|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1-561 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 1215.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 1 MDKPWLSRYPSDVPETINPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALM 80
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAK 160
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 GTLVDFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKG 240
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 241 AYGPVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFH 320
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 321 ELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLN 400
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 401 YGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGK 480
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 481 VLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLAE 560
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAKVDN 559
|
.
gi 521099036 561 Q 561
Cdd:PRK08974 560 K 560
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1-554 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 862.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 1 MDKPWLSRYPSDVPETINPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALM 80
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPrAK 160
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLG-FK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 GTLVDFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKG 240
Cdd:PRK07059 159 GHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 241 AYGPVLREGRE----LVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNN 316
Cdd:PRK07059 239 WLQPAFEKKPRpdqlNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 317 EDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEG 396
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 NVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVA 476
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 477 LHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREEN 554
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGK 556
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1-552 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 782.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 1 MDKPWLSRYPSDVPETINPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALM 80
Cdd:PRK08751 3 QARPWLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAK 160
Cdd:PRK08751 83 MPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 GTLVDFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKG 240
Cdd:PRK08751 163 AALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 241 AYGPV--LREGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNED 318
Cdd:PRK08751 243 WLAGTgkLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 319 FHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNV 398
Cdd:PRK08751 323 FDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALH 478
Cdd:PRK08751 403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 479 GKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK08751 483 PGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1-559 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 779.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 1 MDKPWLSRYPSDVPETINPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALM 80
Cdd:PRK05677 2 IENFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAK 160
Cdd:PRK05677 82 LPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 GTLVDFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKG 240
Cdd:PRK05677 162 RLLINAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 241 AYGPVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFH 320
Cdd:PRK05677 242 LMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 321 ELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDlADYSGAIGLPVPSTEVRIVDDEGNVLN 400
Cdd:PRK05677 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 401 YGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGK 480
Cdd:PRK05677 401 LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 481 VLEVAAIGQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLA 559
Cdd:PRK05677 481 VLQCAAIGVPDEKSGEAIKVFVVvKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
5-552 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 702.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 5 WLSRYPSDVPETINPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNL 84
Cdd:PRK12492 6 WNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKGTLV 164
Cdd:PRK12492 86 LQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAKGWLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 165 DFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQyVKPFMSG-EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYG 243
Cdd:PRK12492 166 NTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLS-LKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 244 -------PVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNN 316
Cdd:PRK12492 245 qlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 317 EDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEG 396
Cdd:PRK12492 325 PGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 NVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVA 476
Cdd:PRK12492 405 NELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 477 LHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK12492 485 AHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-551 |
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: 685.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAIVIvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgAI 184
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 185 SMRKALHKGRRLQYvKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPvLREGRELVVTALPLYHVFA 264
Cdd:cd05936 105 SFTDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLED-LLEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 265 LTVNCLLFIEMGGSNLLITNPRDIpGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEK 344
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 345 WKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEA 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 425 TKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV- 503
Cdd:cd05936 342 TAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVl 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 504 KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05936 421 KEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-553 |
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: 541.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAIVIvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgai 184
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 185 smrkalhkgrrlqyvkpfmsgediAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGrELVVTALPLYHVFA 264
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPG-DVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 265 LTVNCLLFIEMGGSNLLITNpRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEK 344
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 345 WKKITGVHLLEGYGLTECSPLVTGNPYDLAD-YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPE 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPGErRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 424 ATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV 503
Cdd:COG0318 315 ATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 521099036 504 KRD-PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:COG0318 394 LRPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-560 |
3.27e-166 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 484.50 E-value: 3.27e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 2 DKPWLSRYPSDVPETINPDQyLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMM 81
Cdd:PRK05605 12 DKPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLR-ALGVRPGDRVAIVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 82 PNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKG 161
Cdd:PRK05605 90 PNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 162 TLVDFVVKYVKGMVPKYD--LPGAISMRKALHKGRRLQYVK---PFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVL 236
Cdd:PRK05605 170 LALRLPIPALRKARAALTgpAPGTVPWETLVDAAIGGDGSDvshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 237 QAKgAYGPVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPrDIPGFVKELQKHPFTAITGVNTLFNALVNN 316
Cdd:PRK05605 250 QGK-AWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 317 EDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVD--D 394
Cdd:PRK05605 328 AEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 395 EGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDV 474
Cdd:PRK05605 408 PDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 475 VALHGKVLEVAAIGQPHEVSGE-VVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEeVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
....*..
gi 521099036 554 NDAQLAE 560
Cdd:PRK05605 567 LLEKLGA 573
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
23-553 |
1.39e-145 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 429.71 E-value: 1.39e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 23 LSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 103 NVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANT-QVKHVVL--TSLGQMLPRAKGTLVDFVvkyvkgmvpkyd 179
Cdd:PRK07656 84 PLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVIceTEEDDPHTEKMKTFTDFL------------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 180 lpgaismrkALHKGRrlqYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVlQAKGAYGPVLREGRELVVtaLPL 259
Cdd:PRK07656 152 ---------AAGDPA---ERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNA-ADWAEYLGLTEGDRYLAA--NPF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 260 YHVFALTVnCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQR 339
Cdd:PRK07656 217 FHVFGYKA-GVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 340 AVAEKWKKITGV-HLLEGYGLTECSPLVTGNPYD--LADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQ 416
Cdd:PRK07656 296 ALLERFESELGVdIVLTGYGLSEASGVTTFNRLDddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 417 GYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE 496
Cdd:PRK07656 376 GYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 497 VVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK07656 456 VGKAYVVlKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-564 |
5.96e-143 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 424.83 E-value: 5.96e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 1 MDKPWLSRYPSDVPETINPDQYlSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALM 80
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTISYDIQ-PLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQ-KLGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAK 160
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 GTLVDFVVKYVKGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQA-K 239
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGvQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 240 GAYGPVlrEGRELVVTALPLYHVFALTVNCLLFIeMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDF 319
Cdd:PRK06710 241 WLYNCK--EGEEVVLGVLPFFHVYGMTAVMNLSI-MQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 320 HELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDE-GNV 398
Cdd:PRK06710 318 KEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLEtGEA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALH 478
Cdd:PRK06710 398 LPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEH 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 479 GKVLEVAAIGQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREEndaq 557
Cdd:PRK06710 477 EKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE---- 552
|
....*..
gi 521099036 558 laEQKKS 564
Cdd:PRK06710 553 --EKRKN 557
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-552 |
1.50e-138 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 411.89 E-value: 1.50e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 20 DQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGM 99
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 100 IAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQ-VKHVVLTSlgqmlPRAKGTLVDFVVKYVkgmvpky 178
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEG-----DGPAAPLAPEVGEYE------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 179 dlpgaismrkALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVTalP 258
Cdd:PRK06187 150 ----------ELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK-LSRDDVYLVIV--P 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 259 LYHVFALTVnCLLFIEMGGSNLLItnPRDIPGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAV 337
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVIP--RRFDPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 338 QRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYD-----LADYSGAIGLPVPSTEVRIVDDEGNVL--NYGQTGELQVR 410
Cdd:PRK06187 294 PPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEdqlpgQWTKRRSAGRPLPGVEARIVDDDGDELppDGGEVGEIIVR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK06187 374 GPWLMQGYWNRPEATAETI-DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 491 HEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK06187 453 DEKWGERPVAVVVlKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-547 |
7.86e-130 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 386.58 E-value: 7.86e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 29 FEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 109 TPRELEHQLNDADARAIVivsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrk 188
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 189 alhkgrrlqyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAkGAYGPVLREGRELVVtaLPLYHVFALTVN 268
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNA-LAALDLGPDDVLLVV--APLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 CLLFIEMGGSNLLITNPRdiPG-FVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKK 347
Cdd:cd17631 158 TLPTLLRGGTVVILRKFD--PEtVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ItGVHLLEGYGLTECSPLVTGNPYDLAD-YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATK 426
Cdd:cd17631 236 R-GVKFVQGYGMTETSPGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 427 EVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD 506
Cdd:cd17631 315 AAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 521099036 507 PS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:cd17631 394 GAeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
29-462 |
1.77e-128 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 382.43 E-value: 1.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 29 FEQSVHKYADQPAFINMGSV-MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRrLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 108 YTPRELEHQLNDADARAIVIVSNFanTLEQIVANTQ-VKHVVLTSLGQMLPRAKGTLVDFVVKYVKGmvpkydlpgaism 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPADV------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREG-RELVVTALPLYHVFAL 265
Cdd:pfam00501 145 ---------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 266 TVNCLLFIEMGGSNLLI--TNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAE 343
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKKITGVHLLEGYGLTECSPLVTGNPYDLAD--YSGAIGLPVPSTEVRIVDDE-GNVLNYGQTGELQVRGPQVMQGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 521099036 421 RPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS 462
Cdd:pfam00501 376 DPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
12-559 |
8.58e-126 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 380.07 E-value: 8.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 12 DVPETinpdqylSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVAL 91
Cdd:PRK08314 6 TLPET-------SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 92 FGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKG-TLVDFVVky 170
Cdd:PRK08314 79 YAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEiAVPAWLR-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 171 VKGMVPKYDLPGAISMRKALHKGRRLqyvKPFMSG-EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAkGAYGPVLREG 249
Cdd:PRK08314 157 AEPPLQALAPGGVVAWKEALAAGLAP---PPHTAGpDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS-VLWSNSTPES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 250 RELVVtaLPLYHVFALtVNCLLF-IEMGGSNLLITN-PRDIPGfvKELQKHPFTAITGVNTLFNALVNNEDFHELNFANM 327
Cdd:PRK08314 233 VVLAV--LPLFHVTGM-VHSMNApIYAGATVVLMPRwDREAAA--RLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 328 KLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDlADYSGAIGLPVPSTEVRIVD-DEGNVLNYGQTGE 406
Cdd:PRK08314 308 RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 407 LQVRGPQVMQGYWQRPEATKEVINE-EG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLE 483
Cdd:PRK08314 387 IVVHGPQVFKGYWNRPEATAEAFIEiDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQE 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 484 VAAIGQPHEVSGEVVKIYVVKRDPS---LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLA 559
Cdd:PRK08314 467 ACVIATPDPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAA 545
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
41-546 |
7.92e-124 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 372.70 E-value: 7.92e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 41 AFIN--MGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLN 118
Cdd:cd05911 1 AQIDadTGKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 119 DADARAIVI-VSNFANTLEQIVANTQVKHV-VLTSLGQMLPRAkGTLVDFVVKYvkgmvPKYDLPgaismrkaLHKGRrl 196
Cdd:cd05911 80 ISKPKVIFTdPDGLEKVKEAAKELGPKDKIiVLDDKPDGVLSI-EDLLSPTLGE-----EDEDLP--------PPLKD-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 197 qyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYgPVLREGRELVVTALPLYHVFAL--TVNCLLFie 274
Cdd:cd05911 144 -------GKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFL-YGNDGSNDVILGFLPLYHIYGLftTLASLLN-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 275 mgGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKK-ITGVHL 353
Cdd:cd05911 214 --GATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKrFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 354 LEGYGLTECSPLVTGNPyDLADYSGAIGLPVPSTEVRIVDDEGN-VLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEE 432
Cdd:cd05911 292 KQGYGMTETGGILTVNP-DGDDKPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 433 GWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-PSLTK 511
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPgEKLTE 450
|
490 500 510
....*....|....*....|....*....|....*...
gi 521099036 512 DELITHCRKHLTGYKvpKL---IEFREELPKTNVGKIL 546
Cdd:cd05911 451 KEVKDYVAKKVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-546 |
3.89e-114 |
|
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: 342.73 E-value: 3.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 207 DIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGrELVVTALPLYHVFALtvNCLLFIEMGGSNLLITNPR 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEG-DVFLSTLPLFHIGGL--FGLLGALLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLV 366
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 367 T-GNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDE 445
Cdd:cd04433 156 AtGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-EDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 446 NGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTKDELITHCRKHLTG 524
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 521099036 525 YKVPKLIEFREELPKTNVGKIL 546
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
33-550 |
1.25e-107 |
|
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: 331.89 E-value: 1.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 33 VHKYADQPAFIN--MGSVMTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTP 110
Cdd:cd05904 15 ASAHPSRPALIDaaTGRALTYAELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 111 RELEHQLNDADARAIVIVSNFANTLEQIVANtqvkhVVLtslgqmlprakgtlvdfvvkyvkgmVPKYDLPGAiSMRKAL 190
Cdd:cd05904 94 AEIAKQVKDSGAKLAFTTAELAEKLASLALP-----VVL-------------------------LDSAEFDSL-SFSDLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 191 HKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVL-REGRELVVtaLPLYHVFALTV-- 267
Cdd:cd05904 143 FEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdSEDVFLCV--LPMFHIYGLSSfa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 268 NCLLFIemgGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWK- 346
Cdd:cd05904 221 LGLLRL---GATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRa 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 347 KITGVHLLEGYGLTECSPLVT--GNPYDLADYSGAIGLPVPSTEVRIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPE 423
Cdd:cd05904 298 KFPNVDLGQGYGMTESTGVVAmcFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 424 ATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV 503
Cdd:cd05904 378 ATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 504 KR-DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05904 458 RKpGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-545 |
1.51e-106 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 330.85 E-value: 1.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 5 WLSRYPSDVPETIN-PDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPN 83
Cdd:PRK06178 14 QQAAWPAGIPREPEyPHGERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLR-QRGVGAGDRVAVFLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 84 LLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKGTL 163
Cdd:PRK06178 93 CPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAEPTLP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 164 VDFVVKyvkgmVPKYDLPGAISMRKALHkGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANvlqAKGAYG 243
Cdd:PRK06178 173 LPDSLR-----APRLAAAGAIDLLPALR-ACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYT---AAAAYA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 244 PVLREGRELVVTA-LPLYHVfALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHEL 322
Cdd:PRK06178 244 VAVVGGEDSVFLSfLPEFWI-AGENFGLLFPLFSGATLVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 323 NFANMKLSvgggMAVQ------RAVAEKWKKITGVHLLEG-YGLTE---CSPLVTG---NPYDLADYSGAIGLPVPSTEV 389
Cdd:PRK06178 323 DLSSLRQV----RVVSfvkklnPDYRQRWRALTGSVLAEAaWGMTEthtCDTFTAGfqdDDFDLLSQPVFVGLPVPGTEF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 390 RIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYP 468
Cdd:PRK06178 399 KICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFP 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 469 NEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKlIEFREELPKTNVGKI 545
Cdd:PRK06178 478 SEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQlKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKV 554
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-564 |
2.67e-100 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 312.56 E-value: 2.67e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIVANTQVKHVV-LTSLGQMLPRAKGTLVDfvvkyvkgmvpkydlpgaismrkalhkgrrl 196
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVIsITSLKEIEDRKIDNFVE------------------------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 197 qyvkpfmSGEDIAFLQ-YTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLReGRELVVTALPLYHVFALTVNCLLFIEM 275
Cdd:PRK06839 146 -------KNESASFIIcYTSGTTGKPKGAVLTQENMFWNALNNTFAID--LT-MHDRSIVLLPLFHIGGIGLFAFPTLFA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSnLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGG----MAVQRAVAEKwkkitGV 351
Cdd:PRK06839 216 GGV-IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 352 HLLEGYGLTECSPLV-TGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVIn 430
Cdd:PRK06839 290 LFGQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-PSL 509
Cdd:PRK06839 369 QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSsSVL 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 510 TKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRrvlreendAQLAEQKKS 564
Cdd:PRK06839 449 IEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQK--------AQLVNQLKS 495
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-552 |
5.22e-99 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 311.28 E-value: 5.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 33 VHKYADQPAFI-----NMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:COG0365 19 AEGRGDKVALIwegedGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 108 YTPRELEHQLNDADARAIVIVSNFAN---------TLEQIVANT-QVKHVVLtslgqmlprakgtlvdfvvkyVKGMVPK 177
Cdd:COG0365 98 FGAEALADRIEDAEAKVLITADGGLRggkvidlkeKVDEALEELpSLEHVIV---------------------VGRTGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 178 YDLPGAISMRKAL-HKGRRLQYVKpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVL-QAKGAYGpvLREGrELV-- 253
Cdd:COG0365 157 VPMEGDLDWDELLaAASAEFEPEP--TDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAtTAKYVLD--LKPG-DVFwc 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 254 ------VTALPLYHVFALTVNCLLFIeMGGSnlliTNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFH--ELNFA 325
Cdd:COG0365 232 tadigwATGHSYIVYGPLLNGATVVL-YEGR----PDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPlkKYDLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 326 NMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTG 405
Cdd:COG0365 307 SLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 406 ELQVRGPQ--VMQGYWQRPEATKEVI--NEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKV 481
Cdd:COG0365 387 ELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAV 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 482 LEVAAIGQPHEVSGEVVKIYVVKRD---PS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:COG0365 467 AEAAVVGVPDEIRGQVVKAFVVLKPgvePSdELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRK 541
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-552 |
3.11e-98 |
|
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: 307.32 E-value: 3.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 37 ADQPAFINMGSVM--TFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELE 114
Cdd:cd05926 1 PDAPALVVPGSTPalTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 115 HQLNDADARAIVivsnfantleqivantqVKHVVLTSLGQMLPRAKGTLVDFVVKYVKGMVpkYDLPGAISMRKALHKGR 194
Cdd:cd05926 80 FYLADLGSKLVL-----------------TPKGELGPASRAASKLGLAILELALDVGVLIR--APSAESLSNLLADKKNA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 195 RLQyvkPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAY--GPvlrEGRELVVtaLPLYHVFALTVNCLLF 272
Cdd:cd05926 141 KSE---GVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYklTP---DDRTLVV--MPLFHVHGLVASLLST 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 273 IEMGGSnlLITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVNNED------FHELNFANmklSVGGGMAVqrAVAEKW 345
Cdd:cd05926 213 LAAGGS--VVLPPRfSASTFWPDVRDYNATWYTAVPTIHQILLNRPEpnpespPPKLRFIR---SCSASLPP--AVLEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 346 KKITGVHLLEGYGLTECSPLVTGNPYDLADYS-GAIGLPVpSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEA 424
Cdd:cd05926 286 EATFGAPVLEAYGMTEAAHQMTSNPLPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 425 TKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVK 504
Cdd:cd05926 365 NAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 521099036 505 R-DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05926 445 ReGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-550 |
1.75e-97 |
|
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: 303.25 E-value: 1.75e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIV 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 SNFantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgEDI 208
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvlREGRELVVTALPLYHVfALTVNCLLFIEMGGSNLLITNPRDI 288
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG---LTPSDVILACLPLFHV-TGFVGSLNTAVYVGGTYVLMARWDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 289 PGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTG 368
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 369 NPYdLADYSGAIGLPVPSTEVRIVDDE-GNVLNYGQTGELQVRGPQVMQGYWQRPEATKEV---INEEGWLSTGDIVRFD 444
Cdd:cd05935 243 NPP-LRPKLQCLGIP*FGVDARVIDIEtGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 445 ENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDP---SLTKDELITHCRKH 521
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....*....
