 35 RYADQPAFVNMGEVMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPlytprele 114
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQ-QGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 115 hQLNDSgaaaivivsnfahTLEKVVEKTQVKHvILTRMGDQLSTAKGTLvnfvvkyvkrLVPKYHLPDAISFRralhagy 194
Cdd:PRK09029 86 -QLPQP-------------LLEELLPSLTLDF-ALVLEGENTFSALTSL----------HLQLVEGAHAVAWQ------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 195 rmqyvkpeivSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNA--TYGP----LLhpgkelvitALPLYHI------ 262
Cdd:PRK09029 134 ----------PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSlmPFTAqdswLL---------SLPLFHVsgqgiv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 263 ----FAltmncllfielGGQNVLitnpRDIPGLVKELAKypFTAMTGVNTLFNALLNNKefqQLDFSTLHLSAGGGM-PV 337
Cdd:PRK09029 195 wrwlYA-----------GATLVV----RDKQPLEQALAG--CTHASLVPTQLWRLLDNR---SEPLSLKAVLLGGAAiPV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 338 ---QQAVA---ERWVkltgqylleGYGLTECAPLVSVNPhdIDYHSGsIGLPVPSTEAKLVDDEdnevphgepgeLCVRG 411
Cdd:PRK09029 255 eltEQAEQqgiRCWC---------GYGLTEMASTVCAKR--ADGLAG-VGSPLPGREVKLVDGE-----------IWLRG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 412 PQVMLGYWQ----RPdATDEiikDGWLHTGDIAVMDDeGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVG 487
Cdd:PRK09029 312 ASLALGYWRqgqlVP-LVND---EGWFATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVP 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 488 VPSGSSGE---AvkifVVKKDPSLTEDALITFCRRQLTGYKVPklVEF---RDELPKSNVgKILRRELRDEARAKVDNK 560
Cdd:PRK09029 387 VADAEFGQrpvA----VVESDSEAAVVNLAEWLQDKLARFQQP--VAYyllPPELKNGGI-KISRQALKEWVAQQLGNN 458
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-485 |
1.14e-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: 89.33 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEhqlndsgaaaiVIVS 129
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLG-----------FLLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 130 NFAHTLEKVVEKTQVKHVILTRmgdqLSTAKGTLVNfvvkyvKRLVPKYHLPDAISFRRALHAgyRMQYVKPEIVSEDLA 209
Cdd:cd05905 85 TCKVRVALTVEACLKGLPKKLL----KSKTAAEIAK------KKGWPKILDFVKIPKSKRSKL--KKWGPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMLTHRNMLA---NLEQVNATYgpllhpGKELVITALPLYHIFALTMNCLLFIELGGQNVLI---- 282
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAhcrALKEACELY------ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIppel 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 283 --TNPrdiPGLVKELAKYP-FTAMTGVNTLFNALLN-NKEFQQLDFSTLHLS------AGGGMPVQQAVAERWVKL---- 348
Cdd:cd05905 227 mkTNP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDlSSTLASLKNRDVNLSslrmcmVPCENRPRISSCDSFLKLfqtl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 349 ----------------------------TGQYLLEGYGLTECAP-LVSVN-PHDIDYHSGsiGLPVPSTEAKLVDDEdnE 398
Cdd:cd05905 304 glspravstefgtrvnpficwqgtsgpePSRVYLDMRALRHGVVrLDERDkPNSLPLQDS--GKVLPGAQVAIVNPE--T 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 399 VPH---GEPGELCVRGPQVMLGYWQRPDATDEIIKD-------------GWLHTGDI----------AVMDDEGFLRIVD 452
Cdd:cd05905 380 KGLckdGEIGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnnSYARTGLLgflrptkctdLNVEEHDLLFVVG 459
|
490 500 510
....*....|....*....|....*....|....