gi 521099036 522 LTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
24-553 |
1.35e-95 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 301.08 E-value: 1.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 104 VNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLtSLGQMLPRAKGTLVDFVVKYVKGMVPKYDlpga 183
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLIL-SLVLGGREAPGGWLDFADWAEAGSVAEPD---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 184 ismrkalhkgrrlqyvkPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQA--KGAYGPvlregRELVVTALPLYH 261
Cdd:PRK08316 166 -----------------VELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCivAGDMSA-----DDIPLHALPLYH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 262 VFALTVNCLLFIEMGGSNLLITNPRdiPGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRA 340
Cdd:PRK08316 224 CAQLDVFLGPYLYVGATNVILDAPD--PELILRTiEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 V-AEKWKKITGVHLLEGYGLTECSPLVTG-NPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGY 418
Cdd:PRK08316 302 VlKELRERLPGLRFYNCYGQTEIAPLATVlGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE-V 497
Cdd:PRK08316 382 WDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEaV 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 498 VKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK08316 461 TAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-552 |
2.00e-92 |
|
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: 290.35 E-value: 2.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVivsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlq 197
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfmsgeDIAFLQYTGGTTGVAKGAILTHRNMVANV--LQAKGAYGPvlregRELVVTALPLYHVFAL--TVNCLLFI 273
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVraLVDAWRWTE-----DDVLLHVLPLHHVHGLvnALLCPLFA 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 274 emGGSNLLITNPRDIPGFVKELQKhPFTAITGVNTLFNALVNNEDFH--------ELNFANMKLSVGGGMAVQRAVAEKW 345
Cdd:cd05941 156 --GASVEFLPKFDPKEVAISRLMP-SITVFMGVPTIYTRLLQYYEAHftdpqfarAAAAERLRLMVSGSAALPVPTLEEW 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 346 KKITGVHLLEGYGLTECSpLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGN-VLNYGQTGELQVRGPQVMQGYWQRPEA 424
Cdd:cd05941 233 EAITGHTLLERYGMTEIG-MALSNPLDGERRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEA 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 425 TKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS-GFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV 503
Cdd:cd05941 312 TKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVV 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 521099036 504 KRD--PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05941 392 LRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
4-552 |
1.96e-90 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 291.09 E-value: 1.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 4 PWLSRypsDVPEtinpdqylSLVEMFEQSVHKYADQPA---FINMGS-----VMTFRKLEER-SRAfaAYLQNELKLKKG 74
Cdd:PRK07529 17 PLAAR---DLPA--------STYELLSRAAARHPDAPAlsfLLDADPldrpeTWTYAELLADvTRT--ANLLHSLGVGPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 75 DRVALMMPNLLQYPVALFGILRAGmIAVNVNPLYTPRELEHQLNDADARAIVIVSNF-----ANTLEQIVAN-TQVKHVV 148
Cdd:PRK07529 84 DVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAAlPELRTVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 149 LTSLGQMLPRAKGTLVDFVvkYVKGMVPKYDLPGAIsmrkALHKGRRLQYVKPFmSGEDIAFLQYTGGTTGVAKGAILTH 228
Cdd:PRK07529 163 EVDLARYLPGPKRLAVPLI--RRKAHARILDFDAEL----ARQPGDRLFSGRPI-GPDDVAAYFHTGGTTGMPKLAQHTH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 229 RNMVANVLQAKGAYGpvLREGrELVVTALPLYHVFALTVNCLLFIEMGGSNLLIT-----NPRDIPGFVKELQKHPFTAI 303
Cdd:PRK07529 236 GNEVANAWLGALLLG--LGPG-DTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrGPGVIANFWKIVERYRINFL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 304 TGVNTLFNAL----VNNEDFHELNFAnmklsVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGA 379
Cdd:PRK07529 313 SGVPTVYAALlqvpVDGHDISSLRYA-----LCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGS 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 380 IGLPVPSTEVRIV--DDEGNVLN---YGQTGELQVRGPQVMQGYwQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDR 454
Cdd:PRK07529 388 VGLRLPYQRVRVVilDDAGRYLRdcaVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 455 KKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYV-VKRDPSLTKDELITHCRKHLTG-YKVPKLIE 532
Cdd:PRK07529 467 AKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHVR 546
|
570 580
....*....|....*....|
gi 521099036 533 FREELPKTNVGKILRRVLRE 552
Cdd:PRK07529 547 ILDALPKTAVGKIFKPALRR 566
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
14-489 |
2.02e-88 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 284.69 E-value: 2.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 14 PETINPDQYLSLVEMFEQSVHKYADQPAFINMGS----VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPV 89
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 90 ALFGILRAGmiAVNVnPLY---TPRELEHQLNDADARaIVIVSNF--ANTLEQIVANT-QVKHVVLtslgqMLPRAKgtl 163
Cdd:COG1022 81 ADLAILAAG--AVTV-PIYptsSAEEVAYILNDSGAK-VLFVEDQeqLDKLLEVRDELpSLRHIVV-----LDPRGL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 164 vdfvvkyvkgmvpkYDLPGAISMRKALHKGRRLQYVKPF------MSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQ 237
Cdd:COG1022 149 --------------RDDPRLLSLDELLALGREVADPAELearraaVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 238 AKGAYGpvLREGrELVVTALPLYHVFALTVnCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAI--------TGVNT- 308
Cdd:COG1022 215 LLERLP--LGPG-DRTLSFLPLAHVFERTV-SYYALAAGATVAFAESPDTLAEDLREVKPTFMLAVprvwekvyAGIQAk 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 309 ----------LFNALVNN-EDFHELNFANmkLSVGGGMAVQRAVAE-----KWKKITG---------------------- 350
Cdd:COG1022 291 aeeagglkrkLFRWALAVgRRYARARLAG--KSPSLLLRLKHALADklvfsKLREALGgrlrfavsggaalgpelarffr 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 351 ---VHLLEGYGLTECSPLVTGNPYDLADYsGAIGLPVPSTEVRIVDDegnvlnygqtGELQVRGPQVMQGYWQRPEATKE 427
Cdd:COG1022 369 algIPVLEGYGLTETSPVITVNRPGDNRI-GTVGPPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 428 VINEEGWLSTGDIVRFDENGMIYIVDRKKDMI-LVSGFNVYPNEIEDVVALHGKVLEVAAIGQ 489
Cdd:COG1022 438 AFDADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVGD 500
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
36-551 |
4.49e-88 |
|
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: 281.18 E-value: 4.49e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 36 YADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:cd05959 17 RGDKTAFIDDAGSLTYAELEAEARRVAGALR-ALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARAIVIVSNFANTLEQIV--ANTQVKHVVLTSlGQMLPRAKGTLVDFVvkyvkgmvpkydlPGAISMRKALHKG 193
Cdd:cd05959 96 YLEDSRARVVVVSGELAPVLAAALtkSEHTLVVLIVSG-GAGPEAGALLLAELV-------------AAEAEQLKPAATH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 194 RrlqyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNM-VANVLQAKGAYGpvLREGrELVVTALPLYHVFALTvNCLLF 272
Cdd:cd05959 162 A-----------DDPAFWLYSSGSTGRPKGVVHLHADIyWTAELYARNVLG--IRED-DVCFSAAKLFFAYGLG-NSLTF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 273 -IEMGGSNLLITNpRDIPGFV-KELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITG 350
Cdd:cd05959 227 pLSVGATTVLMPE-RPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 351 VHLLEGYGLTECSPLVTGNPYDLADYsGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVIn 430
Cdd:cd05959 306 LDILDGIGSTEMLHIFLSNRPGRVRY-GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR----D 506
Cdd:cd05959 384 QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyeD 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 521099036 507 PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05959 464 SEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-551 |
6.58e-87 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 275.32 E-value: 6.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIvs 129
Cdd:cd05934 5 TYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgeDIA 209
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMV-ANVLQAKGAygpVLREGrELVVTALPLYHVFALTVNCLLFIEMGGSNLLItnPRDI 288
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTfAGYYSARRF---GLGED-DVYLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 289 P-GFVKELQKHpftaitGVnTLFNAL-----------VNNEDfhelnfANMKLSVGGGMAVQRAVAEKWKKITGVHLLEG 356
Cdd:cd05934 159 AsRFWSDVRRY------GA-TVTNYLgamlsyllaqpPSPDD------RAHRLRAAYGAPNPPELHEEFEERFGVRLLEG 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVTGnPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVR---GPQVMQGYWQRPEATKEVInEEG 433
Cdd:cd05934 226 YGMTETIVGVIG-PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNG 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDP-SLTKD 512
Cdd:cd05934 304 WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGeTLDPE 383
|
490 500 510
....*....|....*....|....*....|....*....
gi 521099036 513 ELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05934 384 ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-562 |
1.40e-84 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 273.57 E-value: 1.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFI--NMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK12583 22 DAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAIVIV-----SNFANTLEQIVANtqvkhVVLTSLGQM----LPRAKGtLVDFVVKYVKGMV 175
Cdd:PRK12583 101 NPAYRASELEYALGQSGVRWVICAdafktSDYHAMLQELLPG-----LAEGQPGALacerLPELRG-VVSLAPAPPPGFL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 176 PKYDLpgaISMRKALhKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVt 255
Cdd:PRK12583 175 AWHEL---QARGETV-SREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTEHDRLCV- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 256 ALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGM 335
Cdd:PRK12583 248 PVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 336 AVQRAVAEKwkKITGVHLLE---GYGLTECSPLV--TGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVR 410
Cdd:PRK12583 328 PCPIEVMRR--VMDEMHMAEvqiAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVP 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 491 HEVSGEVVKIYVVKR-DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLAEQK 562
Cdd:PRK12583 486 DEKYGEEIVAWVRLHpGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIEELALPV 558
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-553 |
1.01e-82 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 267.13 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMM----PNLLQYpvalFGILRAGMIAVNVNPLYTPRELEHQLNDAD 121
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 122 ARAIVIVSNFANTLEQIVANTQVKHVvlTSL-----GQMLPRAKGTLVDFVVkyvkgmVPKydlpgaismrkalhkgrrl 196
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGAPHV--ETLdadgtGSLLEAAAAAPDDFET------VPR------------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 197 qyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVvTALPLYHVFALTV--NCLLFie 274
Cdd:PRK07514 154 -------GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWR--FTPDDVLI-HALPIFHTHGLFVatNVALL-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 275 MGGSnlLITNPRDIPGFVKELQKHPfTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLL 354
Cdd:PRK07514 222 AGAS--MIFLPKFDPDAVLALMPRA-TVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 355 EGYGLTEcSPLVTGNPYDLADYSGAIGLPVPSTEVRIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEG 433
Cdd:PRK07514 299 ERYGMTE-TNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVV-ALHGkVLEVAAIGQPHEVSGEVVKIYVVKR-DPSLTK 511
Cdd:PRK07514 378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIdELPG-VVESAVIGVPHPDFGEGVTAVVVPKpGAALDE 456
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 521099036 512 DELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK07514 457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-552 |
1.27e-82 |
|
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: 267.19 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVAN-TQVKHVVLTSLGQMLPRAkgtlvdfvvkyvkgmvpkyDLPGAISMRKALHKGRRLqYVKPFMSGEDI 208
Cdd:cd12119 106 DFLPLLEAIAPRlPTVEHVVVMTDDAAMPEP-------------------AGVGVLAYEELLAAESPE-YDWPDFDENTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRnmvANVLQAKGAYGP--VLREGRELVVTALPLYHVFALtvnCLLFIE-MGGSNLLITNP 285
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHR---SLVLHAMAALLTdgLGLSESDVVLPVVPMFHVNAW---GLPYAAaMVGAKLVLPGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHLLEGYGLTECSP 364
Cdd:cd12119 240 YLDPASLAELiEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 365 LVT---------GNPYDL-ADYSGAIGLPVPSTEVRIVDDEGNVL--NYGQTGELQVRGPQVMQGYWQRPEATKEvINEE 432
Cdd:cd12119 319 LGTvarppsehsNLSEDEqLALRAKQGRPVPGVELRIVDDDGRELpwDGKAVGELQVRGPWVTKSYYKNDEESEA-LTED 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 433 GWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTK 511
Cdd:cd12119 398 GWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAtVTA 477
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 521099036 512 DELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-561 |
5.65e-82 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 266.68 E-value: 5.65e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPA--FINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPN-----LLQYPVAlfgilRAGM 99
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNvpewvLTQFATA-----KIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 100 IAVNVNPLYTPRELEHQLNDADARAIVIV-----SNFANTLEQIV---ANTQ-----------VKHVVltSLGQMLPRak 160
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAAdgfkdSDYVAMLYELApelATCEpgqlqsarlpeLRRVI--FLGDEKHP-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 161 gtlvdfvvkyvkGMvpkYDLPGAISMRKALHKGRrLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVAN---VLQ 237
Cdd:PRK08315 170 ------------GM---LNFDELLALGRAVDDAE-LAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNgyfIGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 238 AKGaYGPVLRegrelVVTALPLYHVF--------ALTVncllfiemgGSNLLITNPRDIPGFV-KELQKHPFTAITGVNT 308
Cdd:PRK08315 234 AMK-LTEEDR-----LCIPVPLYHCFgmvlgnlaCVTH---------GATMVYPGEGFDPLATlAAVEEERCTALYGVPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 309 LFNALVNNEDFHELNFANMKlsvGGGMA-------VQRAVAEKwkkitgVHLLE---GYGLTECSPLVT----GNPYDLA 374
Cdd:PRK08315 299 MFIAELDHPDFARFDLSSLR---TGIMAgspcpieVMKRVIDK------MHMSEvtiAYGMTETSPVSTqtrtDDPLEKR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 375 dySGAIGLPVPSTEVRIVDDE-GNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVD 453
Cdd:PRK08315 370 --VTTVGRALPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 454 RKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDP-SLTKDELITHCRKHLTGYKVPKLIE 532
Cdd:PRK08315 448 RIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGaTLTEEDVRDFCRGKIAHYKIPRYIR 527
|
570 580
....*....|....*....|....*....
gi 521099036 533 FREELPKTNVGKILRRVLREENDAQLAEQ 561
Cdd:PRK08315 528 FVDEFPMTVTGKIQKFKMREMMIEELGLQ 556
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-551 |
2.88e-81 |
|
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: 261.12 E-value: 2.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd05972 2 SFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgEDIA 209
Cdd:cd05972 81 ----------------------------------------------------------------------------EDPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTALP--LYHVFALTVNCLLfieMGGSNLLITNPR- 286
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLG--LRPDDIHWNIADPgwAKGAWSSFFGPWL---LGATVFVYEGPRf 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIPGFVKELQKHPFTAITGVNTLFNALVNnEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSpLV 366
Cdd:cd05972 160 DAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETG-LT 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 367 TGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVR--GPQVMQGYWQRPEATKEVINEeGWLSTGDIVRFD 444
Cdd:cd05972 238 VGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASIRG-DYYLTGDRAYRD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 445 ENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-----KRDPSLtKDELITHCR 519
Cdd:cd05972 317 EDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVltsgyEPSEEL-AEELQGHVK 395
|
490 500 510
....*....|....*....|....*....|..
gi 521099036 520 KHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05972 396 KVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
35-553 |
1.93e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 261.84 E-value: 1.93e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 35 KYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELE 114
Cdd:PRK06188 24 RYPDRPALVLGDTRLTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 115 HQLNDADARAIVIVSN-FANTLEQIVAN-TQVKHVVltSLGqmlprAKGTLVDFvvkyvkgmvpkydLPGAISMRKAlhk 192
Cdd:PRK06188 103 YVLEDAGISTLIVDPApFVERALALLARvPSLKHVL--TLG-----PVPDGVDL-------------LAAAAKFGPA--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 193 grrlqYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVA-NVLQAKGAYGPvlREGRELVVTalPLYHVFALTVNCLL 271
Cdd:PRK06188 160 -----PLVAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIATmAQIQLAEWEWP--ADPRFLMCT--PLSHAGGAFFLPTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 272 fieMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGG--MAVQRaVAEKWKKIT 349
Cdd:PRK06188 231 ---LRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGAspMSPVR-LAEAIERFG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 350 GVhLLEGYGLTECSPLVT-----GNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEA 424
Cdd:PRK06188 307 PI-FAQYYGQTEAPMVITylrkrDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 425 TKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVK 504
Cdd:PRK06188 386 TAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 521099036 505 R-DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK06188 465 RpGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
9-559 |
3.76e-79 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 258.76 E-value: 3.76e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 9 YPSDVPEtINPDQYLSLVEMFEQSVHKYADQPAFIN--MGSVMTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQ 86
Cdd:PLN02246 10 FRSKLPD-IYIPNHLPLHDYCFERLSEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 87 YPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSlgqmlprakgtlvdf 166
Cdd:PLN02246 88 FVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDD--------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 167 vvkYVKGMVPKYDLPGAismrkalhKGRRLQYVKpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVL 246
Cdd:PLN02246 153 ---PPEGCLHFSELTQA--------DENELPEVE--ISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 247 REGRELVV-TALPLYHVFALtvNCLLFIEM-GGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNF 324
Cdd:PLN02246 220 YFHSDDVIlCVLPMFHIYSL--NSVLLCGLrVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 325 ANMKLSVGG----GMAVQRAVAEKwkkITGVHLLEGYGLTECSPLVT------GNPYDLAdySGAIGLPVPSTEVRIVD- 393
Cdd:PLN02246 298 SSIRMVLSGaaplGKELEDAFRAK---LPNAVLGQGYGMTEAGPVLAmclafaKEPFPVK--SGSCGTVVRNAELKIVDp 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 394 DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIED 473
Cdd:PLN02246 373 ETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEA 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 474 VVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRe 552
Cdd:PLN02246 453 LLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSeITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR- 531
|
....*..
gi 521099036 553 endAQLA 559
Cdd:PLN02246 532 ---AKLA 535
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-551 |
5.43e-76 |
|
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: 247.38 E-value: 5.43e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 39 QPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLN 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRN-LGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 119 DADARAIVIvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqy 198
Cdd:cd05919 80 DCEARLVVT----------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 199 vkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANV-LQAKGAYGpvLREGrELVVTALPLYHVFALTvNCLLF-IEMG 276
Cdd:cd05919 89 -----SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALG--LTPG-DRVFSSAKMFFGYGLG-NSLWFpLAVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 277 GSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEG 356
Cdd:cd05919 160 ASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVTGNPYDLADYsGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEeGWLS 436
Cdd:cd05919 240 IGATEVGHIFLSNRPGAWRL-GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG-GWYR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 437 TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELI- 515
Cdd:cd05919 318 TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLAr 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 521099036 516 ---THCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05919 398 dihRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
211-551 |
5.29e-75 |
|
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: 242.18 E-value: 5.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 211 LQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVtALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPG 290
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG--LTEQDRLCI-PVPLFHCFGSVLGVLACLTHGATMVFPSPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 291 FVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGG----MAVQRAVAEKWKkITGVHLleGYGLTECSPLV 366
Cdd:cd05917 84 VLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGapcpPELMKRVIEVMN-MKDVTI--AYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 367 T-GNPYDLADYS-GAIGLPVPSTEVRIVDDEGN-VLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRF 443
Cdd:cd05917 161 TqTRTDDSIEKRvNTVGRIMPHTEAKIVDPEGGiVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 444 DENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-PSLTKDELITHCRKHL 522
Cdd:cd05917 241 DEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEgAELTEEDIKAYCKGKI 320
|
330 340
....*....|....*....|....*....
gi 521099036 523 TGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05917 321 AHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-552 |
1.45e-72 |
|
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: 237.63 E-value: 1.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADaraivivs 129
Cdd:cd05912 3 TFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvkhvvltslgqmlprakgtlvdfvVKYvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgEDIA 209
Cdd:cd05912 74 --------------------------------------VKL-----------------------------------DDIA 80
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVvtALPLYHVFALTVncLLFIEMGGSNLLITNPRDIP 289
Cdd:cd05912 81 TIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLG-LTEDDNWLC--ALPLFHISGLSI--LMRSVIYGMTVYLVDKFDAE 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 290 GFVKELQKHPFTAITGVNTLFNAL--VNNEDFHElNFANMKLsvGGGMAVQRAVAEKWKKitGVHLLEGYGLTE-CSPLV 366
Cdd:cd05912 156 QVLHLINSGKVTIISVVPTMLQRLleILGEGYPN-NLRCILL--GGGPAPKPLLEQCKEK--GIPVYQSYGMTEtCSQIV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 367 TGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVlnyGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDEN 446
Cdd:cd05912 231 TLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 447 GMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPsLTKDELITHCRKHLTGYK 526
Cdd:cd05912 307 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYK 385
|
490 500
....*....|....*....|....*.
gi 521099036 527 VPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05912 386 VPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
49-489 |
1.94e-72 |
|
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: 238.65 E-value: 1.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLY---TPRELEHQLNDADARAI 125
Cdd:cd05907 6 ITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 vIVSNfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsG 205
Cdd:cd05907 82 -FVED--------------------------------------------------------------------------P 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPvlrEGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNP 285
Cdd:cd05907 87 DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA---TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSA 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKELQKHPFTAITGV-NTLFNALVNNED-------FHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHLLEGY 357
Cdd:cd05907 164 ETLLDDLSEVRPTVFLAVPRVwEKVYAAIKVKAVpglkrklFDLAVGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGY 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 358 GLTECSPLVTGNPYDLADYsGAIGLPVPSTEVRIVDDegnvlnygqtGELQVRGPQVMQGYWQRPEATKEVINEEGWLST 437
Cdd:cd05907 243 GLTETSAVVTLNPPGDNRI-GTVGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHT 311
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 521099036 438 GDIVRFDENGMIYIVDRKKDMILVS-GFNVYPNEIEDVVALHGKVLEVAAIGQ 489
Cdd:cd05907 312 GDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIGD 364
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-547 |
3.13e-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: 234.32 E-value: 3.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 207 DIAFLQYTGGTTGVAKGAILTHRNMVAnVLQAKGAYGPVLREGRELVVTalPLYHVFALTVNCLLFIeMGGSNLLITNPR 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR-AAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACL-LTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVH-LLEGYGLTECSPL 365
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 366 VTGNPYDLA-DYSGAIGLPVPSTEVRIVDDegnvlnygqtGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFD 444
Cdd:cd17638 157 TMCRPGDDAeTVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 445 ENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDP-SLTKDELITHCRKHLT 523
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 521099036 524 GYKVPKLIEFREELPKTNVGKILR 547
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-552 |
3.63e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 240.45 E-value: 3.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANtleqiVAnTQVKHVVltSLGQMLPRAKGTLVDFVVKYVKGM------VPKYDLPgaismrkalh 191
Cdd:PRK07786 111 SDCGAHVVVTEAALAP-----VA-TAVRDIV--PLLSTVVVAGGSSDDSVLGYEDLLaeagpaHAPVDIP---------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 192 kgrrlqyvkpfmsgEDI-AFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTALPLYHVFALTvNCL 270
Cdd:PRK07786 173 --------------NDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNG--ADINSDVGFVGVPLFHIAGIG-SML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 271 LFIEMGGSNLLI-TNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMA---VQRAVAEKWK 346
Cdd:PRK07786 236 PGLLLGAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPAsdtLLRQMAATFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 347 kitGVHLLEGYGLTECSP---LVTGNpyDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPE 423
Cdd:PRK07786 316 ---EAQILAAFGQTEMSPvtcMLLGE--DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 424 ATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV 503
Cdd:PRK07786 391 ATAEAF-AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAA 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 521099036 504 KRDPS--LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK07786 470 VRNDDaaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
31-553 |
4.89e-72 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 238.32 E-value: 4.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 31 QSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQ-YPV--ALFGIlraGMIAVNVNPL 107
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEmILVihALQQL---GAVAVLLNTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 108 YTPRELEHQLNDADARAIVIVSNFAntlEQIVANTQVKhvvLTSLGQmLPRAKGTLVdfvvkyvkgmvPKYDLpgaismr 187
Cdd:PRK03640 86 LSREELLWQLDDAEVKCLITDDDFE---AKLIPGISVK---FAELMN-GPKEEAEIQ-----------EEFDL------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 188 kalhkgrrlqyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANvlqakgAYGPVLREG---RELVVTALPLYHVFA 264
Cdd:PRK03640 141 ------------------DEVATIMYTSGTTGKPKGVIQTYGNHWWS------AVGSALNLGlteDDCWLAAVPIFHISG 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 265 LTVncLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVnnEDFHEL----NFANMKLsvGGGMAvQRA 340
Cdd:PRK03640 197 LSI--LMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVSTMLQRLL--ERLGEGtypsSFRCMLL--GGGPA-PKP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 VAEKWKKiTGVHLLEGYGLTE-CSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDeGNVLNYGQTGELQVRGPQVMQGYW 419
Cdd:PRK03640 270 LLEQCKE-KGIPVYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 420 QRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVK 499
Cdd:PRK03640 348 NREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPV 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 521099036 500 IYVVKrDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK03640 427 AFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-552 |
9.85e-72 |
|
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: 236.12 E-value: 9.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 48 VMTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVI 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGL-AALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 VSNFantleqivantqvkhvvltslGQMLPRAkgtlvdfvvkyvkgmvpkydLPGaismrkalhkgrrlqyvkpfmsgeD 207
Cdd:cd05903 80 PERF---------------------RQFDPAA--------------------MPD------------------------A 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 IAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGrELVVTALPLYH----VFALTVNCLLfiemGGSNLL-- 281
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPG-DVFLVASPMAHqtgfVYGFTLPLLL----GAPVVLqd 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 282 ITNPRDIPGFVKElqkHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTE 361
Cdd:cd05903 168 IWDPDKALALMRE---HGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTE 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 362 CSPLVTGNPYDLADYSGAI-GLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDI 440
Cdd:cd05903 245 CPGAVTSITPAPEDRRLYTdGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDL 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 441 VRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDP-SLTKDELITHC- 518
Cdd:cd05903 324 ARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVAYLd 403
|
490 500 510
....*....|....*....|....*....|....
gi 521099036 519 RKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05903 404 RQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-545 |
1.24e-71 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 237.61 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQNELKlkKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAI 125
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMTK--EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 VIVSNF---ANTLEQIVANTQVKHVVLTSLgqmlpRAKGTLVDFVVKYVKGMVPKYDLpgaismrkalhkgRRLQYVKPF 202
Cdd:cd05909 83 LTSKQFiekLKLHHLFDVEYDARIVYLEDL-----RAKISKADKCKAFLAGKFPPKWL-------------LRIFGVAPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 MSgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPvlrEGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLI 282
Cdd:cd05909 145 QP-DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDP---NPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEdfHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTEC 362
Cdd:cd05909 221 PNPLDYKKIPELIYDKKATILLGTPTFLRGYARAA--HPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEC 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 SPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNV-LNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIV 441
Cdd:cd05909 299 SPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 442 RFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALH-GKVLEVAAIGQPHEVSGEvvKIYVVKRDPSLTKDELITHCRK 520
Cdd:cd05909 378 KIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDILKN 455
|
490 500
....*....|....*....|....*.
gi 521099036 521 H-LTGYKVPKLIEFREELPKTNVGKI 545
Cdd:cd05909 456 AgISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
27-553 |
4.09e-70 |
|
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: 234.65 E-value: 4.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLL-ALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVIVS-----NFANTLEQIVANT-QVKHVVL-------TSLGQmLPRAKGTLVDFVVkyvkg 173
Cdd:COG1021 108 AHRRAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVpSLRHVLVvgdagefTSLDA-LLAAPADLSEPRP----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 174 mvpkydlpgaismrkalhkgrrlqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELV 253
Cdd:COG1021 182 ------------------------------DPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICG-LDADTVYLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 254 vtALPLYHVFALTVNCLL-FIEMGGSNLLITNPRDIPGFvkEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSV 331
Cdd:COG1021 231 --ALPAAHNFPLSSPGVLgVLYAGGTVVLAPDPSPDTAF--PLiERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 332 GGGMAVQRAVAEKWKKITGVHLLEGYGLTE----CSPLvtGNPYDLADYSgaIGLPV-PSTEVRIVDDEGNVLNYGQTGE 406
Cdd:COG1021 307 VGGAKLSPELARRVRPALGCTLQQVFGMAEglvnYTRL--DDPEEVILTT--QGRPIsPDDEVRIVDEDGNPVPPGEVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 407 LQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAA 486
Cdd:COG1021 383 LLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 487 IGQPHEVSGEVVKIYVVKRDPSLTKDELITHCR-KHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:COG1021 463 VAMPDEYLGERSCAFVVPRGEPLTLAELRRFLReRGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
14-552 |
1.87e-69 |
|
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: 233.19 E-value: 1.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 14 PETINPDQYLSLVEMFEQSVHKYADQP---AFIN--MGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYP 88
Cdd:cd17642 5 PGPFYPLEDGTAGEQLHKAMKRYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 89 VALFGILRAGMIAVNVNPLYTPRELEHQLNDADARaIVIVSNfaNTLEQiVANTQVKhvvltslgqmlprakgtlvdfvV 168
Cdd:cd17642 84 LPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPT-IVFCSK--KGLQK-VLNVQKK----------------------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 169 KYVKGMV---PKYDLPGAISMRK----ALHKGRRLQYVKP--FMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAK 239
Cdd:cd17642 138 KIIKTIIildSKEDYKGYQCLYTfitqNLPPGFNEYDFKPpsFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHAR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 240 G-AYGPVLREGRElVVTALPLYHVFALTVNCLLFIemGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNED 318
Cdd:cd17642 218 DpIFGNQIIPDTA-ILTVIPFHHGFGMFTTLGYLI--CGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 319 FHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLL-EGYGLTECSPLVTGNPyDLADYSGAIGLPVPSTEVRIVD-DEG 396
Cdd:cd17642 295 VDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDlDTG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 NVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVA 476
Cdd:cd17642 374 KTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 477 LHGKVLEVAAIGQPHEVSGEVVKIYVVKR-DPSLTKDELITHCRKHLTGYKvpKL---IEFREELPKTNVGKILRRVLRE 552
Cdd:cd17642 454 QHPKIFDAGVAGIPDEDAGELPAAVVVLEaGKTMTEKEVMDYVASQVSTAK--RLrggVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
25-551 |
5.24e-69 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 231.50 E-value: 5.24e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFI---NMGSVMTF--RKL-EERSRAFAAYLQneLKLKKGDRVALMMPNLLQYPVALFGILRAG 98
Cdd:PRK08008 9 LRQMWDDLADVYGHKTALIfesSGGVVRRYsyLELnEEINRTANLFYS--LGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 99 MIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQI--VANTQVKHVVLTslGQMLPRAKGTlVDFvvkyvkgmvp 176
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIqqEDATPLRHICLT--RVALPADDGV-SSF---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 177 kydlpgaiSMRKALHKGRrLQYVKPfMSGEDIAFLQYTGGTTGVAKGAILTHRNmvanvLQAKGAYGP---VLREgRELV 253
Cdd:PRK08008 154 --------TQLKAQQPAT-LCYAPP-LSTDDTAEILFTSGTTSRPKGVVITHYN-----LRFAGYYSAwqcALRD-DDVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 254 VTALPLYHV-FALTVNCLLFieMGGSNLLITNPRDIPGFVKELQKHPFTaITG-----VNTLF-NALVNNEDFHELN--F 324
Cdd:PRK08008 218 LTVMPAFHIdCQCTAAMAAF--SAGATFVLLEKYSARAFWGQVCKYRAT-ITEcipmmIRTLMvQPPSANDRQHCLRevM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 325 ANMKLSVgggmavqravAEKWKKIT--GVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYG 402
Cdd:PRK08008 295 FYLNLSD----------QEKDAFEErfGVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 403 QTGELQVRG---PQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHG 479
Cdd:PRK08008 365 EIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHP 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 480 KVLEVAAIGQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PRK08008 445 KIQDIVVVGIKDSIRDEAIKAFVVlNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
7-553 |
2.06e-68 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 230.64 E-value: 2.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 7 SRYPSdVPEtinPDQyLSLVEMFEQSVHKYADQPAFIN--MGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNL 84
Cdd:PLN02330 17 SRYPS-VPV---PDK-LTLPDFVLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARaiVIVSNFANTleqivanTQVKhvvltSLGqmLPrakgtlv 164
Cdd:PLN02330 91 AEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAK--LIVTNDTNY-------GKVK-----GLG--LP------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 165 dfVVkyvkgMVPKYDLPGAISMRKALHKGRRL--QYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAY 242
Cdd:PLN02330 148 --VI-----VLGEEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 243 GPVLReGRELVVTALPLYHVFALTVNCLLFIEMGGSnLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHEL 322
Cdd:PLN02330 221 GPEMI-GQVVTLGLIPFFHIYGITGICCATLRNKGK-VVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 323 NFANMKL----SVGGGMAVQRAVAEKwKKITGVHLLEGYGLTE--CSPLVTGNP---YDLADySGAIGLPVPSTEVRIVD 393
Cdd:PLN02330 299 DLSKLKLqaimTAAAPLAPELLTAFE-AKFPGVQVQEAYGLTEhsCITLTHGDPekgHGIAK-KNSVGFILPNLEVKFID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 394 -DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIE 472
Cdd:PLN02330 377 pDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 473 DVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDE-LITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PLN02330 457 AILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLK 536
|
..
gi 521099036 552 EE 553
Cdd:PLN02330 537 EK 538
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
7-551 |
2.21e-68 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 230.88 E-value: 2.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 7 SRYPSdVPetINPDQYLSLVEmFEQSVHKYADQPAFIN--MGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNL 84
Cdd:PLN02574 27 SKHPP-VP--LPSDPNLDAVS-FIFSHHNHNGDTALIDssTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 85 LQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADArAIVIVSnfANTLEQivantqvkhvvLTSLGqmlprakgtlv 164
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSV-GLAFTS--PENVEK-----------LSPLG----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 165 dfvvkyvkgmVPKYDLPGAI---SMRKALHKGRRLQY------VKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANV 235
Cdd:PLN02574 158 ----------VPVIGVPENYdfdSKRIEFPKFYELIKedfdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 236 -LQAKGAYGPVLREGRELV-VTALPLYHVFALTVNCLLFIEMGgSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNAL 313
Cdd:PLN02574 228 eLFVRFEASQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLG-STIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMAL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 314 VNNEDFHELN-FANMKL-SVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTG--NPYDLADYSgAIGLPVPSTEV 389
Cdd:PLN02574 307 TKKAKGVCGEvLKSLKQvSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRgfNTEKLSKYS-SVGLLAPNMQA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 390 RIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYP 468
Cdd:PLN02574 386 KVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 469 NEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:PLN02574 466 ADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGStLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILR 545
|
....
gi 521099036 548 RVLR 551
Cdd:PLN02574 546 RELK 549
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
40-552 |
9.67e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 227.48 E-value: 9.67e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 40 PAFINMGS--VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK08276 1 PAVIMAPSgeVVTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIVAntqvkhvvltslgqMLPRAKGTLvdfvvkyvkgMVPKYDLPGAISMRKALHKgrrlq 197
Cdd:PRK08276 80 DDSGAKVLIVSAALADTAAELAA--------------ELPAGVPLL----------LVVAGPVPGFRSYEEALAA----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfMSGEDIA------FLQYTGGTTGVAKGAI--LTHR--NMVANVLQAKGAYGPVLREGRELVVTAlPLYH----VF 263
Cdd:PRK08276 131 -----QPDTPIAdetagaDMLYSSGTTGRPKGIKrpLPGLdpDEAPGMMLALLGFGMYGGPDSVYLSPA-PLYHtaplRF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 264 ALTVncllfIEMGGsnLLITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVN--NEDFHELNFANMKLSVGGG----MA 336
Cdd:PRK08276 205 GMSA-----LALGG--TVVVMEKfDAEEALALIERYRVTHSQLVPTMFVRMLKlpEEVRARYDVSSLRVAIHAAapcpVE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQRAVAEKWKKItgvhLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPStEVRIVDDEGNVLNYGQTGELQVRGPQVMQ 416
Cdd:PRK08276 278 VKRAMIDWWGPI----IHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 417 GYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE 496
Cdd:PRK08276 353 EYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGE 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 497 VVKIYV-----VKRDPSLTkDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK08276 433 RVKAVVqpadgADAGDALA-AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
24-553 |
4.15e-67 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 227.32 E-value: 4.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFI-NMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 103 NVNPLYTPRELEHQLNDADARAIVIVSNFANT--LEQIVA-NTQVKHvvltsLGQMLprakgtLVDfvvkyvkGMVPKYD 179
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAPTLFKQTrpVDLILPlQNQLPQ-----LQQIV------GVD-------KLAPATS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 180 lpgAISMRKALHKGRRLQYvKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVAnvlqAKGAYGPVL-REGRELVVTALP 258
Cdd:PRK06087 165 ---SLSLSQIIADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILA----SERAYCARLnLTWQDVFMMPAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 259 LYHVFALTVNCLLFIEMGGSNLL--ITNPRDIpgfVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMA 336
Cdd:PRK06087 237 LGHATGFLHGVTAPFLIGARSVLldIFTPDAC---LALLEQQRCTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQRAVAEKWKKiTGVHLLEGYGLTECSPLVTGNPYDLADYSGAI-GLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVM 415
Cdd:PRK06087 314 IPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 416 QGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSG 495
Cdd:PRK06087 393 MGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLG 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 496 EVVKIYVVKRDP--SLTKDELITH-CRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK06087 473 ERSCAYVVLKAPhhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-551 |
1.26e-65 |
|
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: 217.73 E-value: 1.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 GEDIAFLQYTGGTTGVAKGAILTHRNMVAN--VLQAKGAYGPvlregRELVVTALPLYHVFALTVNCLLFIEMGGSNLLI 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDP-----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 T-----NPRDIPGFVKELQKHPFTAITGVNTLFNALVN---NEDFHELNFAnmklsVGGGMAVQRAVAEKWKKITGVHLL 354
Cdd:cd05944 76 GpagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQvpvNADISSLRFA-----MSGAAPLPVELRARFEDATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 355 EGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIV--DDEGNVL---NYGQTGELQVRGPQVMQGYWQRpEATKEVI 429
Cdd:cd05944 151 EGYGLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 NEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYV-VKRDPS 508
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 521099036 509 LTKDELITHCRKHLTGY-KVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05944 310 VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-551 |
4.20e-65 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 218.89 E-value: 4.20e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 39 QPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLN 118
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 119 DADARAIVIVsnfantleqivantqvkHVVLTSlgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqy 198
Cdd:cd05958 81 KARITVALCA-----------------HALTAS----------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 199 vkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVAnvlqAKGAYGP-VLR-EGRELVVTALPLYHVFALTVNCLLFIEMG 276
Cdd:cd05958 97 -------DDICILAFTSGTTGAPKATMHFHRDPLA----SADRYAVnVLRlREDDRFVGSPPLAFTFGLGGVLLFPFGVG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 277 GSNLLI--TNPRDIPGFVKELQKhpfTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLL 354
Cdd:cd05958 166 ASGVLLeeATPDLLLSAIARYKP---TVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPII 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 355 EGYGLTECSPLVTGNPYDLADySGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQvmqGYWQRPEATKEVINEEGW 434
Cdd:cd05958 243 DGIGSTEMFHIFISARPGDAR-PGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGW 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 435 LSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR-----DPSL 509
Cdd:cd05958 319 NITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipGPVL 398
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 521099036 510 TKdELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05958 399 AR-ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-551 |
9.06e-65 |
|
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: 218.46 E-value: 9.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 60 AFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAG----MIAVNVNPLYTPRELEHQLNDADARaIVIVSNFANTL 135
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGR-IVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 136 EQIVAntqvkhvvltslgqmlprakgtlvdfVVKYVKGMVpkYDLPGAISMRKALhKGRRLqyvkpfmSGEDIAFLQYTG 215
Cdd:cd05922 83 LRDAL--------------------------PASPDPGTV--LDADGIRAARASA-PAHEV-------SHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 216 GTTGVAKGAILTHRNMVANVlQAKGAYGPVlrEGRELVVTALPLYHVFALTVncLLFIEMGGSNLLITNPRDIP-GFVKE 294
Cdd:cd05922 127 GSTGSPKLVRLSHQNLLANA-RSIAEYLGI--TADDRALTVLPLSYDYGLSV--LNTHLLRGATLVLTNDGVLDdAFWED 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 295 LQKHPFTAITGVNTLFNALVNnedfheLNFANMKL-------SVGGGMAvQRAVAEKWKKITGVHLLEGYGLTECSPLVT 367
Cdd:cd05922 202 LREHGATGLAGVPSTYAMLTR------LGFDPAKLpslryltQAGGRLP-QETIARLRELLPGAQVYVMYGQTEATRRMT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 368 GNPYDLADYS-GAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDEN 446
Cdd:cd05922 275 YLPPERILEKpGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDED 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 447 GMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPhEVSGEVVKIYVVkRDPSLTKDELITHCRKHLTGYK 526
Cdd:cd05922 355 GFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVT-APDKIDPKDVLRSLAERLPPYK 432
|
490 500
....*....|....*....|....*
gi 521099036 527 VPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05922 433 VPATVRVVDELPLTASGKVDYAALR 457
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
38-552 |
3.17e-64 |
|
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: 218.55 E-value: 3.17e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:TIGR02262 20 GKTAFIDDISSLSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYML 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIVANT-QVKHVVLTSLGQmlprakgtlvdfvvkyvkgmvpkydlPGAISMRKALHKGRRL 196
Cdd:TIGR02262 99 EDSRARVVFVSGALLPVIKAALGKSpHLEHRVVVGRPE--------------------------AGEVQLAELLATESEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 197 QYVKPfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANvlqAKGAYGPVL--REGrELVVTALPLYHVFALTvNCLLFIE 274
Cdd:TIGR02262 153 FKPAA-TQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT---AELYARNTLgiRED-DVCFSAAKLFFAYGLG-NALTFPM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 275 MGGSNLLITNPRDIPGFV-KELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHL 353
Cdd:TIGR02262 227 SVGATTVLMGERPTPDAVfDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 354 LEGYGLTECSPLVTGNPYDLADYsGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEG 433
Cdd:TIGR02262 307 VDGIGSTEMLHIFLSNLPGDVRY-GTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTF-QGE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-PSLTKD 512
Cdd:TIGR02262 385 WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPgQTALET 464
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 521099036 513 ELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:TIGR02262 465 ELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-552 |
8.68e-64 |
|
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: 218.26 E-value: 8.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQNELKlkKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPRELEHQ------LNDADA 122
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPPPTPGRHAerlaaiLADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 123 RAIVIVSNFANTLEQIVANtqvkhvvltslgqmlPRAKGTLVDFVVkyvkgmvpkyDLPGAismrkalhkGRRLQYVKPF 202
Cdd:cd05931 100 RVVLTTAAALAAVRAFAAS---------------RPAAGTPRLLVV----------DLLPD---------TSAADWPPPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 MSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGrELVVTALPLYHVFALTVNCLLFIEMGGSNLLI 282
Cdd:cd05931 146 PDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYG--LDPG-DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TnPRDipgFV-------KELQKHPFTaITGV-NtlFnAL------VNNEDFHELNFANMKLSVGGG----MAVQRAVAEK 344
Cdd:cd05931 223 S-PAA---FLrrplrwlRLISRYRAT-ISAApN--F-AYdlcvrrVRDEDLEGLDLSSWRVALNGAepvrPATLRRFAEA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 345 WKKiTGVH---LLEGYGLTECSPLVTGNP---------YDLADYSGAI----------------GLPVPSTEVRIVDDEG 396
Cdd:cd05931 295 FAP-FGFRpeaFRPSYGLAEATLFVSGGPpgtgpvvlrVDRDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 N-VLNYGQTGELQVRGPQVMQGYWQRPEATKEVIN------EEGWLSTGDI-VRFDenGMIYIVDRKKDMILVSGFNVYP 468
Cdd:cd05931 374 GrELPDGEVGEIWVRGPSVASGYWGRPEATAETFGalaatdEGGWLRTGDLgFLHD--GELYITGRLKDLIIVRGRNHYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 469 NEIEDVVALHGKVLE---VAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITH------CRKH-LTGYKVpKLIEFReELP 538
Cdd:cd05931 452 QDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAairaavAREHgVAPADV-VLVRPG-SIP 529
|
570
....*....|....