gi 489956626 453 RKKDMILVSGFNVYPNEIEDVVMQ-HSGVLEVAA 485
Cdd:cd05905 460 SIDETLEVRGLRHHPSDIEATVMRvHPYRGRCAV 493
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
469-543 |
1.23e-18 |
|
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: 80.28 E-value: 1.23e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489956626 469 EIEDVVMQHSGVLEVAAVGVPSGSSGEAVKIFVV-KKDPSLTEDALITFCRRQLTGYKVPKLVEFRDELPKSNVGK 543
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
206-552 |
2.14e-17 |
|
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: 84.79 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANlEQVNATYgplLHPGKEL-VITALPLYHIFAL---TMNCLLFielGGQNVL 281
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVT-SNLLSHD---LNLKNGDrTYTCMPLYHGTAAflgACNCLMS---GGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 282 -------------ITNPRDIPGLVKELAKYpftamtgvntLFNALLNNKEFQQldfsTLHLSAGGGM--PVQQAVAERW- 345
Cdd:cd05937 160 srkfsasqfwkdvRDSGATIIQYVGELCRY----------LLSTPPSPYDRDH----KVRVAWGNGLrpDIWERFRERFn 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 346 VKLTGQYllegYGLTEcAPLVSVNPHDIDYHSGSIGL--------------PV---PSTEAKLVDDEDN---EVPHGEPG 405
Cdd:cd05937 226 VPEIGEF----YAATE-GVFALTNHNVGDFGAGAIGHhglirrwkfenqvvLVkmdPETDDPIRDPKTGfcvRAPVGEPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 406 ELCVRGPQVML----GYWQRPDATD-EIIK------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
Cdd:cd05937 301 EMLGRVPFKNReafqGYLHNEDATEsKLVRdvfrkgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 475 MQHSGVLEVAAVGVP-SGSSGEAVKIFVVKKDPSLTEDALI-----TFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRE 548
Cdd:cd05937 381 GAHPDIAEANVYGVKvPGHDGRAGCAAITLEESSAVPTEFTksllaSLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGV 460
|
....
gi 489956626 549 LRDE 552
Cdd:cd05937 461 LRDE 464
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
35-461 |
6.91e-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: 84.04 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 35 RYADQPAF------VNMGEV--------------MTFRKLEERSRAFAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGI 94
Cdd:cd17632 34 GYADRPALgqrateLVTDPAtgrttlrllprfetITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 95 LRAGMIVVnvnPLYT---PRELEHQLNDSGAAAI-VIVSNFAHTLEKVVEKTQVKHVI-------LTRMGDQLSTAKGTL 163
Cdd:cd17632 114 TRLGAVSV---PLQAgasAAQLAPILAETEPRLLaVSAEHLDLAVEAVLEGGTPPRLVvfdhrpeVDAHRAALESARERL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 164 VNFVVKYVkrlvpkyhLPDAISFR-RALHAGYRMqyvKPEIVSEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATY 242
Cdd:cd17632 191 AAVGIPVT--------TLTLIAVRgRDLPPAPLF---RPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 243 GPllHPGKELVITALPLYHIfaltmncllfielGGQNVLITnprdipGLVKELAKYpFTAMTGVNTLFN--ALLNNKE-- 318
Cdd:cd17632 260 DI--RPPASITLNFMPMSHI-------------AGRISLYG------TLARGGTAY-FAAASDMSTLFDdlALVRPTElf 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 319 ---------FQQLDFSTLHLSAGGGMPV---QQAVAE-RWVKLTGQY-------------------------LLEGYGLT 360
Cdd:cd17632 318 lvprvcdmlFQRYQAELDRRSVAGADAEtlaERVKAElRERVLGGRLlaavcgsaplsaemkafmeslldldLHDGYGST 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 361 EcAPLVSVNphdidyhsGSIGLPvPSTEAKLVDDED-----NEVPHgeP-GELCVRGPQVMLGYWQRPDATDEII-KDGW 433
Cdd:cd17632 398 E-AGAVILD--------GVIVRP-PVLDYKLVDVPElgyfrTDRPH--PrGELLVKTDTLFPGYYKRPEVTAEVFdEDGF 465
|
490 500
....*....|....*....|....*...