gi 521099036 539 KTNVGKILRRVLRE 552
Cdd:cd05931 530 RTSSGKIQRRACRA 543
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
38-552 |
1.11e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 216.60 E-value: 1.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINM--GSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:PRK09088 10 QRLAAVDLalGRRWTYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARAIvivsnfantleqivantqvkhvvltsLGQMLPRAKGTLVDfvvkyvkgmvpkyDLPGAISMRKALHKGRR 195
Cdd:PRK09088 89 LLQDAEPRLL--------------------------LGDDAVAAGRTDVE-------------DLAAFIASADALEPADT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 196 lqyvkPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAkGAYGPVLREGRELVVTalPLYHVFALTVNCLLFIEM 275
Cdd:PRK09088 130 -----PSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRVDAHSSFLCDA--PMFHIIGLITSVRPVLAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSnLLITNPRDiPGFVKELQKHPFTAIT---GVNTLFNALVNNEDFHELNFANMKLSVGGGmAVQRAVAEKWKKITGVH 352
Cdd:PRK09088 202 GGS-ILVSNGFE-PKRTLGRLGDPALGIThyfCVPQMAQAFRAQPGFDAAALRHLTALFTGG-APHAAEDILGWLDDGIP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 LLEGYGLTECSPlVTGNPYD---LADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVI 429
Cdd:PRK09088 279 MVDGFGMSEAGT-VFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 NEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSL 509
Cdd:PRK09088 358 TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAP 437
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 521099036 510 TKDELI-THCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK09088 438 LDLERIrSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
25-553 |
7.50e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 215.29 E-value: 7.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAIVIVSNFANTLEQI-VANTQVKHVVltSLGqmLPRAkGTLVDFVVkyvkgmvpkydlpga 183
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARAMICHADFPEHAAAVrAASPDLTHVV--AIG--GARA-GLDYEALV--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 184 ismrkALHKGRRLQYVKpfMSGEDIAFLQYTGGTTGVAKGAILTHRNM---VANVLqakGAYGPVLRE-GRELVVTalPL 259
Cdd:PRK07470 148 -----ARHLGARVANAA--VDHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHL---ADLMPGTTEqDASLVVA--PL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 260 YHvfALTVNCLLFIEMGGSNLLITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQ 338
Cdd:PRK07470 216 SH--GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 339 RAVAEKWKKITGVHLLEGYGLTEcsplVTGN-----PY--DLADYS----GAIGLPVPSTEVRIVDDEGNVLNYGQTGEL 407
Cdd:PRK07470 294 RADQKRALAKLGKVLVQYFGLGE----VTGNitvlpPAlhDAEDGPdariGTCGFERTGMEVQIQDDEGRELPPGETGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 408 QVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAI 487
Cdd:PRK07470 370 CVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 488 GQPHEVSGEV-VKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK07470 449 GVPDPVWGEVgVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
24-553 |
2.20e-61 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 211.54 E-value: 2.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 104 VNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANtqvkhvvltslgqMLPRAKGTLVDfvvkyvkgMVPKYDLPGA 183
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLVVEAALLAALEAADPG-------------DLPLPAVWLLD--------APASVSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 184 ISMRKALHKGRRLQYVKPfmSGEDIAFLQYTGGTTGVAKGAILTH-------RNMvANVLQakgaygpvLREGrELVVTA 256
Cdd:PRK06155 160 WSTAPLPPLDAPAPAAAV--QPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNS-AEDLE--------IGAD-DVLYTT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 257 LPLYHVFALtvNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTaitgVNTLFNALVN---------NEDFHELNFAnm 327
Cdd:PRK06155 228 LPLFHTNAL--NAFFQALLAGATYVLEPRFSASGFWPAVRRHGAT----VTYLLGAMVSillsqpareSDRAHRVRVA-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 328 kLSVGGGMAVQRAVAEKwkkiTGVHLLEGYGLTEcSPLVTGNPYDlADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGEL 407
Cdd:PRK06155 300 -LGPGVPAALHAAFRER----FGVDLLDGYGSTE-TNFVIAVTHG-SQRPGSMGRLAPGFEARVVDEHDQELPDGEPGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 408 QVRGPQ---VMQGYWQRPEATKEVINEEgWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEV 484
Cdd:PRK06155 373 LLRADEpfaFATGYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 485 AAIGQPHEVSGEVVKIYVVKRD-PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-551 |
3.64e-61 |
|
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: 208.44 E-value: 3.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 47 SVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIV 126
Cdd:cd05971 5 EKVTFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 127 IvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkyDLPgaismrkalhkgrrlqyvkpfmsgE 206
Cdd:cd05971 84 T---------------------------------------------------DGS------------------------D 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 207 DIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGR------------ELVVTALP-LYHvfaltvncllfi 273
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDlywtpadwawigGLLDVLLPsLYF------------ 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 274 emgGSNLLITNPR--DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGV 351
Cdd:cd05971 157 ---GVPVLAHRMTkfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 352 HLLEGYGLTECSpLVTGNPYDLADY-SGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQ--VMQGYWQRPEATKEV 428
Cdd:cd05971 234 EVNEFYGQTECN-LVIGNCSALFPIkPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKK 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 429 INEeGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRdPS 508
Cdd:cd05971 313 MAG-DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLN-PG 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 509 LTKDELIT-----HCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05971 391 ETPSDALAreiqeLVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
50-547 |
5.51e-61 |
|
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: 208.45 E-value: 5.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd05914 9 TYKDLADNIAKFALLLKIN-GVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgEDIA 209
Cdd:cd05914 88 E---------------------------------------------------------------------------DDVA 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKgAYGPVLREGRelVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRdiP 289
Cdd:cd05914 93 LINYTSGTTGNSKGVMLTYRNIVSNVDGVK-EVVLLGKGDK--ILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP--S 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 290 GFVKELQKHPFTAITGVNTLF-----------------------NALVNNEDFHELNF--------ANMKLSVGGGMAVQ 338
Cdd:cd05914 168 AKIIALAFAQVTPTLGVPVPLviekifkmdiipkltlkkfkfklAKKINNRKIRKLAFkkvheafgGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 339 RAVAEKWKKItGVHLLEGYGLTECSPLVTGNPYDlADYSGAIGLPVPSTEVRIVDDEGNVlnygQTGELQVRGPQVMQGY 418
Cdd:cd05914 248 PDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPN-RIRLGSAGKVIDGVEVRIDSPDPAT----GEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILV-SGFNVYPNEIEDVVALHGKVLEvAAIGQPHEvsGEV 497
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEK--KLV 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 498 VKIYVvkrDPSL--------------TKDELITHCRKHLTGY-KVPKLIEFREELPKTNVGKILR 547
Cdd:cd05914 399 ALAYI---DPDFldvkalkqrniidaIKWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
50-550 |
6.45e-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: 207.69 E-value: 6.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADaraivivs 129
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALK-AQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvKHVVLTSlgqmlprAKGTLVDFVvkyvkgmvpkydlpgAISMRKALHKGRRLQYVKPFMSGEDIA 209
Cdd:TIGR01923 72 ---------------VQLLLTD-------SLLEEKDFQ---------------ADSLDRIEAAGRYETSLSASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVtaLPLYHVFALTV--NCLLfiemGGSNLLITNPRD 287
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG-FTEDDNWLLS--LPLYHISGLSIlfRWLI----EGATLRIVDKFN 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 288 ipGFVKELQKHPFTAITGVNTLFNALVNnEDFHELNFANMKLsvgGGMAVQRAVAEKWKKiTGVHLLEGYGLTE-CSPLV 366
Cdd:TIGR01923 188 --QLLEMIANERVTHISLVPTQLNRLLD-EGGHNENLRKILL---GGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 367 TGNPYDLADYSGAiGLPVPSTEVRIVDDegnvlNYGQTGELQVRGPQVMQGYWQRPEATkEVINEEGWLSTGDIVRFDEN 446
Cdd:TIGR01923 261 TATPEMLHARPDV-GRPLAGREIKIKVD-----NKEGHGEIMVKGANLMKGYLYQGELT-PAFEQQGWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 447 GMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPsLTKDELITHCRKHLTGYK 526
Cdd:TIGR01923 334 GFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD-ISQAKLIAYLTEKLAKYK 412
|
490 500
....*....|....*....|....
gi 521099036 527 VPKLIEFREELPKTNVGKILRRVL 550
Cdd:TIGR01923 413 VPIAFEKLDELPYNASGKILRNQL 436
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
36-552 |
4.90e-60 |
|
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: 206.77 E-value: 4.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 36 YADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:cd12118 17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARAIVIVSNFanTLEQIVAntqvkhvvltslgqmlpRAKGtlvDFvvkyvkGMVPKYDLPGAISmrkalhkgrr 195
Cdd:cd12118 96 ILRHSEAKVLFVDREF--EYEDLLA-----------------EGDP---DF------EWIPPADEWDPIA---------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 196 lqyvkpfmsgediafLQYTGGTTGVAKGAILTHR----NMVANVLQAKGAYGPVLregrelvVTALPLYHV----FALTV 267
Cdd:cd12118 138 ---------------LNYTSGTTGRPKGVVYHHRgaylNALANILEWEMKQHPVY-------LWTLPMFHCngwcFPWTV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 268 NCLlfiemGGSNLLITNPrDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKK 347
Cdd:cd12118 196 AAV-----GGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ItGVHLLEGYGLTECSPLVTGNPY-----DLADYSGAI-----GLPVPS-TEVRIVDDEGN--VLNYGQT-GELQVRGPQ 413
Cdd:cd12118 270 L-GFDVTHVYGLTETYGPATVCAWkpewdELPTEERARlkarqGVRYVGlEEVDVLDPETMkpVPRDGKTiGEIVFRGNI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 414 VMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEV 493
Cdd:cd12118 349 VMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEK 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 494 SGEVVKIYV-VKRDPSLTKDELITHCRKHLTGYKVPKLIEFReELPKTNVGKILRRVLRE 552
Cdd:cd12118 428 WGEVPCAFVeLKEGAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTGKIQKFVLRD 486
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
213-547 |
7.46e-60 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 201.73 E-value: 7.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 213 YTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREgRELVVTALPLYHVFALTVNcLLFIEMGGSNLLITNpRDIPGFV 292
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTE-ADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEK-FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 293 KELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAvqrAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYD 372
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLSPYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 373 laDYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATkEVINEEGWLSTGDIVRFDENGMIYIV 452
Cdd:cd17637 159 --ERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELT-AYTFRNGWHHTGDLGRFDEDGYLWYA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 453 DRK--KDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVK-IYVVKRDPSLTKDELITHCRKHLTGYKVPK 529
Cdd:cd17637 236 GRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKaVCVLKPGATLTADELIEFVGSRIARYKKPR 315
|
330
....*....|....*...
gi 521099036 530 LIEFREELPKTNVGKILR 547
Cdd:cd17637 316 YVVFVEALPKTADGSIDR 333
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
75-553 |
2.52e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 204.45 E-value: 2.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 75 DRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIvivsnfantleqivantqvkhvvltsLGQ 154
Cdd:PRK07787 46 RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW--------------------------LGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 155 mLPRAKGTLvdfvvkyvkgmvPKYDLpgaismrkALHKGRRLQYVKPfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVAN 234
Cdd:PRK07787 100 -APDDPAGL------------PHVPV--------RLHARSWHRYPEP--DPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 235 VLQAKGAYGpvlREGRELVVTALPLYHVFALTVNCLLFIEMGGSnlLITNPRDIPGFVKELQKHPFTAITGVNTLFNALV 314
Cdd:PRK07787 157 LDALAEAWQ---WTADDVLVHGLPLFHVHGLVLGVLGPLRIGNR--FVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 315 NNEDfHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTE----CSPLVTGNPYdladySGAIGLPVPSTEVR 390
Cdd:PRK07787 232 ADPE-AARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTEtlitLSTRADGERR-----PGWVGLPLAGVETR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 391 IVDDEGNVLNY-GQT-GELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKK-DMILVSGFNVY 467
Cdd:PRK07787 306 LVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 468 PNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSlTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:PRK07787 386 AGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLK 464
|
....*.
gi 521099036 548 RVLREE 553
Cdd:PRK07787 465 KQLLSE 470
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
38-555 |
1.12e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 203.19 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFAntleqIVANTQVKHVVLTSLGQMLPRAKGTlvdfvvkyvkgmvpkydlPGAISMRKALhkgrrlq 197
Cdd:PRK06145 96 GDAGAKLLLVDEEFD-----AIVALETPKIVIDAAAQADSRRLAQ------------------GGLEIPPQAA------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVTalPLYHVFALTVNCLLFIEMGG 277
Cdd:PRK06145 146 -VAP----TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALG-LTASERLLVVG--PLYHVGAFDLPGIAVLWVGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SnLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAV-QRAVAEKWKKITGVHLLEG 356
Cdd:PRK06145 218 T-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRARYIDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECsplVTGNPYDLA----DYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEE 432
Cdd:PRK06145 297 YGLTET---CSGDTLMEAgreiEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 433 GWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE-VVKIYVVKRDPSLTK 511
Cdd:PRK06145 373 DWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGErITAVVVLNPGATLTL 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 521099036 512 DELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREEND 555
Cdd:PRK06145 453 EALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
28-552 |
2.54e-58 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 202.61 E-value: 2.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 28 MF-EQSVHKYADQPAFI--NMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK13391 1 MYpGIHAQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFRS-LGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAIVivsnfantleqivaNTQVKHVVLTSLGQMLPRAKGTLVdfvvkyvkgmvpkYDLPGAI 184
Cdd:PRK13391 80 NSHLTPAEAAYIVDDSGARALI--------------TSAAKLDVARALLKQCPGVRHRLV-------------LDGDGEL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 185 SMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKG--AILTHRNMVAN-----VLQAkgAYGpvLREGRELVVTAl 257
Cdd:PRK13391 133 EGFVGYAEAVAGLPATPIADESLGTDMLYSSGTTGRPKGikRPLPEQPPDTPlpltaFLQR--LWG--FRSDMVYLSPA- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 258 PLYHVfALTVNCLLFIEMGGSNLLITNpRDIPGFVKELQKHPFTAITGVNTLFNALVN--NEDFHELNFANMKLSVGGG- 334
Cdd:PRK13391 208 PLYHS-APQRAVMLVIRLGGTVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAa 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 335 ---MAVQRAVAEKWKKItgVHllEGYGLTECSPLVTGNPYDLADYSGAIGLPVPStEVRIVDDEGNVLNYGQTGELQVRG 411
Cdd:PRK13391 286 pcpPQVKEQMIDWWGPI--IH--EYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 412 PQVMQgYWQRPEATKEVINEEG-WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK13391 361 GRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVP 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 491 HEVSGEVVKIYVVKRDPSLTKD----ELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK13391 440 NEDLGEEVKAVVQPVDGVDPGPalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-550 |
3.29e-57 |
|
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: 198.14 E-value: 3.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 37 ADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYtPRE-LEH 115
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLR-ERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARaivivsnfantleqivantqvkhVVLTSlgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrr 195
Cdd:cd05930 79 ILEDSGAK-----------------------LVLTD-------------------------------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 196 lqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREGRELVVTALplyhVFALTVNCLLFIEM 275
Cdd:cd05930 92 ---------PDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRVLQFTSF----SFDVSVWEIFGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFheLNFANMKLSVGGGMAVQRAVAEKWKKI-TGV 351
Cdd:cd05930 158 AGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLVLVGGEALPPDLVRRWRELlPGA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 352 HLLEGYGLTECSPLVTGN--PYDLADYSG-AIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEV 428
Cdd:cd05930 236 RLVNLYGPTEATVDATYYrvPPDDEEDGRvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAER 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 429 INEEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYV 502
Cdd:cd05930 316 FVPNPFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYV 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 521099036 503 V-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05930 396 VpDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
50-553 |
1.93e-56 |
|
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: 198.07 E-value: 1.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd05928 43 SFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVANTqvkhvvltslgqmlPRAKgtlvdfvvkyVKGMVPKYDLPGAISMRKaLHKGRRLQYVKPFMSGEDIA 209
Cdd:cd05928 123 ELAPEVDSVASEC--------------PSLK----------TKLLVSEKSRDGWLNFKE-LLNEASTEHHCVETGSQEPM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHrnmvanvlqakGAYG-PVLREGRELVvtALPLYHVF--------ALTVNCLLFIE-MGGSN 279
Cdd:cd05928 178 AIYFTSGTTGSPKMAEHSH-----------SSLGlGLKVNGRYWL--DLTASDIMwntsdtgwIKSAWSSLFEPwIQGAC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 280 LLITN-PR-DIPGFVKELQKHPFTAITGVNTLFNALVNnEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGY 357
Cdd:cd05928 245 VFVHHlPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 358 GLTEcSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVR-GPQ----VMQGYWQRPEATKEVINEE 432
Cdd:cd05928 324 GQTE-TGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 433 GWLsTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV------KRD 506
Cdd:cd05928 403 FYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflSHD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 507 P-SLTKdELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:cd05928 482 PeQLTK-ELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
18-552 |
2.37e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 195.53 E-value: 2.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 18 NPDQYLSLVEMF----------EQSVHKYADQPAFIN-MGSvMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQ 86
Cdd:PRK07788 34 RPDNGLRLAADIrrygpfaglvAHAARRAPDRAALIDeRGT-LTYAELDEQSNALARGLL-ALGVRAGDGVAVLARNHRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 87 YPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKG--TLV 164
Cdd:PRK07788 112 FVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTdeTLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 165 DFVVKYVKGMVPKYDLPGAISMrkalhkgrrlqyvkpfmsgediaflqYTGGTTGVAKGAILTHRNMVANVlqakgayGP 244
Cdd:PRK07788 192 DLIAGSSTAPLPKPPKPGGIVI--------------------------LTSGTTGTPKGAPRPEPSPLAPL-------AG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 245 VLRE----GRELVVTALPLYHvfALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFH 320
Cdd:PRK07788 239 LLSRvpfrAGETTLLPAPMFH--ATGWAHLTLAMALGSTVVLRRRFDPEATLEDIAKHKATALVVVPVMLSRILDLGPEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 321 ELNF--ANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNV 398
Cdd:PRK07788 317 LAKYdtSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPeaTKEVINeeGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALH 478
Cdd:PRK07788 397 VPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGH 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 479 GKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK07788 473 PDVVEAAVIGVDDEEFGQRLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-489 |
6.10e-55 |
|
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: 192.57 E-value: 6.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGmiAVNVnplytPR-------ELEHQLNDADA 122
Cdd:cd17640 7 TYKDLYQEILDFAAGLRS-LGVKAGEKVALFADNSPRWLIADQGIMALG--AVDV-----VRgsdssveELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 123 RAIViVSNfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpf 202
Cdd:cd17640 79 VALV-VEN------------------------------------------------------------------------ 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 mSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAkGAYGPVLREGRELVVtaLPLYHVFALTvnCLLFIEMGGSNLLI 282
Cdd:cd17640 86 -DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSL-SDIVPPQPGDRFLSI--LPIWHSYERS--AEYFIFACGCSQAY 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNPRDIPgfvKELQKHPFTAITGVNTLFNALVNNED-------------FHELNFA-NMKLSVGGGMAVQRAVaEKWKKI 348
Cdd:cd17640 160 TSIRTLK---DDLKRVKPHYIVSVPRLWESLYSGIQkqvsksspikqflFLFFLSGgIFKFGISGGGALPPHV-DTFFEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 349 TGVHLLEGYGLTECSPLVTGNPYDlADYSGAIGLPVPSTEVRIVDDEGN-VLNYGQTGELQVRGPQVMQGYWQRPEATKE 427
Cdd:cd17640 236 IGIEVLNGYGLTETSPVVSARRLK-CNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 428 VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS-GFNVYPNEIEDvVALHGKVLE-VAAIGQ 489
Cdd:cd17640 315 VLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEE-ALMRSPFIEqIMVVGQ 377
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
15-554 |
8.38e-55 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 194.12 E-value: 8.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 15 ETINPDqylslvemFEQSVHKYADQPAFINM----GSV--MTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYP 88
Cdd:PRK13295 24 RTINDD--------LDACVASCPDKTAVTAVrlgtGAPrrFTYRELAALVDRVAVGL-ARLGVGRGDVVSCQLPNWWEFT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 89 VALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFAN-TLEQIVANTQVKhvvLTSLGQMLPRAKGTLVDFV 167
Cdd:PRK13295 95 VLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGfDHAAMARRLRPE---LPALRHVVVVGGDGADSFE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 168 VKYvkgMVPKYDL-PGAismrKALHKGRRLqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLqakgAYGPVL 246
Cdd:PRK13295 172 ALL---ITPAWEQePDA----PAILARLRP-------GPDDVTQLIYTSGTTGEPKGVMHTANTLMANIV----PYAERL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 247 REGRELVV-TALPLYHVFALTVNCLLFIEMGGSNLL--ITNPRDipgFVKELQKHPFTAITGVNTLFNALVNNEDFHELN 323
Cdd:PRK13295 234 GLGADDVIlMASPMAHQTGFMYGLMMPVMLGATAVLqdIWDPAR---AAELIRTEGVTFTMASTPFLTDLTRAVKESGRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 324 FANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAI-GLPVPSTEVRIVDDEGNVLNYG 402
Cdd:PRK13295 311 VSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVRVVDADGAPLPAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 403 QTGELQVRGPQVMQGYWQRPEATKEviNEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVL 482
Cdd:PRK13295 391 QIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 483 EVAAIGQPHEVSGEVVKIYVVKR-DPSLTKDELITHCR-KHLTGYKVPKLIEFREELPKTNVGKI----LRRVLREEN 554
Cdd:PRK13295 469 QVAIVAYPDERLGERACAFVVPRpGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIqkfrLREMLRGED 546
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-486 |
1.17e-54 |
|
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: 190.17 E-value: 1.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVivs 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvkhvvltSLGQMLPRAKGtlvdfvvkyvkgmVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIA 209
Cdd:TIGR01733 78 ---------------------TDSALASRLAG-------------LVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVTALplyhVFALTVNCLLFIEMGGSNLLITNPRDIP 289
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG-LDPDDRVLQFASL----SFDASVEEIFGALLAGATLVVPPEDEER 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 290 GFVKELQ----KHPFTAITGVNTLFNALVnneDFHELNFANMKLSVGGGMAVQRAVAEKWK-KITGVHLLEGYGLTECSP 364
Cdd:TIGR01733 199 DDAALLAaliaEHPVTVLNLTPSLLALLA---AALPPALASLRLVILGGEALTPALVDRWRaRGPGARLINLYGPTETTV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 365 LVTGNPYDLADYSGA----IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEV-INEEGWLS--- 436
Cdd:TIGR01733 276 WSTATLVDPDDAPREspvpIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERfVPDPFAGGdga 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 521099036 437 ----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAA 486
Cdd:TIGR01733 356 rlyrTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
36-553 |
1.28e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 193.62 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 36 YADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:PRK08162 31 YPDRPAVIHGDRRRTWAETYARCRRLASALA-RRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARAIVIVSNFANTLEQIVAntqvkhvvltslgqMLPRAKGTLVDfvvkYVKGMVPKYDLPGAISMRKALHKGR- 194
Cdd:PRK08162 110 MLRHGEAKVLIVDTEFAEVAREALA--------------LLPGPKPLVID----VDDPEYPGGRFIGALDYEAFLASGDp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 195 RLQYVKPFMSGEDIAfLQYTGGTTGVAKGAILTHR----NMVANVLQAKGAYGPVLregrelvVTALPLYHV----FALT 266
Cdd:PRK08162 172 DFAWTLPADEWDAIA-LNYTSGTTGNPKGVVYHHRgaylNALSNILAWGMPKHPVY-------LWTLPMFHCngwcFPWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCllfieMGGSNLLItnpRDI-PGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEK 344
Cdd:PRK08162 244 VAA-----RAGTNVCL---RKVdPKLIFDLiREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 345 WKKItGVHLLEGYGLTECSPLVTGN----------PYDLADYSGAIGLPVPSTE-VRIVDDEG--NVLNYGQT-GELQVR 410