gi 489956626 434 LHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:cd17632 466 YRTGDVMAELGPDRLVYVDRRNNVLKLS 493
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-558 |
1.81e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 82.64 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSgAAAIVIV 128
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDC-KPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 129 SNFAHTLEKVVEKTQVKHVILTRmgdqlSTAKGTLVNFVVKY-----VKRLVPKYHLPDAISFRRALhAGYRMQYVKPEI 203
Cdd:PLN02654 199 CNAVKRGPKTINLKDIVDAALDE-----SAKNGVSVGICLTYenqlaMKREDTKWQEGRDVWWQDVV-PNYPTKCEVEWV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 204 VSEDLAFLQYTGGTTGVAKGAMLTHRNML----------------------ANLEQVNA----TYGPLLHPGKELVITAL 257
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMvytattfkyafdykptdvywctADCGWITGhsyvTYGPMLNGATVLVFEGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 258 PLYhifaltmncllfielggqnvlitnPRdiPGLVKELA-KYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGG--G 334
Cdd:PLN02654 353 PNY------------------------PD--SGRCWDIVdKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLGsvG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 335 MPVQQAvAERWV-KLTG-----------QYLLEGYGLTecaPLVSVNPHDidyhSGSIGLPVPSTEAKLVDDEDNEVPHG 402
Cdd:PLN02654 407 EPINPS-AWRWFfNVVGdsrcpisdtwwQTETGGFMIT---PLPGAWPQK----PGSATFPFFGVQPVIVDEKGKEIEGE 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 403 EPGELCVRGP-----QVMLGYWQRPDATDEIIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQH 477
Cdd:PLN02654 479 CSGYLCVKKSwpgafRTLYGDHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSH 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 478 SGVLEVAAVGVPSGSSGEAVKIFVVKKDP-SLTED---ALITFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
Cdd:PLN02654 559 PQCAEAAVVGIEHEVKGQGIYAFVTLVEGvPYSEElrkSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
....*
gi 489956626 554 RAKVD 558
Cdd:PLN02654 639 SRQLD 643
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
194-461 |
4.12e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 81.69 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 194 YRMQYVKPEIVSEdlafLQYTGGTTGVAKGAMLTHRNMLANL-----EQVNATYGPLLHpgkelvITALPLYHIFALTMN 268
Cdd:PTZ00342 296 YKIQNEDPDFITS----IVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTH------LSYLPISHIYERVIA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 269 CLLFIeLGGQnVLITNpRDIPGLVKELAKYPFTAMTGVNTLFNALL----------------------------NNKEFQ 320
Cdd:PTZ00342 366 YLSFM-LGGT-INIWS-KDINYFSKDIYNSKGNILAGVPKVFNRIYtnimteinnlpplkrflvkkilslrksnNNGGFS 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 321 QLDFSTLHLSA---------------GGGMPVQQAVAERWVKLTGQYLlEGYGLTECAPLVSVNPHDiDYHSGSIGLPV- 384
Cdd:PTZ00342 443 KFLEGITHISSkikdkvnpnlevilnGGGKLSPKIAEELSVLLNVNYY-QGYGLTETTGPIFVQHAD-DNNTESIGGPIs 520
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489956626 385 PSTEAKLVDDEDNEVPHGEP-GELCVRGPQVMLGYWQRPDATDE-IIKDGWLHTGDIAVMDDEGFLRIVDRKKDMILVS 461
Cdd:PTZ00342 521 PNTKYKVRTWETYKATDTLPkGELLIKSDSIFSGYFLEKEQTKNaFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
210-546 |
2.66e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 66.30 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 210 FLQYTGGTTGVAKGAMlthRNMLANLEQVNATYGPLLHPGKELVItaLPLYHIFALTMNCLLFIELGGQNVL------IT 283
Cdd:PTZ00237 258 YILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVV--FSHSSIGWVSFHGFLYGSLSLGNTFvmfeggII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 284 NPRDIP-GLVKELAKYPFT-AMTGVNTLFNALLNNKEFQQL----DFSTLHLSAGGGMPVQQAVAERWVKLTGQYLLEGY 357
Cdd:PTZ00237 333 KNKHIEdDLWNTIEKHKVThTLTLPKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 358 GLTE--CAPLVSVNPHDIDYHSgsIGLPVPSTEAKLVDDEDNEVPHGEPGELCVR---GPQVMLGYWQRpdatDEIIKD- 431
Cdd:PTZ00237 413 GQTEigITYLYCYGHINIPYNA--TGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKN----DEKFKQl 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 432 -----GWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGSSGEA-VKIFVVKKD 505
Cdd:PTZ00237 487 fskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVpIGLLVLKQD 566
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489956626 506 PSLTEDALITF-------CRRQLTGYKVPKLVEFRDELPKSNVGKILR 546
Cdd:PTZ00237 567 QSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
320-480 |
1.12e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.38 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 320 QQLDFSTLHLSAG--GGMPV----QQAVAERW-VKLtgqylLEGYGLTECAPLVSVNPHDIDyhsgsiGLPVPS----TE 388
Cdd:COG1541 196 EGIDPRDLSLKKGifGGEPWseemRKEIEERWgIKA-----YDIYGLTEVGPGVAYECEAQD------GLHIWEdhflVE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 389 akLVDDEDNE-VPHGEPGELCV----RGPQVMLGYwqrpdatdeiikdgwlHTGDIAVMDDEG---------FLRIVDRK 454
Cdd:COG1541 265 --IIDPETGEpVPEGEEGELVVttltKEAMPLIRY----------------RTGDLTRLLPEPcpcgrthprIGRILGRA 326
|
170 180
....*....|....*....|....*.
gi 489956626 455 KDMILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:COG1541 327 DDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
49-552 |
2.93e-07 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 53.54 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 49 MTFRKLEERSRAfAAYLQEGLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI--- 125
Cdd:PLN03052 209 MTLSELRSQVSR-VANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIftq 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 126 -VIV-SNFAHTL-EKVVEKTQVKHVILtrmgdqlsTAKGTLVNFVVKyVKRLVPKYHLPDAISFRRAlhagyrMQYVKPE 202
Cdd:PLN03052 288 dVIVrGGKSIPLySRVVEAKAPKAIVL--------PADGKSVRVKLR-EGDMSWDDFLARANGLRRP------DEYKAVE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 203 IVSEDLAFLQYTGGTTGVAKGAMLTHRNML-------ANLE-QVNATY----------GPLLHPGKELVITALPLYHIFA 264
Cdd:PLN03052 353 QPVEAFTNILFSSGTTGEPKAIPWTQLTPLraaadawAHLDiRKGDIVcwptnlgwmmGPWLVYASLLNGATLALYNGSP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 265 LTMNCLLFIELGGQNVLITnprdIPGLVKelakypftamTGVNTlfNALLNnkefqqLDFSTLHL--SAGGGMPVQQAVa 342
Cdd:PLN03052 433 LGRGFAKFVQDAKVTMLGT----VPSIVK----------TWKNT--NCMAG------LDWSSIRCfgSTGEASSVDDYL- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 343 erWVKLTGQY--LLEGYGLTECAPlvsvnphdiDYHSGSIGLP-------VPSTEAKLV--DDEDNEVPHGEP--GElCV 409
Cdd:PLN03052 490 --WLMSRAGYkpIIEYCGGTELGG---------GFVTGSLLQPqafaafsTPAMGCKLFilDDSGNPYPDDAPctGE-LA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 410 RGPQvMLG-------------YWQ-RPDATDEIIKDgwlHtGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVM 475
Cdd:PLN03052 558 LFPL-MFGasstllnadhykvYFKgMPVFNGKILRR---H-GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 476 Q-HSGVLEVAAVGVPSGSSG-EAVKIFVVKKDPSLTEDAL----ITFCR---RQLTG-YKVPKLVEFrDELPKSNVGKIL 545
Cdd:PLN03052 633 AaDESVLETAAIGVPPPGGGpEQLVIAAVLKDPPGSNPDLnelkKIFNSaiqKKLNPlFKVSAVVIV-PSFPRTASNKVM 711
|
....*..