Cdd:PRK08162 316 MEEI-GFDLTHVYGLTETYGPATVCawqpewdalpLDERAQLKARQGVRYPLQEgVTVLDPDTmqPVPADGETiGEIMFR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK08162 395 GNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKP 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 491 HEVSGEVVKIYV-VKRDPSLTKDELITHCRKHLTGYKVPKLIEFrEELPKTNVGKILRRVLREE 553
Cdd:PRK08162 474 DPKWGEVPCAFVeLKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-551 |
1.28e-54 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 191.18 E-value: 1.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYT---PRELEHQLNDADARaiv 126
Cdd:cd05969 2 TFAQLKVLSARFANVLKS-LGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 127 ivsnfantleqivantqvkhVVLTSlgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlQYVKPFMSGE 206
Cdd:cd05969 75 --------------------VLITT---------------------------------------------EELYERTDPE 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 207 DIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTALP------LYHVFALTVNcllfiemGGSNL 280
Cdd:cd05969 90 DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD--LHPDDIYWCTADPgwvtgtVYGIWAPWLN-------GVTNV 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 281 LITNPRDIPGFVKELQKHP----FTAITGVNTLFN---ALVNNEDFHELNFAnmkLSVGGGMAVQravAEKW-KKITGVH 352
Cdd:cd05969 161 VYEGRFDAESWYGIIERVKvtvwYTAPTAIRMLMKegdELARKYDLSSLRFI---HSVGEPLNPE---AIRWgMEVFGVP 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 LLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRG--PQVMQGYWQRPEATKEVIn 430
Cdd:cd05969 235 IHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR---DP 507
Cdd:cd05969 314 IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKegfEP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 521099036 508 S-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05969 394 SdELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
27-550 |
1.55e-54 |
|
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: 191.95 E-value: 1.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINM--GSVMTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:cd05923 5 EMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARL-HARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYTPRELEHQLNDADARAiVIVSNFANTLEQIVantqvkhvvlTSLGQMLprAKGTLVDFVVKYVKGMVPKYDLPGAi 184
Cdd:cd05923 84 NPRLKAAELAELIERGEMTA-AVIAVDAQVMDAIF----------QSGVRVL--ALSDLVGLGEPESAGPLIEDPPREP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 185 smrkalhkgrrlqyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTAL-PLYHV- 262
Cdd:cd05923 150 ---------------------EQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAG--LRHGRHNVVLGLmPLYHVi 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 263 --FALTVNCLLFiemGGSNLLITNprDIPGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQR 339
Cdd:cd05923 207 gfFAVLVAALAL---DGTYVVVEE--FDPADALKLiEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 340 AVAEKWKKITGVHLLEGYGLTEcsplVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNV---LNYGQTGELQVR--GPQV 414
Cdd:cd05923 282 AVLERVNQHLPGEKVNIYGTTE----AMNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 415 MQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVS 494
Cdd:cd05923 358 FTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERW 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 495 GEVVKIYVVKRDPSLTKDELITHCR-KHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05923 437 GQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-550 |
3.75e-54 |
|
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: 190.87 E-value: 3.75e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR-AAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVIvsnfANTLEQIVANTQVKHVVLTSLGQmlprakgtlvdfvvkyvkgmVPKYDLPGAISm 186
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLEVAVVIDEALDA--------------------GPAGNPAVPVS- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAygpVLREGRELVVTALPLYHVFALT 266
Cdd:cd12117 135 ------------------PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYV---TLGPDDRVLQTSPLAFDASTFE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 V-NCLLFiemGGSNLLIT--NPRDIPGFVKELQKHPFTAITGVNTLFNALVnneDFHELNFANMK-LSVGGGMAVQRAVA 342
Cdd:cd12117 194 IwGALLN---GARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQLA---DEDPECFAGLReLLTGGEVVSPPHVR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 343 EKWKKITGVHLLEGYGLTECSPLVT----GNPYDLADySGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGY 418
Cdd:cd12117 268 RVLAACPGLRLVNGYGPTENTTFTTshvvTELDEVAG-SIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGY 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKEVINEEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHE 492
Cdd:cd12117 347 LNRPALTAERFVADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 493 VSGEVVKIYVVKRDPsLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd12117 427 GGDKRLVAYVVAEGA-LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
50-551 |
1.07e-53 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 191.65 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIavnVNPLYT---PRELEHQLNDADARAIV 126
Cdd:PRK04319 75 TYKELKELSNKFANVLK-ELGVEKGDRVFIFMPRIPELYFALLGALKNGAI---VGPLFEafmEEAVRDRLEDSEAKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 127 IVsnfANTLEQIVAN--TQVKHVVLtslgqmlprakgtlVDFVVKYVKGMVpkyDLPGAisMRKALHkgrrlQYVKPFMS 204
Cdd:PRK04319 151 TT---PALLERKPADdlPSLKHVLL--------------VGEDVEEGPGTL---DFNAL--MEQASD-----EFDIEWTD 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 GEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKgaYGPVLREGRELVVTALP------LYHVFALTVNcllfiemGGS 278
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGK--YVLDLHEDDVYWCTADPgwvtgtSYGIFAPWLN-------GAT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 279 NLLITNPRDIPGFVKELQKHP----FTAITGVNTLFNA---LVNNEDFHELNFAnmkLSVGGGM---AVqravaeKW-KK 347
Cdd:PRK04319 275 NVIDGGRFSPERWYRILEDYKvtvwYTAPTAIRMLMGAgddLVKKYDLSSLRHI---LSVGEPLnpeVV------RWgMK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRG--PQVMQGYWQRPEAT 425
Cdd:PRK04319 346 VFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKY 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 426 KEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR 505
Cdd:PRK04319 426 ESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALR 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 521099036 506 D---PSLT-KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PRK04319 505 PgyePSEElKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
211-552 |
2.09e-53 |
|
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: 188.36 E-value: 2.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 211 LQYTGGTTGVAKGaILthRNMVANVLQAKGAYGPVLREGRELVVTAL---PLYHVFALTVnCLLFIEMGGSnLLITNPRD 287
Cdd:cd05929 130 MLYSGGTTGRPKG-IK--RGLPGGPPDNDTLMAAALGFGPGADSVYLspaPLYHAAPFRW-SMTALFMGGT-LVLMEKFD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 288 IPGFVKELQKHPFTAITGVNTLFNAL--VNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPL 365
Cdd:cd05929 205 PEEFLRLIERYRVTFAQFVPTMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 366 VTGNPYDLADYSGAIGLPVPStEVRIVDDEGNVLNYGQTGELQVRGPQVMQgYWQRPEATKEVINEEGWLSTGDIVRFDE 445
Cdd:cd05929 285 TIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYLDE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 446 NGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYV----VKRDPSLTKDELITHCRKH 521
Cdd:cd05929 363 DGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAGTALAEELIAFLRDR 442
|
330 340 350
....*....|....*....|....*....|.
gi 521099036 522 LTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05929 443 LSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
48-561 |
2.59e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 189.14 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 48 VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVI 127
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 VSNFANTLEQIVANTqVKHVVLTSLGQMLPRAKGTLVDFVVKyvkgmvpkydlPGAISMRKALHKGRrlQYVKPfmSGED 207
Cdd:PRK12406 90 HADLLHGLASALPAG-VTVLSVPTPPEIAAAYRISPALLTPP-----------AGAIDWEGWLAQQE--PYDGP--PVPQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 IAFLQYTGGTTGVAKG---AILTHRNMVANVLQAKGAYGpvLREGRELVVTAlPLYH----VFALTVncllfIEMGGsnL 280
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGvrrAAPTPEQAAAAEQMRALIYG--LKPGIRALLTG-PLYHsapnAYGLRA-----GRLGG--V 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 281 LITNPR-DIPGFVKELQKHPFTAITGVNTLFNALV-------NNEDFHELNFanmklsVGGGMA-----VQRAVAEKWkk 347
Cdd:PRK12406 224 LVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLklpeevrAKYDVSSLRH------VIHAAApcpadVKRAMIEWW-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 itGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQ-GYWQRPEATK 426
Cdd:PRK12406 296 --GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 427 EvINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVkIYVVKRD 506
Cdd:PRK12406 374 E-IDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL-MAVVEPQ 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 507 PSLTKDE--LITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLAEQ 561
Cdd:PRK12406 452 PGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
50-552 |
4.61e-53 |
|
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: 189.24 E-value: 4.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd05970 49 TFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NfANTLEQIvantqvkhvvltslgqmlpraKGTLVDFVVKYVKGMVPKYDLPGAISMRKALHKG-----RRLQYVKPfmS 204
Cdd:cd05970 128 E-DNIPEEI---------------------EKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNAspdfeRPTANSYP--C 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 GEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKgaYGPVLRE-GRELVVTALPlyhvFALTVNCLLFIE-MGGSNLLI 282
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAK--YWQNVREgGLHLTVADTG----WGKAVWGKIYGQwIAGAAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TN-PRDIP-GFVKELQKHPFTAITGVNTLFNALVNnEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLT 360
Cdd:cd05970 258 YDyDKFDPkALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 361 ECSpLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQ-----VMQGYWQRPEATKEVINEeGWL 435
Cdd:cd05970 337 ETT-LTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHD-GYY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 436 STGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-----KRDPSLT 510
Cdd:cd05970 415 HTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgyEPSEELK 494
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 521099036 511 KdELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05970 495 K-ELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
14-552 |
1.25e-52 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 187.87 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 14 PETINPDQYLSLVEMFEQSVHKYADQ-PAFI-NMGSV--MTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPV 89
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRAAERGPTKgITYIdADGSEefQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 90 ALFGILRAGMIAVNVNPLYTPRELEHQLNDadaraiviVSNFANTLEQivantqvkHVVLTS---LGQMLPRAKGTLVDF 166
Cdd:cd05906 80 AFWACVLAGFVPAPLTVPPTYDEPNARLRK--------LRHIWQLLGS--------PVVLTDaelVAEFAGLETLSGLPG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 167 VVkyvkgmvpkydlpgAISMRKALHKGRrlQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANvLQAKGAYGPVL 246
Cdd:cd05906 144 IR--------------VLSIEELLDTAA--DHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR-SAGKIQHNGLT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 247 REGRELV------VTALPLYHVFAL-----TVNCLlfiemggSNLLITNPRDipgFVKELQKHPFTAITGVNTLFnALVN 315
Cdd:cd05906 207 PQDVFLNwvpldhVGGLVELHLRAVylgcqQVHVP-------TEEILADPLR---WLDLIDRYRVTITWAPNFAF-ALLN 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 316 N-----EDFHeLNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLE------GYGLTE-CSplvtGNPYDLADYSG----- 378
Cdd:cd05906 276 DlleeiEDGT-WDLSSLRYLVNAGEAVVAKTIRRLLRLLEPYGLPpdairpAFGMTEtCS----GVIYSRSFPTYdhsqa 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 379 ----AIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVrFDENGMIYIVDR 454
Cdd:cd05906 351 lefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGR 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 455 KKDMILVSGFNVYPNEIEDVV-----ALHGKVLeVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHLT---GYK 526
Cdd:cd05906 430 TKDTIIVNGVNYYSHEIEAAVeevpgVEPSFTA-AFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVSrevGVS 508
|
570 580
....*....|....*....|....*..
gi 521099036 527 VPKLIEF-REELPKTNVGKILRRVLRE 552
Cdd:cd05906 509 PAYLIPLpKEEIPKTSLGKIQRSKLKA 535
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
24-550 |
1.85e-52 |
|
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: 185.99 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 104 VNPLYTPRELEHQLNDADARAIVIVSNFAntleqivantQVKHVVLtslgqmlprakgtlvdfvvkyvkgmvpkydlpga 183
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIVPDRHA----------GFDHRAL---------------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 184 isMRKALHKGRrlqyvkpfmsgeDIAFLQYTGGTTGVAKGAILTHRNMVANVlqakGAYGPVLREGRELV-VTALPLYHV 262
Cdd:cd05920 131 --ARELAESIP------------EVALFLLSGGTTGTPKLIPRTHNDYAYNV----RASAEVCGLDQDTVyLAVLPAAHN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 263 FALTVNCLLFIEM-GGSNLLITNPRdiPGFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRA 340
Cdd:cd05920 193 FPLACPGVLGTLLaGGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 VAEKWKKITGVHLLEGYGLTEcsPLVT----GNPYDLADYSGaiGLPV-PSTEVRIVDDEGNVLNYGQTGELQVRGPQVM 415
Cdd:cd05920 271 LARRVPPVLGCTLQQVFGMAE--GLLNytrlDDPDEVIIHTQ--GRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 416 QGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSG 495
Cdd:cd05920 347 RGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLG 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 496 EVVKIYVVKRDPSLTKDELithcRKHLTG-----YKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05920 427 ERSCAFVVLRDPPPSAAQL----RRFLRErglaaYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
24-549 |
1.69e-51 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 190.52 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFIN-MGSVMTFRKLEERSRAFAAYLQNELKlkKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKRELK--DEENVGILLPPSVAGALANLALLLAGKVPV 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 103 NVNplYTPRE--LEHQLNDADARAIVIVSNFANTLEQIVANTQVKhvvltSLGQMLP----RAKGTLVDFVVKYVKGMVp 176
Cdd:PRK08633 694 NLN--YTASEaaLKSAIEQAQIKTVITSRKFLEKLKNKGFDLELP-----ENVKVIYledlKAKISKVDKLTALLAARL- 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 177 kydLPgaismrKALHKGRRLQYVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKgaygPVLR-EGRELVVT 255
Cdd:PRK08633 766 ---LP------ARLLKRLYGPTFKP----DDTATIIFSSGSEGEPKGVMLSHHNILSNIEQIS----DVFNlRNDDVILS 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 256 ALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGM 335
Cdd:PRK08633 829 SLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAE 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 336 AVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDL--ADYS-------GAIGLPVPSTEVRIVD-DEGNVLNYGQTG 405
Cdd:PRK08633 909 KLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPDVlaADFKrqtgskeGSVGMPLPGVAVRIVDpETFEELPPGEDG 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 406 ELQVRGPQVMQGYWQRPEATKEVINE---EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVA--LHGK 480
Cdd:PRK08633 989 LILIGGPQVMKGYLGDPEKTAEVIKDidgIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGGE 1068
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 481 VLEVAAIGQPHEVSGEvvKIYVVKRDPSLTKDELithcRKHLTGYKVPKL-----IEFREELPKTNVGKI-LRRV 549
Cdd:PRK08633 1069 EVVFAVTAVPDEKKGE--KLVVLHTCGAEDVEEL----KRAIKESGLPNLwkpsrYFKVEALPLLGSGKLdLKGL 1137
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
38-552 |
2.54e-51 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 184.19 E-value: 2.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQ-ALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIVANTqvkhvvltslgqmlPRAKgTLVDFVvkyvkgmvpkyDLPGAISMRK--ALHKGRR 195
Cdd:PRK13382 137 TREGVDTVIYDEEFSATVDRALADC--------------PQAT-RIVAWT-----------DEDHDLTVEVliAAHAGQR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 196 lqyvkPFMSGEDIAFLQYTGGTTGVAKGAiltHRNMVANVLQAKGAYGPVLREGRELVVTALPLYH-------VFALTVN 268
Cdd:PRK13382 191 -----PEPTGRKGRVILLTSGTTGTPKGA---RRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHawgfsqlVLAASLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 CLLfiemggsnllITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVN--NEDFHELNFANMKLSVGGGMAVQRAVAEKW 345
Cdd:PRK13382 263 CTI----------VTRRRfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 346 KKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYwqRPEAT 425
Cdd:PRK13382 333 MDQFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGST 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 426 KEVIneEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-K 504
Cdd:PRK13382 411 KDFH--DGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVlK 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 505 RDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK13382 489 PGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-552 |
1.47e-50 |
|
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: 176.75 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 207 DIAFLQYTGGTTGVAKGAILTHRNMVANVlQAKGAYGPVLREGRELVvtALPLYHV--FALTVNCLLfiemGGSNLLITN 284
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASA-AGLHSRLGFGGGDSWLL--SLPLYHVggLAILVRSLL----AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 285 PRDipGFVKELQKHPFTAITGVNT-LFNALVNNEDFHELnfANMKLSVGGGMAVQRAVAEKWKKiTGVHLLEGYGLTECS 363
Cdd:cd17630 74 RNQ--ALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPAAL--KSLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTETA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 364 PLVTGNPYDLADYSGAiGLPVPSTEVRIVDDegnvlnygqtGELQVRGPQVMQGYWQRPEatKEVINEEGWLSTGDIVRF 443
Cdd:cd17630 149 SQVATKRPDGFGRGGV-GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQL--VPEFNEDGWFTTKDLGEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 444 DENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVkIYVVKRDPSLTKDELITHCRKHLT 523
Cdd:cd17630 216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRP-VAVIVGRGPADPAELRAWLKDKLA 294
|
330 340
....*....|....*....|....*....
gi 521099036 524 GYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd17630 295 RFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-544 |
5.64e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 180.47 E-value: 5.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 28 MFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 108 YTPRELEHQLNDADARAIVIVSNFANTLEQIVANT-QVKHVVLTslgqmlprAKGTLVDFvvkyvkgmvpkydLPGAISM 186
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLpKLRTLVVV--------EDGSGNDL-------------LPGAVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 RKALHKGRRLQyvkPFM--SGEDIAFLqYTGGTTGVAKGAILTHRNMVANVLQAKGAY-GPVLREGRELVVTAL------ 257
Cdd:PRK07798 146 EDALAAGSPER---DFGerSPDDLYLL-YTGGTTGMPKGVMWRQEDIFRVLLGGRDFAtGEPIEDEEELAKRAAagpgmr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 258 -----PLYHVFAL--TVNCLLfieMGGSNLLITNPR-DIPGFVKELQKHPFTAITGVNT-----LFNALVNNEDFhelNF 324
Cdd:PRK07798 222 rfpapPLMHGAGQwaAFAALF---SGQTVVLLPDVRfDADEVWRTIEREKVNVITIVGDamarpLLDALEARGPY---DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 325 ANMKLSVGGGMAVQRAVAEKW-KKITGVHLLEGYGLTEcsplvTGNPYDLADYSGAIGLPVPSTEVR----IVDDEGNVL 399
Cdd:PRK07798 296 SSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSE-----TGFGGSGTVAKGAVHTGGPRFTIGprtvVLDEDGNPV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 400 --NYGQTGELQVRGPqVMQGYWQRPEATKE---VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDV 474
Cdd:PRK07798 371 epGSGEIGWIARRGH-IPLGYYKDPEKTAEtfpTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEA 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 475 VALHGKVLEVAAIGQPHEVSG-EVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGK 544
Cdd:PRK07798 450 LKAHPDVADALVVGVPDERWGqEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
26-550 |
7.56e-49 |
|
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: 176.31 E-value: 7.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 26 VEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVN 105
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 106 PLYTPRELEHQLNDADARaivivsnfantleqivantqvkhVVLTSLGQMLPRAKGTLVDFVVKYVKGMVPKydlpgais 185
Cdd:cd17646 80 PGYPADRLAYMLADAGPA-----------------------VVLTTADLAARLPAGGDVALLGDEALAAPPA-------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 186 mrkalhkGRRLQYVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYgPVLREGRELVVTALPlyhvFAL 265
Cdd:cd17646 129 -------TPPLVPPRP----DNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY-PLGPGDRVLQKTPLS----FDV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 266 TVNCLLFIEMGGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELnfANMKLSVGGGMAVQRAVA 342
Cdd:cd17646 193 SVWELFWPLVAGARLVVARPgghRDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGSC--ASLRRVFCSGEALPPELA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 343 EKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGA--IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQ 420
Cdd:cd17646 271 ARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 421 RPEATKE--VINEEGWLS----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVS 494
Cdd:cd17646 351 RPALTAErfVPDPFGPGSrmyrTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAG 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 495 GEVVKIYVVKRD--PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17646 431 AARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
41-561 |
1.63e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 176.86 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 41 AFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDA 120
Cdd:PRK06164 28 ALIDEDRPLSRAELRALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 121 DARAIVIVSNFANT-LEQIVANTQvkhvvltslGQMLPRAKGTlvdFVVKYVKGMVPKyDLPGAISMRKALHKGRRLQYV 199
Cdd:PRK06164 107 RARWLVVWPGFKGIdFAAILAAVP---------PDALPPLRAI---AVVDDAADATPA-PAPGARVQLFALPDPAPPAAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 200 KPFMSGEDIAFLQYT-GGTTGVAKGAILTHRNMVANVLQAKGAYGpvlREGRELVVTALPLYHVFALtvNCLLFIEMGGS 278
Cdd:PRK06164 174 GERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYG---YDPGAVLLAALPFCGVFGF--STLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 279 NLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDfHELNFANMKLSvgGGMAVQRAVAE--KWKKITGVHLLEG 356
Cdd:PRK06164 249 PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLF--GFASFAPALGElaALARARGVPLTGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVTGNPYDL--ADYSGAIGLPV-PSTEVRIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEE 432
Cdd:PRK06164 326 YGSSEVQALVALQPATDpvSVRIEGGGRPAsPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 433 GWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKD 512
Cdd:PRK06164 406 GYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDGASPDEA 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 521099036 513 ELITHCRKHLTGYKVPKLIEFREELPKT---NVGKILRRVLREENDAQLAEQ 561
Cdd:PRK06164 486 GLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLREMAQARLAAE 537
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-551 |
4.07e-48 |
|
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: 173.47 E-value: 4.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYT---PRELEHQLNDADARai 125
Cdd:cd05973 1 LTFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 VIVSNFANtleqivantqvkhvvltslgqmlpRAKGTlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsg 205
Cdd:cd05973 75 LVVTDAAN------------------------RHKLD------------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVAnvLQAKGAYGPVLREGRELVVTALP--LYHVFALTVNCLLfieMGGSNLLIT 283
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAVDLRPEDSFWNAADPgwAYGLYYAITGPLA---LGHPTILLE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 NPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEdfhelnfANMKLSVGGGMAVQRAVAE-------KWKKIT-GVHLLE 355
Cdd:cd05973 163 GGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAG-------AEVPARPKGRLRRVSSAGEpltpeviRWFDAAlGVPIHD 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 356 GYGLTECSpLVTGNPYDLAD--YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQV---RGPQV-MQGYWQRPEATKEvi 429
Cdd:cd05973 236 HYGQTELG-MVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAID-- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 neEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD--- 506
Cdd:cd05973 313 --GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGghe 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 521099036 507 --PSLTkDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05973 391 gtPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
23-561 |
4.16e-48 |
|
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: 180.44 E-value: 4.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 23 LSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:COG1020 476 ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 103 NVNPLYtPRE-LEHQLNDADARAIVIVSNFANTLeqivANTQVKHVVLTSLGqmLPRAKGTLVDFVVkyvkgmvpkydlp 181
Cdd:COG1020 555 PLDPAY-PAErLAYMLEDAGARLVLTQSALAARL----PELGVPVLALDALA--LAAEPATNPPVPV------------- 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 182 gaismrkalhkgrrlqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREGRELVVTALplyh 261
Cdd:COG1020 615 ----------------------TPDDLAYVIYTSGSTGRPKGVMVEHRA-LVNLLAWMQRRYGLGPGDRVLQFASL---- 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 262 VF---------ALTVncllfiemGGSnLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVnneDFHELNFANMKL 329
Cdd:COG1020 668 SFdasvweifgALLS--------GAT-LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRL 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 330 SVGGGMAVQRAVAEKWKKIT-GVHLLEGYGLTECSPLVTGNPYDLADYSGA---IGLPVPSTEVRIVDDEGNVLNYGQTG 405
Cdd:COG1020 736 VLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGGsvpIGRPIANTRVYVLDAHLQPVPVGVPG 815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 406 ELQVRGPQVMQGYWQRPEATKE--VINEEGWLS-----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALH 478
Cdd:COG1020 816 ELYIGGAGLARGYLNRPELTAErfVADPFGFPGarlyrTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQH 895
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 479 GKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITHC-RKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQ 557
Cdd:COG1020 896 PGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
....
gi 521099036 558 LAEQ 561
Cdd:COG1020 976 AAAA 979
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
213-540 |
1.94e-47 |
|
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: 168.63 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 213 YTGGTTGVAKGAILTHRNMVANVLQAkgAYGPVLREGrELVVTALPLYHVFALTVNCLLFIeMGGSNLLI--TNPRDIPG 290
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALVL--AVLQAIDEG-TVFLNSGPLFHIGTLMFTLATFH-AGGTNVFVrrVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 291 FV-KELQKHPFtaitgvntLFNALVnnEDFHELNFANMK-LSvggGMAVQRAVAEKWKKIT-----GVHLLEGYGLTECS 363
Cdd:cd17636 83 LIeAERCTHAF--------LLPPTI--DQIVELNADGLYdLS---SLRSSPAAPEWNDMATvdtspWGRKPGGYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 364 PLVTGNPYDLADYSGAiGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEatkevINEE----GWLSTGD 439
Cdd:cd17636 150 GLATFAALGGGAIGGA-GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPE-----VNARrtrgGWHHTND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 440 IVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVK-IYVVKRDPSLTKDELITHC 518
Cdd:cd17636 224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKaIVVLKPGASVTEAELIEHC 303
|
330 340
....*....|....*....|..
gi 521099036 519 RKHLTGYKVPKLIEFREELPKT 540
Cdd:cd17636 304 RARIASYKKPKSVEFADALPRT 325
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-553 |
3.72e-47 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 173.01 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVANtqvkhvvltslgqmLPRAKgtlvDFVVKYVKGMVPKYDLPGAISMRKALhKGRRLQYVKPFMSGEDIA 209
Cdd:PRK06018 120 TFVPILEKIADK--------------LPSVE----RYVVLTDAAHMPQTTLKNAVAYEEWI-AEADGDFAWKTFDENTAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRnmvANVLQAKGAYGP-VLREG-RELVVTALPLYHVFA--LTVNCllfiEMGGSNLLITNP 285
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHR---SNVLHALMANNGdALGTSaADTMLPVVPLFHANSwgIAFSA----PSMGTKLVMPGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKEL---QKHPFTAitGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHLLEGYGLTEC 362
Cdd:PRK06018 254 KLDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 SPLVT----GNPYDLADYSGAI------GLPVPSTEVRIVDDEGNVLNY-GQT-GELQVRGPQVMQGYWQrpeATKEVIN 430
Cdd:PRK06018 331 SPLGTlaalKPPFSKLPGDARLdvlqkqGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYR---VDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE-VVKIYVVKRDPSL 509
Cdd:PRK06018 408 DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErPLLIVQLKPGETA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 521099036 510 TKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK06018 488 TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-550 |
1.60e-46 |
|
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: 169.35 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 35 KYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPlYTPREle 114
Cdd:cd05945 3 ANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSPAE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 115 hqlndadaRaivivsnfantLEQIVANtqvkhvvltslgqmlprAKGTLVdfvvkyvkgmvpkydlpgaismrkalhkgr 194
Cdd:cd05945 79 --------R-----------IREILDA-----------------AKPALL------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 195 rlqyvkpFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVA--NVLQAKGAYGPvlregrELVVTALPLYHvFALTVN---- 268
Cdd:cd05945 93 -------IADGDDNAYIIFTSGSTGRPKGVQISHDNLVSftNWMLSDFPLGP------GDVFLNQAPFS-FDLSVMdlyp 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 CLLfieMGGSnlLITNPRDIPGFVKEL----QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEK 344
Cdd:cd05945 159 ALA---SGAT--LVPVPRDATADPKQLfrflAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 345 WKKIT-GVHLLEGYGLTECSPLVTGN---PYDLADY-SGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYW 419
Cdd:cd05945 234 LQQRFpDARIYNTYGPTEATVAVTYIevtPEVLDGYdRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYL 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 420 QRPEATKEVIN-EEGWLS--TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE 496
Cdd:cd05945 314 NNPEKTAAAFFpDEGQRAyrTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 497 VVKIYVVKRDPSLTKD--ELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd05945 394 ELIAFVVPKPGAEAGLtkAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-488 |
2.38e-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: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFA-AYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYtpreleHQLNdadaraivi 127
Cdd:cd05927 6 ISYKEVAERADNIGsALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLY------DTLG--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 vsnfANTLEQIVANTQVKHVvltslgqmlprakgtlvdFVVKYVKgmvpkydlpgAISMRKALHKGRRLQYVKPFMSGED 207
Cdd:cd05927 68 ----PEAIEYILNHAEISIV------------------FCDAGVK----------VYSLEEFEKLGKKNKVPPPPPKPED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 IAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGRELV-VTALPLYHVFALTVNCLLFIEMGGSNLLITNPR 286
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyISYLPLAHIFERVVEALFLYHGAKIGFYSGDIR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIPGFVKELQkhPfTAITGV----------------------NTLFNALVNNEDFH-------------ELNFANMKLSV 331
Cdd:cd05927 196 LLLDDIKALK--P-TVFPGVprvlnriydkifnkvqakgplkRKLFNFALNYKLAElrsgvvraspfwdKLVFNKIKQAL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 332 G--------GGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVT-GNPYDLAdySGAIGLPVPSTEVRIVDdegnV--LN 400
Cdd:cd05927 273 GgnvrlmltGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATlTLPGDTS--VGHVGGPLPCAEVKLVD----VpeMN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 401 Y-----GQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMI-LVSGFNVYPNEIEDV 474
Cdd:cd05927 347 YdakdpNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENI 426
|
490 500
....*....|....*....|...
gi 521099036 475 VAL---------HGKVLEVAAIG 488
Cdd:cd05927 427 YARspfvaqifvYGDSLKSFLVA 449
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
50-553 |
3.37e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 170.27 E-value: 3.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:PRK07008 41 TYRDCERRAKQLAQAL-AALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVAN-TQVKHVVLTSLGQMLPRAKGTLVDFvvkyvkgmvpkydlpgaismrKALHKGRRLQYVKPFMSGEDI 208
Cdd:PRK07008 120 TFLPLVDALAPQcPNVKGWVAMTDAAHLPAGSTPLLCY---------------------ETLVGAQDGDYDWPRFDENQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRnmvANVLQAKGAYGP-VLR-EGRELVVTALPLYHVFA--LTVNCllfiEMGGSNLLITN 284
Cdd:PRK07008 179 SSLCYTSGTTGNPKGALYSHR---STVLHAYGAALPdAMGlSARDAVLPVVPMFHVNAwgLPYSA----PLTGAKLVLPG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 285 PrDIPG-FVKEL---QKHPFTAitGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLT 360
Cdd:PRK07008 252 P-DLDGkSLYELieaERVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 361 ECSPLVT-----GNPYDLA-DYSGAI----GLPVPSTEVRIVDDEGNVLNY-GQT-GELQVRGPQVMQGYWQRpEATKEV 428
Cdd:PRK07008 329 EMSPLGTlcklkWKHSQLPlDEQRKLlekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG-DASPLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 429 ineEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR-DP 507
Cdd:PRK07008 408 ---DGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRpGA 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 521099036 508 SLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK07008 485 EVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-553 |
6.22e-43 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 161.21 E-value: 6.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGS--VMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIA 101
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 102 VNVNPLYTPRELEHQLNDADARAIVIVSNFANtleQIVANTQVKHVVLTSLGQMLPRAKGTLVdfvvkyvkgmvPKYDLP 181
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVVLIDADGPH---DRAEPTTRWWPLTVNVGGDSGPSGGTLS-----------VHLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 182 GAISMRKALHKGRRlqyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAY--GPvlregRELVVTALPL 259
Cdd:PRK05852 162 TEPTPATSTPEGLR----------PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYrlSP-----RDATVAVMPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 260 YHVFALTVNCLLFIEMGGSNLLITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSV--GGGMA 336
Cdd:PRK05852 227 YHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFirSCSAP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYS----GAIGLPVPST--EVRIVDDEGNVLNYGQTGELQVR 410
Cdd:PRK05852 307 LTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEVINEeGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK05852 387 GTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 491 HEVSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK05852 466 DQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
201-547 |
1.12e-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: 155.26 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 201 PFMSGediaflqYTGGTTGVAKGAILTHRN-MVANVLQAKGAYgpvlREGRELVVTALPLyhVFALTVNCLLFIEMGGSN 279
Cdd:cd17633 2 PFYIG-------FTSGTTGLPKAYYRSERSwIESFVCNEDLFN----ISGEDAILAPGPL--SHSLFLYGAISALYLGGT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 280 LLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNnEDFHELNfanMKLSVGGGMAVQRAVAEKWKKIT-GVHLLEGYG 358
Cdd:cd17633 69 FIGQRKFNPKSWIRKINQYNATVIYLVPTMLQALAR-TLEPESK---IKSIFSSGQKLFESTKKKLKNIFpKANLIEFYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 359 LTECSpLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLnygqtGELQVRGPQVMQGYwqrpeATKEVINEEGWLSTG 438
Cdd:cd17633 145 TSELS-FITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGY-----VRGGFSNPDGWMSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 439 DIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVkIYVVKRDpSLTKDELITHC 518
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFL 291
|
330 340
....*....|....*....|....*....
gi 521099036 519 RKHLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:cd17633 292 KQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
27-552 |
1.96e-42 |
|
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: 158.47 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPA-FINMGSvMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVN 105
Cdd:cd05918 3 DLIEERARSQPDAPAvCAWDGS-LTYAELDRLSSRLAHHLR-SLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 106 PLYtPRElehqlndadaRaivivsnfantLEQIVANTQVKhVVLTSlgqmlprakgtlvdfvvkyvkgmvpkydlpgais 185
Cdd:cd05918 81 PSH-PLQ----------R-----------LQEILQDTGAK-VVLTS---------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 186 mrkalhkgrrlqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLqakgAYGPVLREGRELVVTA-------LP 258
Cdd:cd05918 104 ------------------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSAL----AHGRALGLTSESRVLQfasytfdVS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 259 LYHVF-ALTVNCLLFIemgGSNLLITNprDIPGFVKELQkhpftaitgVNTLF-----NALVNNEDFHELnfanmKLSVG 332
Cdd:cd05918 162 ILEIFtTLAAGGCLCI---PSEEDRLN--DLAGFINRLR---------VTWAFltpsvARLLDPEDVPSL-----RTLVL 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 333 GGMAVQRAVAEKWKKitGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTeVRIVD--DEGNVLNYGQTGELQVR 410
Cdd:cd05918 223 GGEALTQSDVDTWAD--RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIE 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEV-INEEGWLS------------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVV-- 475
Cdd:cd05918 300 GPILARGYLNDPEKTAAAfIEDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLrq 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 476 ALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKD-------------------ELITHCRKHLTGYKVPKLIEFREE 536
Cdd:cd05918 380 SLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSH 459
|
570
....*....|....*.
gi 521099036 537 LPKTNVGKILRRVLRE 552
Cdd:cd05918 460 LPLTASGKIDRRALRE 475
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
48-551 |
3.26e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 158.02 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 48 VMTFRKLEERSRAFAAYLQNelKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVI 127
Cdd:PRK07638 26 VLTYKDWFESVCKVANWLNE--KESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 VSNFANTLeqivantqvkhvvltslgqmlPRAKGTLVDfvVKYVKGMVPKYdLPgaismrkALHKGRRLQYvKPFMSGed 207
Cdd:PRK07638 104 ERYKLNDL---------------------PDEEGRVIE--IDEWKRMIEKY-LP-------TYAPIENVQN-APFYMG-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 iaflqYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVTALPLYHVFALTVNCLLfieMGGSnlLITNPRD 287
Cdd:PRK07638 150 -----FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFH-MKREDSVLIAGTLVHSLFLYGAISTLY---VGQT--VHLMRKF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 288 IPGFVKE-LQKHPFTAITGVNTLFNALVNNEDFHElnfANMKLSVGGgmAVQRAVAEKWKKITGVH--LLEGYGLTECSP 364
Cdd:PRK07638 219 IPNQVLDkLETENISVMYTVPTMLESLYKENRVIE---NKMKIISSG--AKWEAEAKEKIKNIFPYakLYEFYGASELSF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 365 LVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEvINEEGWLSTGDIVRFD 444
Cdd:PRK07638 294 VTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYED 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 445 ENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVvkrDPSLTKDELITHCRKHLTG 524
Cdd:PRK07638 373 EEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQLKSFCLQRLSS 449
|
490 500
....*....|....*....|....*..
gi 521099036 525 YKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PRK07638 450 FKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
17-553 |
3.66e-42 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 160.04 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 17 INPDQYLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILR 96
Cdd:PRK08279 31 ITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAA-ARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 97 AGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVkHVVLTSLGQMLPRAKGTLVDfvvkyVKGMvp 176
Cdd:PRK08279 110 LGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLAR-PPRLWVAGGDTLDDPEGYED-----LAAA-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 177 kydLPGAISMRKALHKGrrlqyvkpfMSGEDIAFLQYTGGTTGVAKGAILTHRnmvaNVLQAKGAYGPVLREGRELVV-T 255
Cdd:PRK08279 182 ---AAGAPTTNPASRSG---------VTAKDTAFYIYTSGTTGLPKAAVMSHM----RWLKAMGGFGGLLRLTPDDVLyC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 256 ALPLYHVFALTVnCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVN-----NEDFHELnfanmKLS 330
Cdd:PRK08279 246 CLPLYHNTGGTV-AWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNqppkpTDRDHRL-----RLM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 331 VGGGMavQRAVAEKWKKITGV-HLLEGYGLTEC----------------SPLVTGNPYDLADYSGAIGLPvpsteVRivD 393
Cdd:PRK08279 320 IGNGL--RPDIWDEFQQRFGIpRILEFYAASEGnvgfinvfnfdgtvgrVPLWLAHPYAIVKYDVDTGEP-----VR--D 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 394 DEGNVL--NYGQTGEL--QVRGPQVMQGYWQrPEATKEVI----NEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSG 463
Cdd:PRK08279 391 ADGRCIkvKPGEVGLLigRITDRGPFDGYTD-PEASEKKIlrdvFKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 464 FNVYPNEIEDVVALHGKVLEVAAIGqphevsgevVKI-----------YVVKRDPSLTKDELITHCRKHLTGYKVPKLIE 532
Cdd:PRK08279 470 ENVATTEVENALSGFPGVEEAVVYG---------VEVpgtdgragmaaIVLADGAEFDLAALAAHLYERLPAYAVPLFVR 540
|
570 580
....*....|....*....|.
gi 521099036 533 FREELPKTNVGKILRRVLREE 553
Cdd:PRK08279 541 LVPELETTGTFKYRKVDLRKE 561
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-550 |
7.45e-42 |
|
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: 156.31 E-value: 7.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVivsnfantleqivanTQvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlq 197
Cdd:cd17643 81 ADSGPSLLL---------------TD------------------------------------------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVAnvLQAkgAYGPVLREGRELVVTalpLYHVFALTVNCLlfiEMGG 277
Cdd:cd17643 92 -------PDDLAYVIYTSGSTGRPKGVVVSHANVLA--LFA--ATQRWFGFNEDDVWT---LFHSYAFDFSVW---EIWG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SNL----LITNPRDI---PGFVKELQKHpfTAITGVN---TLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKK 347
Cdd:cd17643 155 ALLhggrLVVVPYEVarsPEDFARLLRD--EGVTVLNqtpSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ITGV---HLLEGYGLTECSPLVTGNPYDLADYSGA----IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQ 420
Cdd:cd17643 233 RFGLdrpQLVNMYGITETTVHVTFRPLDAADLPAAaaspIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLG 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 421 RPEATKE--VINEEGWLS-----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEV 493
Cdd:cd17643 313 RPELTAErfVANPFGGPGsrmyrTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEP 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 494 SGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17643 393 GDTRLVAYVVADDGAaADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
206-553 |
8.36e-42 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 158.42 E-value: 8.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLqAKGA---YGpvlrEGRELVVTAlPLYHVFALTvNCLLFIEMGGSNLLI 282
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSL-AKIAivgYG----EDDVYLHTA-PLCHIGGLS-SALAMLMVGACHVLL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 tnprdiPGF-----VKELQKHPFTAITGVNTLFNALV-------NNEDFHELnfanMKLSVGGGMAVQRAVAEKWKKITG 350
Cdd:PLN02860 245 ------PKFdakaaLQAIKQHNVTSMITVPAMMADLIsltrksmTWKVFPSV----RKILNGGGSLSSRLLPDAKKLFPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 351 VHLLEGYGLTE-CSPL------------------VTGNPYDLAD--YSGA-IGLPVPSTEVRIVDDEGNvlnygQTGELQ 408
Cdd:PLN02860 315 AKLFSAYGMTEaCSSLtfmtlhdptlespkqtlqTVNQTKSSSVhqPQGVcVGKPAPHVELKIGLDESS-----RVGRIL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 409 VRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIG 488
Cdd:PLN02860 390 TRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 489 QPHEVSGEVVKIYVVKRDP---------------SLTKDELITHCR-KHLTGYKVPKLI-EFREELPKTNVGKILRRVLR 551
Cdd:PLN02860 470 VPDSRLTEMVVACVRLRDGwiwsdnekenakknlTLSSETLRHHCReKNLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVR 549
|
..
gi 521099036 552 EE 553
Cdd:PLN02860 550 RE 551
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-551 |
3.73e-41 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 159.95 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQNELKLkkGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPREL--EHQ------L 117
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESArrHHQerllsiI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIvantqvKHVVLTSLGQMLprakgtLVDfvvkyvkgmvpkyDLPGAISMRkalhkgrrlq 197
Cdd:PRK05691 113 ADAEPRLLLTVADLRDSLLQM------EELAAANAPELL------CVD-------------TLDPALAEA---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 YVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGrELVVTALPLYHVFALTVNCLLFIEMGG 277
Cdd:PRK05691 158 WQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPD-DVIVSWLPLYHDMGLIGGLLQPIFSGV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SNLLITnprdiPGF-----VKELQ--KHPFTAITG----VNTLFNALVNNEDFHELNFANMKLSVGGGMAVQ----RAVA 342
Cdd:PRK05691 237 PCVLMS-----PAYflerpLRWLEaiSEYGGTISGgpdfAYRLCSERVSESALERLDLSRWRVAYSGSEPIRqdslERFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 343 EKWKK--ITGVHLLEGYGLTECSPLVTGNP---------YDLADYS--------GAI----GLPVPSTEVRIVD-DEGNV 398
Cdd:PRK05691 312 EKFAAcgFDPDSFFASYGLAEATLFVSGGRrgqgipaleLDAEALArnraepgtGSVlmscGRSQPGHAVLIVDpQSLEV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPEAT-KEVINEEG--WLSTGDIvRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDV- 474
Cdd:PRK05691 392 LGDNRVGEIWASGPSIAHGYWRNPEASaKTFVEHDGrtWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTv 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 475 -----VALHGKVLEVA-------AIGQPHEVSGEVVKIyvvkrdpsLTKDELITHCRKHLTG--YKVPKLIEFRE--ELP 538
Cdd:PRK05691 471 ereveVVRKGRVAAFAvnhqgeeGIGIAAEISRSVQKI--------LPPQALIKSIRQAVAEacQEAPSVVLLLNpgALP 542
|
570
....*....|...