gi 489956626 546 RRELRDE 552
Cdd:PLN03052 712 RRVLRQQ 718
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
92-554 |
6.39e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 52.13 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 92 FGILRAGMIVVNVNPLYTPRELEHQLNDSGAAAI-----VIVSNFAHTL-EKVVEKTQVKHVILTRMGDQLSTAkgtLVN 165
Cdd:PLN03051 12 LAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVftqdvVLRGGRALPLySKVVEAAPAKAIVLPAAGEPVAVP---LRE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 166 FVVKYVKRLVPKYHLPDAisfrRALHagYRMQYVKPEIVSEDLaflqYTGGTTGVAKGAMLTHRNML-------ANLE-Q 237
Cdd:PLN03051 89 QDLSWCDFLGVAAAQGSV----GGNE--YSPVYAPVESVTNIL----FSSGTTGEPKAIPWTHLSPLrcasdgwAHMDiQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 238 VNATY----------GPLLHPGKELVITALPLYHIFALTMNCLLFIELGGQNVLITnprdIPGLVKELAKYPFTAMTGVN 307
Cdd:PLN03051 159 PGDVVcwptnlgwmmGPWLLYSAFLNGATLALYGGAPLGRGFGKFVQDAGVTVLGL----VPSIVKAWRHTGAFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 308 -TLFNALLNNKEFQQLDfSTLHLSAGGGM--PVQQAVAErwVKLTGQYLLeGYGLTECAPlvsvnphdidyhsGSIGLPV 384
Cdd:PLN03051 235 wSKLRVFASTGEASAVD-DVLWLSSVRGYykPVIEYCGG--TELASGYIS-STLLQPQAP-------------GAFSTAS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 385 PSTEAKLVDDEDNEVPHGEP--GELCVRGPqvMLGYWQR--PDATDEIIKDG---WLHT-------GDIAVMDDEGFLRI 450
Cdd:PLN03051 298 LGTRFVLLNDNGVPYPDDQPcvGEVALAPP--MLGASDRllNADHDKVYYKGmpmYGSKgmplrrhGDIMKRTPGGYFCV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 451 VDRKKDMILVSGFNVYPNEIEDVVMQ-HSGVLEVAAVGV-PSGSSGEAVKIFVVKKDPSLT-----EDALITFCRRQLTG 523
Cdd:PLN03051 376 QGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVaPPDGGPELLVIFLVLGEEKKGfdqarPEALQKKFQEAIQT 455
|
490 500 510
....*....|....*....|....*....|....*.