gi 521099036 539 KTNVGKILRRVLR 551
Cdd:PRK05691 543 KTSSGKLQRSACR 555
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
47-552 |
4.07e-41 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 156.48 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 47 SVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGIlrAGMIAVnVNPL---YTPRELEHQLNDADAR 123
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAV--ACMGAV-FNPLnkqLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 124 AIVIVSNFANTLEQIVANT-QVKHVVLTSlgqmlprakGTLVDFVVKYVKGMVPKYDLpgaismrKALHKGRRLQYVKPF 202
Cdd:PRK05620 114 VIVADPRLAEQLGEILKECpCVRAVVFIG---------PSDADSAAAHMPEGIKVYSY-------EALLDGRSTVYDWPE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 MSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGrELVVTALPLYHVFALTVNCLLFieMGGSNLLI 282
Cdd:PRK05620 178 LDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHG-ESFLCCVPIYHVLSWGVPLAAF--MSGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNPR-DIPGFVKELQ-KHPFTAiTGVNTLFNALVnnedFHELNFANMKLSV----GGGMAVQRAVAEKWKKITGVHLLEG 356
Cdd:PRK05620 255 PGPDlSAPTLAKIIAtAMPRVA-HGVPTLWIQLM----VHYLKNPPERMSLqeiyVGGSAVPPILIKAWEERYGVDVVHV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPL---------VTGNPYDLADYSGAiGLPVpSTEVRIVDDeGNVLNYG--QTGELQVRGPQVMQGYWQRP--- 422
Cdd:PRK05620 330 WGMTETSPVgtvarppsgVSGEARWAYRVSQG-RFPA-SLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPtee 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 423 -------------EATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQ 489
Cdd:PRK05620 407 gggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGY 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 490 PHEVSGE----VVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKI----LRRVLRE 552
Cdd:PRK05620 487 PDDKWGErplaVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLAD 557
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-551 |
6.04e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 154.78 E-value: 6.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFI--NMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEH 115
Cdd:PRK13390 12 DRPAVIvaETGEQVSYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 116 QLNDADARAIVIvsnfANTLEQIVANTQVKHVVLTSLGQmlpRAKGtLVDFVVKYVKGMVPKYDLP-GAISMrkalhkgr 194
Cdd:PRK13390 91 IVGDSGARVLVA----SAALDGLAAKVGADLPLRLSFGG---EIDG-FGSFEAALAGAGPRLTEQPcGAVML-------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 195 rlqyvkpfmsgediaflqYTGGTTGVAKG--AILTHRNMVAN----VLQAKGAYGPvlrEGRELVVTALPLYHVFALTVn 268
Cdd:PRK13390 155 ------------------YSSGTTGFPKGiqPDLPGRDVDAPgdpiVAIARAFYDI---SESDIYYSSAPIYHAAPLRW- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 CLLFIEMGGSnLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALV--NNEDFHELNFANMKLSVGGGMAVQRAVAEKWK 346
Cdd:PRK13390 213 CSMVHALGGT-VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 347 KITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTeVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATK 426
Cdd:PRK13390 292 DWLGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 427 EVINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYV-- 502
Cdd:PRK13390 371 AAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIql 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 521099036 503 ---VKRDPSLTKdELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PRK13390 451 vegIRGSDELAR-ELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-551 |
9.14e-41 |
|
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: 156.11 E-value: 9.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGS-----VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIA 101
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 102 VNVNPLYTPRELEHQLNDADARAIVIVSNFA----------NTLEQIVANTQVKHVVLT-SLGQMLPRAKGTlvdfvvky 170
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkeEADKACAQCPTVEKVVVVrHLGNDFTPAKGR-------- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 171 vkgmvpkyDLPGAISMRKALHKGRRLQYVKPFMsgediafLQYTGGTTGVAKGAILTHrnMVANVLQAKGAYGPV-LREG 249
Cdd:cd05968 216 --------DLSYDEEKETAGDGAERTESEDPLM-------IIYTSGTTGKPKGTVHVH--AGFPLKAAQDMYFQFdLKPG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 250 RELV-VTAL-----PLYHVFALTVNCLLFIEMGgsnllitnprdIPGFVKELQ------KHPFTAITGVNTLFNALVNNE 317
Cdd:cd05968 279 DLLTwFTDLgwmmgPWLIFGGLILGATMVLYDG-----------APDHPKADRlwrmveDHEITHLGLSPTLIRALKPRG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 318 DFHELNFANMKLSVGGGmavqraVAEKWKKITGVHLLEGYGL-----------TECSPLVTGN----PYDLADYSGaigl 382
Cdd:cd05968 348 DAPVNAHDLSSLRVLGS------TGEPWNPEPWNWLFETVGKgrnpiinysggTEISGGILGNvlikPIKPSSFNG---- 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 383 PVPSTEVRIVDDEGNVLNyGQTGELQVRGPQV--MQGYWQRPEATKEVINE--EGWLSTGDIVRFDENGMIYIVDRKKDM 458
Cdd:cd05968 418 PVPGMKADVLDESGKPAR-PEVGELVLLAPWPgmTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRSDDT 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 459 ILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-----PSLtKDELITHCRKHLTGYKVPKLIEF 533
Cdd:cd05968 497 INVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEAL-AEELMERVADELGKPLSPERILF 575
|
570
....*....|....*...
gi 521099036 534 REELPKTNVGKILRRVLR 551
Cdd:cd05968 576 VKDLPKTRNAKVMRRVIR 593
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-551 |
1.12e-40 |
|
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: 154.04 E-value: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 29 FEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLR-ARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 109 TPRELEHQLNDADARAIVIVSNFANTLEQivantqvkhvvltslgqmlPRAKGTLVDfvvkyvkgmVPKYDLPGAISMRK 188
Cdd:cd17651 80 PAERLAFMLADAGPVLVLTHPALAGELAV-------------------ELVAVTLLD---------QPGAAAGADAEPDP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 189 ALHKGrrlqyvkpfmsgeDIAFLQYTGGTTGVAKGAILTHRnMVANVLQAKGAYGPVLREGRELVvTALPLYHVFALTVN 268
Cdd:cd17651 132 ALDAD-------------DLAYVIYTSGSTGRPKGVVMPHR-SLANLVAWQARASSLGPGARTLQ-FAGLGFDVSVQEIF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 CLLfieMGGSNLLITNPR---DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMK-LSVGG-GMAVQRAVAE 343
Cdd:cd17651 197 STL---CAGATLVLPPEEvrtDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRyLLTGGeQLVLTEDLRE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKKITGVHLLEGYGLTEcSPLVTGN--PYDLADYSGA--IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYW 419
Cdd:cd17651 274 FCAGLPGLRLHNHYGPTE-THVVTALslPGDPAAWPAPppIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 420 QRPEATKEVINEEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEV 493
Cdd:cd17651 353 NRPELTAERFVPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 494 SGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd17651 433 GEKRLVAYVVgDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-537 |
1.59e-40 |
|
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: 153.78 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIvivs 129
Cdd:cd05932 8 TWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nFANTLEqivANTQVKHVVLTSLGQMLprakgtlvdfvvkyvkgmVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIA 209
Cdd:cd05932 83 -FVGKLD---DWKAMAPGVPEGLISIS------------------LPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVanvLQAKGAYGPVLREGRELVVTALPLYHVFALTvncllFIEMGG--SNLLITNPRD 287
Cdd:cd05932 141 TLIYTSGTTGQPKGVMLTFGSFA---WAAQAGIEHIGTEENDRMLSYLPLAHVTERV-----FVEGGSlyGGVLVAFAES 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 288 IPGFVKELQKHPFTAITGVN---TLF----------------------NALVNNEDFHELNFANMKLSVGGGMAVQRAVA 342
Cdd:cd05932 213 LDTFVEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkipvvNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 343 EkWKKITGVHLLEGYGLTECSPLVTGNpYDLADYSGAIGLPVPSTEVRIVDDegnvlnygqtGELQVRGPQVMQGYWQRP 422
Cdd:cd05932 293 E-WYRSLGLNILEAYGMTENFAYSHLN-YPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 423 EATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS-GFNVYPNEIEDVVALHGKVLEVAAIG--QPHEVSGEVVK 499
Cdd:cd05932 361 EATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGsgLPAPLALVVLS 440
|
490 500 510
....*....|....*....|....*....|....*...
gi 521099036 500 IYVVKRDPSLTKDELITHCRKHLTGykVPKLIEFREEL 537
Cdd:cd05932 441 EEARLRADAFARAELEASLRAHLAR--VNSTLDSHEQL 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-561 |
1.29e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 155.50 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 7 SRYPSDvpetinpdqyLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQ 86
Cdd:PRK12316 4545 AGYPAT----------RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAE 4613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 87 YPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDADARAIVivsnfantleqivanTQvkhvvlTSLGQMLPRAKGTLVD 165
Cdd:PRK12316 4614 MMVGLLAVLKAGGAYVPLDPEY-PRErLAYMMEDSGAALLL---------------TQ------SHLLQRLPIPDGLASL 4671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 166 FVvkyvkgmvpkyDLPGAISMRKALHKGRRLQyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpV 245
Cdd:PRK12316 4672 AL-----------DRDEDWEGFPAHDPAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYE-L 4732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 246 LREGRELVVTALPlyhvFALTVNCLLFIEMGGSNLLITNPR--DIPGFVKELQKHPFTAITGVNTLFNALVNNeDFHELN 323
Cdd:PRK12316 4733 TPDDRVLQFMSFS----FDGSHEGLYHPLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEH-AERDGE 4807
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 324 FANMKLSVGGGMAVQRA-VAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADYSGA----IGLPVPSTEVRIVDDEGNV 398
Cdd:PRK12316 4808 PPSLRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACGAaympIGTPLGNRSGYVLDGQLNP 4887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPEATKE-----VINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEI 471
Cdd:PRK12316 4888 LPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEI 4967
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 472 EDVVALHGKVLEVAAIGQPHEVSGEVVKiYVVKRDPSLT---------KDELITHCRKHLTGYKVPKLIEFREELPKTNV 542
Cdd:PRK12316 4968 EARLREHPAVREAVVIAQEGAVGKQLVG-YVVPQDPALAdadeaqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPN 5046
|
570
....*....|....*....
gi 521099036 543 GKILRRVLrEENDAQLAEQ 561
Cdd:PRK12316 5047 GKLDRKAL-PQPDASLLQQ 5064
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-545 |
4.39e-39 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 153.20 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQNELKLkkGDRVALMMPNLLQYPVALFGILRAGMIAVNVNplYTprelehqlndADARAI 125
Cdd:PRK06814 656 NGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FS----------AGIANI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 VIVSNFAntleqivantQVKhVVLTSlGQMLPRAK-GTLVDFVVKYVKgMVPKYDLPGAISMR---KALHKGRRLQYVKP 201
Cdd:PRK06814 722 LSACKAA----------QVK-TVLTS-RAFIEKARlGPLIEALEFGIR-IIYLEDVRAQIGLAdkiKGLLAGRFPLVYFC 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 202 FMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQ--AKGAYGPvlregRELVVTALPLYHVFALTVNCLLFIEMGGSN 279
Cdd:PRK06814 789 NRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQvaARIDFSP-----EDKVFNALPVFHSFGLTGGLVLPLLSGVKV 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 280 LLITNP---RDIPGFVKELQKhpfTAITGVNTLFNALVNNEdfHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEG 356
Cdd:PRK06814 864 FLYPSPlhyRIIPELIYDTNA---TILFGTDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEG 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVTGN-PydLADYSGAIGLPVPSTEVRIVDDEGnvLNYGqtGELQVRGPQVMQGYWqRPEATKeVIN--EEG 433
Cdd:PRK06814 939 YGVTETAPVIALNtP--MHNKAGTVGRLLPGIEYRLEPVPG--IDEG--GRLFVRGPNVMLGYL-RAENPG-VLEppADG 1010
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEvvKIYVVKRDPSLTKDE 513
Cdd:PRK06814 1011 WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE--RIILLTTASDATRAA 1088
|
490 500 510
....*....|....*....|....*....|...
gi 521099036 514 LITHCRKH-LTGYKVPKLIEFREELPKTNVGKI 545
Cdd:PRK06814 1089 FLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-558 |
6.45e-39 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 150.79 E-value: 6.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 33 VHKYADQPAFI------NMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd05966 63 LKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLK-SLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVIVSNF----------ANTLEQIVANTQVKHVVltslgqMLPRAKGTLVdfvvkyvkgMVP 176
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGGyrggkviplkEIVDEALEKCPSVEKVL------VVKRTGGEVP---------MTE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 177 KYDLPGAISMRKALhkgrrlQYVKP-FMSGEDIAFLQYTGGTTGVAKG-----------AILTHRNmvanVLQAK----- 239
Cdd:cd05966 207 GRDLWWHDLMAKQS------PECEPeWMDSEDPLFILYTSGSTGKPKGvvhttggyllyAATTFKY----VFDYHpddiy 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 240 --------------GAYGP-------VLREGrelvvtaLPLYHVFALTVNcllFIEMGGSNLLITNPRDIPGFVKELQKH 298
Cdd:cd05966 277 wctadigwitghsyIVYGPlangattVMFEG-------TPTYPDPGRYWD---IVEKHKVTIFYTAPTAIRALMKFGDEW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 299 PftaitgvntlfnalvnneDFHELnfANMKL--SVGGGMAVQ------RAVAEK--------WKKITGVHLLegygltec 362
Cdd:cd05966 347 V------------------KKHDL--SSLRVlgSVGEPINPEawmwyyEVIGKErcpivdtwWQTETGGIMI-------- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 SPLvtgnPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRG--PQVMQGYWQRPEATKEVI--NEEGWLSTG 438
Cdd:cd05966 399 TPL----PGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRpwPGMARTIYGDHERYEDTYfsKFPGYYFTG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 439 DIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD-----PSLTKdE 513
Cdd:cd05966 475 DGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepsDELRK-E 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 521099036 514 LITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE--ENDAQL 558
Cdd:cd05966 554 LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKiaAGEEEL 600
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
27-552 |
8.57e-39 |
|
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: 148.63 E-value: 8.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVIVSNfantLEQIVANTQvkHVVLTSLGQMLPRAKGTLvdfvvkyvkgmvpkydlpgaism 186
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSH----LQPPIAFIG--LIDLLDEDTIYHEESENL----------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYgpVLREGRELVVTAlPLYhvFALT 266
Cdd:cd17655 131 -------------EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI--YQGEHLRVALFA-SIS--FDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLFIEMGGSNLLITnPR----DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFanMKLSVGGGmAVQRAVA 342
Cdd:cd17655 193 VTEIFASLLSGNTLYIV-RKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSL--KHLIVGGE-ALSTELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 343 EKWKKI--TGVHLLEGYGLTECSPLVTGNPYDLADYSGA---IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQG 417
Cdd:cd17655 269 KKIIELfgTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 418 YWQRPEATKE--VINE----EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPH 491
Cdd:cd17655 349 YLNRPELTAEkfVDDPfvpgERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKD 428
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 492 EVSGEVVKIYVVKrDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd17655 429 EQGQNYLCAYIVS-EKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-552 |
1.42e-38 |
|
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: 146.69 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLL-QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVivsnFANtleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaism 186
Cdd:cd17653 80 KLPSARIQAILRTSGATLLL----TTD----------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAyGPVLREGRELVVTALPLYHVFALT 266
Cdd:cd17653 103 -----------------SPDDLAYIIFTSGSTGIPKGVMVPHRG-VLNYVSQPPA-RLDVGPGSRVAQVLSIAFDACIGE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 V-NCLLFiemgGSNLLITNPRDipgfvkelqkhPF-TAITGVNTL-----FNALVNNEDfhelnFANMKLSVGGGMAVQR 339
Cdd:cd17653 164 IfSTLCN----GGTLVLADPSD-----------PFaHVARTVDALmstpsILSTLSPQD-----FPNLKTIFLGGEAVPP 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 340 AVAEKWKKitGVHLLEGYGLTECSPLVT------GNPYdladysgAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQ 413
Cdd:cd17653 224 SLLDRWSP--GRRLYNAYGPTECTISSTmtellpGQPV-------TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQ 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 414 VMQGYWQRPEAT----KEVINEEGWL--STGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVV-ALHGKVLEVAA 486
Cdd:cd17653 295 VARGYLGNPALTaskfVPDPFWPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVlQSQPEVTQAAA 374
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 487 IgqpheVSGEVVKIYVVkrdP-SLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd17653 375 I-----VVNGRLVAFVT---PeTVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
49-550 |
1.98e-38 |
|
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: 147.05 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDADARAIVI 127
Cdd:cd12116 13 LSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYILEDAEPALVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 VSNFANTLEQIvantqvkhvvltslgqmlprakgtlvdfvvkyvkGMVPKYDLPGAismrKALHKGRRlqyvkPFMSGED 207
Cdd:cd12116 91 DDALPDRLPAG----------------------------------LPVLLLALAAA----AAAPAAPR-----TPVSPDD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 IAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREGRELVVTALplyhVFALTVNCLLFIEMGGSNLLITNP-- 285
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRN-LVNFLHSMRERLGLGPGDRLLAVTTY----AFDISLLELLLPLLAGARVVIAPRet 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 -RDIPGFVKELQKHPFTAITGVNTLFNALVNNEdfhELNFANMKLSVGGgMAVQRAVAEKWKKITGVhLLEGYGLTECSP 364
Cdd:cd12116 203 qRDPEALARLIEAHSITVMQATPATWRMLLDAG---WQGRAGLTALCGG-EALPPDLAARLLSRVGS-LWNLYGPTETTI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 365 LVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVI-----NEEG--WLST 437
Cdd:cd12116 278 WSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFvpdpfAGPGsrLYRT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 438 GDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDELITH 517
Cdd:cd12116 358 GDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPDAAALRAH 437
|
490 500 510
....*....|....*....|....*....|...