gi 489956626 524 -----YKVPKlVEFRDELPKSNVGKILRRELRDEAR 554
Cdd:PLN03051 456 nlnplFKVSR-VKIVPELPRNASNKLLRRVLRDQLK 490
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
30-560 |
1.48e-06 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 51.03 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 30 EHSVRRYADQPAFVNMGEV-----MTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNV 104
Cdd:TIGR01217 91 ENLLRAAGTEPALLYVDEThepapVTWAELRRQVASLAAALRA-LGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 105 NPLYTPRELEHQLNDSGAAAIVIVSNFAHTlekvvEKTQVKHVILTRMGDQLSTAKGTLVNFVVKYVKRLVPKyhLPDAI 184
Cdd:TIGR01217 170 SPDFGARGVLDRFQQIEPKLLFTVDGYRYN-----GKEHDRRDKVAEVRKELPTLRAVVHIPYLGPRETEAPK--IDGAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 185 sFRRALHAGYRmqyvKPEIVSEDLAF-----LQYTGGTTGVAKgAMlthrnmlanleqVNATYGPLLHPGKELVITA--- 256
Cdd:TIGR01217 243 -DLEDFTAAAQ----AAELVFEQLPFdhplwILFSSGTTGLPK-CI------------VHSAGGTLVQHLKEHGLHCdlg 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 257 ----LPLYHIFALTM-NCLLFIELGGQNVLITNPRdiPGLVKELAKYPFTAMTGVnTLFNA------LLNNKEF---QQL 322
Cdd:TIGR01217 305 pgdrLFYYTTTGWMMwNWLVSGLATGATLVLYDGS--PGFPATNVLWDIAERTGA-TLFGTsakyvmACRKAGVhpaRTH 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 323 DFSTLHLSAGGGMPVqQAVAERWV----KLTGQYLLEGYGLTECAPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDEDNE 398
Cdd:TIGR01217 382 DLSALQCVASTGSPL-PPDGFRWVydeiKADVWLASISGGTDICSCFAGANP-TLPVHIGEIQAPGLGTAVQSWDPEGKP 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 399 VpHGEPGEL-CVRG-PQVMLGYWQRPDATD------EIIKDGWLHtGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEI 470
Cdd:TIGR01217 460 V-TGEVGELvCTNPmPSMPIRFWNDPDGSKyrdayfDTYPGVWRH-GDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEI 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 471 EDVVMQHSGVLEVAAVGVPSGSSGEAVKIFV-----VKKDPSLTeDALITFCRRQLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:TIGR01217 538 YNAVERLDEVRESLCIGQEQPDGGYRVVLFVhlapgATLDDALL-DRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRV 616
|
570
....*....|....*.
gi 489956626 546 RRELRDEARAK-VDNK 560
Cdd:TIGR01217 617 EVAVKRVLQGTpVDNP 632
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
276-539 |
1.93e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 50.87 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 276 GGQNVLITNPRDIPGLVKELAKYPFTAMTGVNTLFNALLNNKEFQQLDFSTLHLSAGGGMPvqqavAERWVKLTGQY--- 352
Cdd:PRK07868 671 GGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMP-----TGLWERVVEAFapa 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 353 -LLEGYGLTEC-APLVSVNPHDIdyhsGSIGLPVPST-----------EAKLVDDEDNEVPHGEPGElcvrgPQVMLGYW 419
Cdd:PRK07868 746 hVVEFFATTDGqAVLANVSGAKI----GSKGRPLPGAgrvelaaydpeHDLILEDDRGFVRRAEVNE-----VGVLLARA 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 420 QRP-DATDEIIK------DGWLHTGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAVGVPSGS 492
Cdd:PRK07868 817 RGPiDPTASVKRgvfapaDTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGG 896
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489956626 493 SGEAVKIFVVKKDPSLTEDALITFCRRQLTGYKvPKLVEFRDELPKS 539
Cdd:PRK07868 897 RQLAVAAVTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLS 942
|
|
| 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 489956626 392 VDDEDNE-VPHGEPGE-----LCVRGPQVmLGYWqrpdatdeiikdgwlhTGDIAVMDDEG---------FLRIVDRKKD 456
Cdd:cd05913 262 IDPETGEpVPPGEVGElvfttLTKEAMPL-IRYR----------------TRDITRLLPGPcpcgrthrrIDRITGRSDD 324
|
90 100
....*....|....*....|....
gi 489956626 457 MILVSGFNVYPNEIEDVVMQHSGV 480
Cdd:cd05913 325 MLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-545 |
5.02e-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: 49.19 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 50 TFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPlytprelehqlnDSGAAAIV--- 126
Cdd:cd05943 100 TWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSP------------DFGVPGVLdrf 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 127 --IVSNFAHTLEKVVEKTQVKHVI--LTRMGDQLSTAKGTLvnfVVKYvkrlVPKYHLPDAISFRRALH-AGYRMQYVKP 201
Cdd:cd05943 167 gqIEPKVLFAVDAYTYNGKRHDVRekVAELVKGLPSLLAVV---VVPY----TVAAGQPDLSKIAKALTlEDFLATGAAG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 202 EIVSEDLAF-----LQYTGGTTGVAKGAMLTHRNMLanLEQVNATygpLLH----PGKELvitalplyHIFALTM----N 268
Cdd:cd05943 240 ELEFEPLPFdhplyILYSSGTTGLPKCIVHGAGGTL--LQHLKEH---ILHcdlrPGDRL--------FYYTTCGwmmwN 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 269 CLL-FIELGGQNVLITNPrdiPGLVKELAKYPFTAMTGVNTL-----FNALLNNKEFQQ---LDFSTLH--LSAGGGMPV 337
Cdd:cd05943 307 WLVsGLAVGATIVLYDGS---PFYPDTNALWDLADEEGITVFgtsakYLDALEKAGLKPaetHDLSSLRtiLSTGSPLKP 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 338 QQAvaeRWV--KLTGQYLLEGY-GLTE-CAPLVSVNPhDIDYHSGSIGLPVPSTEAKLVDDEDNEVPhGEPGEL-CVRG- 411
Cdd:cd05943 384 ESF---DYVydHIKPDVLLASIsGGTDiISCFVGGNP-LLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELvCTKPf 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 412 PQVMLGYWQRPDATD------EIIKDGWLHtGDIAVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAA 485
Cdd:cd05943 459 PSMPVGFWNDPDGSRyraayfAKYPGVWAH-GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLV 537
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489956626 486 VGVPSGSSGEAVKIFVVKKDPSLTEDALI----TFCRRQLTGYKVPKLVEFRDELPKSNVGKIL 545
Cdd:cd05943 538 VGQEWKDGDERVILFVKLREGVELDDELRkrirSTIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
30-84 |
1.07e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 48.25 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489956626 30 EHSVR-RYADQPAFVNMGE-----VMTFRKLEERSRAFAAYLQEgLGLQKGDRVALMMPNL 84
Cdd:PRK03584 90 ENLLRhRRDDRPAIIFRGEdgprrELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNI 149
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
206-549 |
2.44e-05 |
|
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: 47.08 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 206 EDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGplLHPGKELVITALPLYHIFALTmnclLFIELGGQNVLITNP 285
Cdd:cd17654 118 ECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFN--ITSEDILFLTSPLTFDPSVVE----IFLSLSSGATLLIVP 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 286 RDIPGLVKELAKYPF-----TAMTGVNTLFNALLN--NKEFQQLDFSTLHLSAGGGMP-VQQAVAERWV-KLTGQYLLEG 356
Cdd:cd17654 192 TSVKVLPSKLADILFkrhriTVLQATPTLFRRFGSqsIKSTVLSATSSLRVLALGGEPfPSLVILSSWRgKGNRTRIFNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 357 YGLTECAPLVSVNPHDIDYHSGSIGLPVPSTEAKLVDDEDNEVPHGEPGELCVRGpQVMLGYWQRPDATdeiikdgWLHT 436
Cdd:cd17654 272 YGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRV-CILDDEVTVPKGT-------MRAT 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489956626 437 GDIaVMDDEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHSGVLEVAAvgvpSGSSGEAVKIFVVkkdpSLTEDALItF 516
Cdd:cd17654 344 GDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV----TLSDQQRLIAFIV----GESSSSRI-H 413
|
330 340 350
....*....|....*....|....*....|....*.
gi 489956626 517 CRRQLTG---YKVPKLVEFRDELPKSNVGKILRREL 549
Cdd:cd17654 414 KELQLTLlssHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
|