gi 521099036 518 CRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd12116 438 LRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
36-565 |
2.52e-38 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 150.18 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 36 YADQPAFInMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPlytprEL-- 113
Cdd:PRK06060 19 WYDRPAFY-AADVVTHGQIHDGAARLGEVLRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP-----ELhr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 114 -EHQLNDADARAIVIVSNfantleqivantqvkhvvltslGQMLPR-AKGTLVDfvvkyvkgmvPKYDLPGAISMRKALH 191
Cdd:PRK06060 92 dDHALAARNTEPALVVTS----------------------DALRDRfQPSRVAE----------AAELMSEAARVAPGGY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 192 KgrrlqyvkpFMSGEDIAFLQYTGGTTGVAKGAILTHRN-------MVANVLQAKGAygpvlregrELVVTALPLYHVFA 264
Cdd:PRK06060 140 E---------PMGGDALAYATYTSGTTGPPKAAIHRHADpltfvdaMCRKALRLTPE---------DTGLCSARMYFAYG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 265 LTVNCLLFIEMGGSnlLITNPRDIPGFVKELQKHPF--TAITGVNTLFNALVN--NEDfhelNFANMKLSVGGGMAVQRA 340
Cdd:PRK06060 202 LGNSVWFPLATGGS--AVINSAPVTPEAAAILSARFgpSVLYGVPNFFARVIDscSPD----SFRSLRCVVSAGEALELG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 VAEKWKKI-TGVHLLEGYGLTECSPLVTGNPYDlaDYS-GAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGY 418
Cdd:PRK06060 276 LAERLMEFfGGIPILDGIGSTEVGQTFVSNRVD--EWRlGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGY 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEAtkeVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVV 498
Cdd:PRK06060 354 WNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTL 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 499 KIYVVKRDPSLTKDELITHCRK----HLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQ------LAEQKKSA 565
Cdd:PRK06060 431 QAFLVATSGATIDGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTKpiwelsLTEPGSGV 507
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
211-561 |
6.80e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 144.78 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 211 LQYTGGTTGVAKGAILTHRnmvanvlqakGAYGPVLRE--GREL-----VVTALPLYHVFALTVNCLLfIEMGGSNLLIT 283
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHR----------GAYLSTLSAiiGWEMgtcpvYLWTLPMFHCNGWTFTWGT-AARGGTSVCMR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 NPrDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHLLEGYGLTECS 363
Cdd:PLN03102 260 HV-TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEAT 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 364 -------------PLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQT-GELQVRGPQVMQGYWQRPEATKEVI 429
Cdd:PLN03102 338 gpvlfcewqdewnRLPENQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 nEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV------ 503
Cdd:PLN03102 418 -KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVlekget 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 504 ----KRDPSLTKD-ELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQLAEQ 561
Cdd:PLN03102 497 tkedRVDKLVTRErDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIAKGLVVED 559
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
6-476 |
1.13e-36 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 144.86 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 6 LSRYPsDVPETinpdqyLSLVEMFEQSVHKYADQPAFINM----GSV-----MTFRKL-EERSRAFAAYLQneLKLKKGD 75
Cdd:PLN02736 34 VSRFP-DHPEI------GTLHDNFVYAVETFRDYKYLGTRirvdGTVgeykwMTYGEAgTARTAIGSGLVQ--HGIPKGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 76 RVALMMPNLLQYPVALFGILRAGMIAVnvnPLYT---PRELEHQLNDADARAIVIVSNFANTLeqivantqvkhvvLTSL 152
Cdd:PLN02736 105 CVGLYFINRPEWLIVDHACSAYSYVSV---PLYDtlgPDAVKFIVNHAEVAAIFCVPQTLNTL-------------LSCL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 153 GQMlPRAKgTLVdfVVKYVKGMVPKydLPGA-----ISMRKALHKGRRLQyvKPFM--SGEDIAFLQYTGGTTGVAKGAI 225
Cdd:PLN02736 169 SEI-PSVR-LIV--VVGGADEPLPS--LPSGtgveiVTYSKLLAQGRSSP--QPFRppKPEDVATICYTSGTTGTPKGVV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 226 LTHRNMVANVLQAKGA--YGPvlregRELVVTALPLYHVFAlTVNCLLFIEMG-------GSNLLITNprDIPGF----- 291
Cdd:PLN02736 241 LTHGNLIANVAGSSLStkFYP-----SDVHISYLPLAHIYE-RVNQIVMLHYGvavgfyqGDNLKLMD--DLAALrptif 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 292 --VKELQKHPFTAIT-GVNT-------LFN--------ALVNNED----FHELNFANMKLSVGGGM--------AVQRAV 341
Cdd:PLN02736 313 csVPRLYNRIYDGITnAVKEsgglkerLFNaaynakkqALENGKNpspmWDRLVFNKIKAKLGGRVrfmssgasPLSPDV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 342 AEKWKKITGVHLLEGYGLTECSPLVTGNpyDLADY-SGAIGLPVPSTEVRIVD-DEGNVLNYGQT---GELQVRGPQVMQ 416
Cdd:PLN02736 393 MEFLRICFGGRVLEGYGMTETSCVISGM--DEGDNlSGHVGSPNPACEVKLVDvPEMNYTSEDQPyprGEICVRGPIIFK 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 417 GYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMI-LVSGFNVYPNEIEDVVA 476
Cdd:PLN02736 471 GYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYA 531
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
206-547 |
1.13e-36 |
|
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: 139.32 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQakgaygpVLREGRELVV-----TALPLYHVFAL--TVNCLLF---IEM 275
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDI-------LQKEGLNWVVgdvtyLPLPATHIGGLwwILTCLIHgglCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSNLLITNprdipgFVKELQKHPFTAITGVNTLFNALVN-----NEDFHELNFanmkLSVGGGMAVQRAVAE-KWKKIT 349
Cdd:cd17635 74 GGENTTYKS------LFKILTTNAVTTTCLVPTLLSKLVSelksaNATVPSLRL----IGYGGSRAIAADVRFiEATGLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 350 GVhlLEGYGLTECSP---LVTGNpyDLADySGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATK 426
Cdd:cd17635 144 NT--AQVYGLSETGTalcLPTDD--DSIE-INAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 427 EVINEeGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKrd 506
Cdd:cd17635 219 EVLID-GWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA-- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 521099036 507 pSLTKDE-----LITHCRKHLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:cd17635 296 -SAELDEnairaLKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
204-459 |
2.61e-36 |
|
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: 141.97 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 204 SGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREgRELVVTALPLYHVFALTV-NCLLFI--EMGGSN- 279
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAeNVCLYRggTIGYGSp 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 280 ---------------------LLITNPR--------------DIPGFVKELQKHPFT----AIT-GVNT-LFNALVnned 318
Cdd:cd17639 165 rtltdkskrgckgdltefkptLMVGVPAiwdtirkgvlaklnPMGGLKRTLFWTAYQsklkALKeGPGTpLLDELV---- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 319 fhelnFANMKLSVGG-------GMAVQRAVAEKWKKITGVHLLEGYGLTE-CSPLVTGNPYDLadYSGAIGLPVPSTEVR 390
Cdd:cd17639 241 -----FKKVRAALGGrlrymlsGGAPLSADTQEFLNIVLCPVIQGYGLTEtCAGGTVQDPGDL--ETGRVGPPLPCCEIK 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099036 391 IVD-DEGNVLNYGQT--GELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMI 459
Cdd:cd17639 314 LVDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
48-458 |
8.53e-36 |
|
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: 141.41 E-value: 8.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 48 VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLlqyPVALFGILRAGMIAVNVNPLYT---PRELEHQLNDADARA 124
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 125 IVivsnfANTLEQIVAntqvkhvvLTSLGQMLPRakgtlVDFVVkYV--KGMvPKYDLPGAISMRKALHKGRRLQYVKPF 202
Cdd:cd17641 87 VI-----AEDEEQVDK--------LLEIADRIPS-----VRYVI-YCdpRGM-RKYDDPRLISFEDVVALGRALDRRDPG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 M--------SGEDIAFLQYTGGTTGVAKGAILTHRNMV---ANVLQAKGaygpvLREGRElVVTALPLYHV--FALTV-- 267
Cdd:cd17641 147 LyerevaagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLghcAAYLAADP-----LGPGDE-YVSVLPLPWIgeQMYSVgq 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 268 -----NCLLFIE-----MG-----GSNLLITNPR--------------DIPGFVKELQKH-----------------PFT 301
Cdd:cd17641 221 alvcgFIVNFPEepetmMEdlreiGPTFVLLPPRvwegiaadvrarmmDATPFKRFMFELgmklglraldrgkrgrpVSL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 302 AITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHLLEGYGLTECSPLVTGNPYDLADYSgAIG 381
Cdd:cd17641 301 WLRLASWLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDPD-TVG 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 382 LPVPSTEVRIVDdegnvlnygqTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDM 458
Cdd:cd17641 379 VPFPGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDV 445
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
37-551 |
9.22e-36 |
|
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: 141.68 E-value: 9.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 37 ADQPAFINMGSV------MTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTP 110
Cdd:cd05967 65 GDQIALIYDSPVtgtertYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 111 RELEHQLNDADArAIVIVSNFANTLEQIV------------ANTQVKHVVLTSLGQMLPRA--KGTLVDFvvkyvkgmvp 176
Cdd:cd05967 144 KELASRIDDAKP-KLIVTASCGIEPGKVVpykplldkalelSGHKPHHVLVLNRPQVPADLtkPGRDLDW---------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 177 kYDLpgaismrkaLHKGRRLQYVKpfMSGEDIAFLQYTGGTTGVAKGAILT---HRNMVANVLQ-----AKG-------- 240
Cdd:cd05967 213 -SEL---------LAKAEPVDCVP--VAATDPLYILYTSGTTGKPKGVVRDnggHAVALNWSMRniygiKPGdvwwaasd 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 241 ----------AYGPVLREGRELVVTALPLYhvfalTVNCLLF---IEMGGSNLLITNP-------RDIPGfVKELQKHPF 300
Cdd:cd05967 281 vgwvvghsyiVYGPLLHGATTVLYEGKPVG-----TPDPGAFwrvIEKYQVNALFTAPtairairKEDPD-GKYIKKYDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 301 TAITgvnTLFnalvnnedfhelnfanmklsvgggMAVQRAVAE--KW-KKITGVHLLEGYGLTECSPLVTGNPYDLADYS 377
Cdd:cd05967 355 SSLR---TLF------------------------LAGERLDPPtlEWaENTLGVPVIDHWWQTETGWPITANPVGLEPLP 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 378 ---GAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGP---QVMQGYWQRPEATKEVINEE--GWLSTGDIVRFDENGMI 449
Cdd:cd05967 408 ikaGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 450 YIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-----KRDPSLTKDELITHCRKHLTG 524
Cdd:cd05967 488 FIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVlkegvKITAEELEKELVALVREQIGP 567
|
570 580
....*....|....*....|....*..
gi 521099036 525 YKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd05967 568 VAAFRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
27-550 |
2.77e-35 |
|
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: 137.83 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARaivivsnfantleqivantqvkhVVLTSlgqmlprakgtlvdfvvkyvkgmvpkydlpgaism 186
Cdd:cd12115 82 AYPPERLRFILEDAQAR-----------------------LVLTD----------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGrELVVTA----LPLYHV 262
Cdd:cd12115 104 ------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAG-VLASTSicfdLSVFEL 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 263 FA-LTVncllfiemGGSNLLITNPRDIPGFVKELQkhpFTAITGVNTLFNALVNNEDFHE----LNFANMKLSvgggmav 337
Cdd:cd12115 165 FGpLAT--------GGKVVLADNVLALPDLPAAAE---VTLINTVPSAAAELLRHDALPAsvrvVNLAGEPLP------- 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 338 QRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADY-SGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQ 416
Cdd:cd12115 227 RDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASgEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVAR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 417 GYWQRPEATKE--VINEEG----WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:cd12115 307 GYLGRPGLTAErfLPDPFGpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIG 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 491 HEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd12115 387 DAAGERRLVAYIVaEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
206-556 |
8.87e-35 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 139.46 E-value: 8.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAK--GAYGPvlregRELVVTALPLYHVFALTVNCLLFIEMGGSNLLIT 283
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKtiADFTP-----NDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 NP---RDIPGFVKElqkHPFTAITGVNTLfnaLVNNEDF-HELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGL 359
Cdd:PRK08043 440 SPlhyRIVPELVYD---RNCTVLFGTSTF---LGNYARFaNPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGV 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 360 TECSPLVTGN-PydLADYSGAIGLPVPSTEVRIVddegNVLNYGQTGELQVRGPQVMQGY--------WQRPEA-TKEVI 429
Cdd:PRK08043 514 TECAPVVSINvP--MAAKPGTVGRILPGMDARLL----SVPGIEQGGRLQLKGPNIMNGYlrvekpgvLEVPTAeNARGE 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 NEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVkrDPSL 509
Cdd:PRK08043 588 MERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DSEL 665
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521099036 510 TKDELITHCRKH-LTGYKVPKLIEFREELPKTNVGK----ILRRVLREENDA 556
Cdd:PRK08043 666 TREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKpdfvTLKSMVDEPEQH 717
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
24-515 |
1.78e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 137.94 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPA--FINMGSV-------MTFRKLEERSRAFAAYLQNelKLKKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAyrFLDFSTErdgvardLTWSQFGARNRAVGARLQQ--VTKPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 95 LRAGMIAVnvnPLYTPRELEHqlndadaraivivsnfANTLEQIVANTQVKhVVLTSLGQmlprAKGtlvdfVVKYVKGm 174
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGH----------------VGRLHAVLDDCTPS-AILTTTDS----AEG-----VRKFFRA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 175 VPKYDLPGAISMrKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRElVV 254
Cdd:PRK07769 150 RPAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE--GQEGDR-GV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 255 TALPLYHVFAL-TVnclLFIEMGGSNLLITNPRDI---PG-FVKELQKHPftaiTGVNTLFNALVN------------NE 317
Cdd:PRK07769 226 SWLPFFHDMGLiTV---LLPALLGHYITFMSPAAFvrrPGrWIRELARKP----GGTGGTFSAAPNfafehaaarglpKD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 318 DFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLE------GYGLTECSPLVTGNPYD------------------- 372
Cdd:PRK07769 299 GEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPptaikpSYGMAEATLFVSTTPMDeeptviyvdrdelnagrfv 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 373 --LADYSGAI-----GLPVPSTEVRIVDDE-GNVLNYGQTGELQVRGPQVMQGYWQRPEATKEV--------INE---EG 433
Cdd:PRK07769 379 evPADAPNAVaqvsaGKVGVSEWAVIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATfqnilksrLSEshaEG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 ------WLSTGDI-VRFDenGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLE---VAAIGQPHEVSGEVV---KI 500
Cdd:PRK07769 459 apddalWVRTGDYgVYFD--GELYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALRtgyVAAFSVPANQLPQVVfddSH 536
|
570
....*....|....*
gi 521099036 501 YVVKRDPSLTKDELI 515
Cdd:PRK07769 537 AGLKFDPEDTSEQLV 551
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
44-498 |
2.04e-34 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 137.44 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 44 NMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTP-----RE-----L 113
Cdd:PRK09192 45 QLEEALPYQTLRARAEAGARRLLA-LGLKPGDRVALIAETDGDFVEAFFACQYAGLVPV---PLPLPmgfggREsyiaqL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 114 EHQLNDADARAIVIVSNFANTLEQIVANTQVKHVvltslgqmlprakGTLVDFvvkyvkgmvpkYDLPGAismrkalhkG 193
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHV-------------LSHAWF-----------KALPEA---------D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 194 RRLQYVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANvLQAKGAYGPVLREGrELVVTALPLYHVFALtVNCLLfi 273
Cdd:PRK09192 168 VALPRPTP----DDIAYLQYSSGSTRFPRGVIITHRALMAN-LRAISHDGLKVRPG-DRCVSWLPFYHDMGL-VGFLL-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 274 EMGGSNL-------------------LIT-NPRDI---PGFVKELqkhpftaitgvntlfNAL-VNNEDFHELNFANMKL 329
Cdd:PRK09192 239 TPVATQLsvdylptrdfarrplqwldLISrNRGTIsysPPFGYEL---------------CARrVNSKDLAELDLSCWRV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 330 S-VGGGMA---VQRAVAEKWKK--ITGVHLLEGYGLTEC------SPLVTGNPYDLAD-----YSGAI------------ 380
Cdd:PRK09192 304 AgIGADMIrpdVLHQFAEAFAPagFDDKAFMPSYGLAEAtlavsfSPLGSGIVVEEVDrdrleYQGKAvapgaetrrvrt 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 381 ----GLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKeVINEEGWLSTGDIvRFDENGMIYIVDRKK 456
Cdd:PRK09192 384 fvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQD-VLAADGWLDTGDL-GYLLDGYLYITGRAK 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 521099036 457 DMILVSGFNVYPNEIEDVVALHGKVL--EVAAIGQPHEVSGEVV 498
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV 505
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-553 |
2.06e-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: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGrelVVTALPLYHVFALtVNCLLFIEMGGSN------ 279
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDR---ILSWMPLTHDMGL-IAFHLAPLIAGMNqylmpt 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 280 -LLITNPRDipgFVKELQKHPFTAITGVNTLFNALV---NNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKITGVH--- 352
Cdd:cd05908 182 rLFIRRPIL---WLKKASEHKATIVSSPNFGYKYFLktlKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYglk 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 ---LLEGYGLTECS----------PLVT----------GNPYDLADYSGA-------IGLPVPSTEVRIVDDEGNVLNYG 402
Cdd:cd05908 259 rnaILPVYGLAEASvgaslpkaqsPFKTitlgrrhvthGEPEPEVDKKDSecltfveVGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 403 QTGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIvRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDV-VALHGKV 481
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDL-GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIaEELEGVE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 482 L-EVAAIG-QPHEVSGEVVKIYVVKRDPSLTKDELITHCRKHL---TGYKVPKLIEFReELPKTNVGKILRRVLREE 553
Cdd:cd05908 418 LgRVVACGvNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLnkrGGWQINEVLPIR-RIPKTTSGKVKRYELAQR 493
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
19-546 |
6.31e-34 |
|
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: 136.17 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 19 PDQYLSLV-EMFEQSVHKYADQPAFI---NMGSV---MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVAL 91
Cdd:cd17634 48 EDATLNLAaNALDRHLRENGDRTAIIyegDDTSQsrtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 92 FGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIvantQVKHVVLTSLgqmlpRAKGTLVDFVVKYV 171
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGRSV----PLKKNVDDAL-----NPNVTSVEHVIVLK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 172 KGMVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGA---YGPvlre 248
Cdd:cd17634 198 RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvfdYGP---- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 249 gRELVVTALPLYHVFA---LTVNCLLfieMGGSNLLITNPRDIPG---FVKELQKHPFTAITGVNTLFNALVNNED--FH 320
Cdd:cd17634 274 -GDIYWCTADVGWVTGhsyLLYGPLA---CGATTLLYEGVPNWPTparMWQVVDKHGVNILYTAPTAIRALMAAGDdaIE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 321 ELNFANMKLSVGGGMAVQ-RAVAEKWKKITGVH--LLEGYGLTECS-PLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEG 396
Cdd:cd17634 350 GTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKcpVVDTWWQTETGgFMITPLPGAIELKAGSATRPVFGVQPAVVDNEG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 NVLNYGQTGELQVRGP---QVMQGYWQRPEATKEVINE-EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIE 472
Cdd:cd17634 430 HPQPGGTEGNLVITDPwpgQTRTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIE 509
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 473 DVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR----DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKIL 546
Cdd:cd17634 510 SVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
24-565 |
7.24e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 138.17 E-value: 7.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVN 103
Cdd:PRK12316 512 GVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVP 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 104 VNPLYTPRELEHQLNDADARAIVivsnfantleqivanTQvkhvvlTSLGQMLPRAKGTlvdfvvkyvkgMVPKYDLPGA 183
Cdd:PRK12316 591 LDPEYPAERLAYMLEDSGVQLLL---------------SQ------SHLGRKLPLAAGV-----------QVLDLDRPAA 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 184 ismrkaLHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvlREGRELVVTALPLyhVF 263
Cdd:PRK12316 639 ------WLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG---LGVGDTVLQKTPF--SF 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 264 ALTVNCLLFIEMGGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELnfANMKLSVGGGMAVQRA 340
Cdd:PRK12316 708 DVSVWEFFWPLMSGARLVVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASC--TSLRRIVCSGEALPAD 785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 VAEK-WKKITGVHLLEGYGLTECSPLVTGNPY-DLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGY 418
Cdd:PRK12316 786 AQEQvFAKLPQAGLYNLYGPTEAAIDVTHWTCvEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGY 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKE------VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQphe 492
Cdd:PRK12316 866 HGRPGLTAErfvpspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--- 942
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 493 vSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLrEENDAQLAEQKKSA 565
Cdd:PRK12316 943 -DGKQLVGYVVLESEGgDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL-PAPEASVAQQGYVA 1014
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
32-565 |
9.86e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 134.73 E-value: 9.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 32 SVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMiaVNVNPLYTPR 111
Cdd:PRK10946 32 TRHAASDAIAVICGERQFSYRELNQASDNLACSLR-RQGIKPGDTALVQLGNVAEFYITFFALLKLGV--APVNALFSHQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 112 ELEhqLNdADAR----AIVIVSN----FANT--LEQIVA-NTQVKHVVLtsLGQmlprakgtlvdfvvkyvkgmvpkydl 180
Cdd:PRK10946 109 RSE--LN-AYASqiepALLIADRqhalFSDDdfLNTLVAeHSSLRVVLL--LND-------------------------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 181 PGAISMRKALHKGRRLQYVKPFMSGEdIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVvtALPLY 260
Cdd:PRK10946 158 DGEHSLDDAINHPAEDFTATPSPADE-VAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICG-FTPQTRYLC--ALPAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 261 HVFALTV-NCLLFIEMGGSNLLITNPRDIPGFvKELQKHPFTAIT----GVNTLFNALVNNEDFHELnfANMKLSVGGGM 335
Cdd:PRK10946 234 HNYPMSSpGALGVFLAGGTVVLAPDPSATLCF-PLIEKHQVNVTAlvppAVSLWLQAIAEGGSRAQL--ASLKLLQVGGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 336 AVQRAVAEKWKKITGVHLLEGYGLTEcsPLVtgNPYDLADYSGAI----GLPV-PSTEVRIVDDEGNVLNYGQTGELQVR 410
Cdd:PRK10946 311 RLSETLARRIPAELGCQLQQVFGMAE--GLV--NYTRLDDSDERIfttqGRPMsPDDEVWVADADGNPLPQGEVGRLMTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP 490
Cdd:PRK10946 387 GPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSME 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 491 HEVSGEVVKIYVVKRDPsLTKDELithcRKHLTG-----YKVPKLIEFREELPKTNVGKILRRVLReendaQLAEQKKSA 565
Cdd:PRK10946 467 DELMGEKSCAFLVVKEP-LKAVQL----RRFLREqgiaeFKLPDRVECVDSLPLTAVGKVDKKQLR-----QWLASRASA 536
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-550 |
1.32e-33 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 132.76 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVivsnfantleqivanTQVkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlq 197
Cdd:cd17652 81 ADARPALLL---------------TTP----------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREGRELVVTALPlyhvFALTVNCLLFIEMGG 277
Cdd:cd17652 93 --------DNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPS----FDASVWELLMALLAG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SNLLITNPRDI---PGFVKELQKHPFTAITGVNTLFNAL--VNNEDFHELnfanmklsVGGGMAVQRAVAEKWKKitGVH 352
Cdd:cd17652 160 ATLVLAPAEELlpgEPLADLLREHRITHVTLPPAALAALppDDLPDLRTL--------VVAGEACPAELVDRWAP--GRR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 LLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKE--VIN 430
Cdd:cd17652 230 MINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfVAD 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLS-----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-K 504
Cdd:cd17652 310 PFGAPGsrmyrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVpA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 521099036 505 RDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17652 390 PGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
49-521 |
3.08e-33 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 133.49 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIViv 128
Cdd:PRK09274 42 LSFAELDARSDAIAHGL-NAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 snfANTLEQIVAntqvkhvvltslgQMLPRAKGTLVDFVVkyvkgmVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDI 208
Cdd:PRK09274 119 ---GIPKAHLAR-------------RLFGWGKPSVRRLVT------VGGRLLWGGTTLATLLRDGAAAPFPMADLAPDDM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVtaLPLYHVF--ALTVNCLLfIEMGGSNLLITNPR 286
Cdd:PRK09274 177 AAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYG-IEPGEIDLPT--FPLFALFgpALGMTSVI-PDMDPTRPATVDPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIpgfvkelqkhpFTAIT--GVNTLF------NALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKI--TGVHLLEG 356
Cdd:PRK09274 253 KL-----------FAAIEryGVTNLFgspallERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMlpPDAEILTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVT-------GNPYDLADYSGAI--GLPVPSTEVRIVD---------DEGNVLNYGQTGELQVRGPQVMQGY 418
Cdd:PRK09274 322 YGATEALPISSiesreilFATRAATDNGAGIcvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVAGPMVTRSY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKE--VINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGqpHEVS 494
Cdd:PRK09274 402 YNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG--VGVP 479
|
490 500 510
....*....|....*....|....*....|...
gi 521099036 495 GEVVKIYVVKRDPSLTKD------ELITHCRKH 521
Cdd:PRK09274 480 GAQRPVLCVELEPGVACSksalyqELRALAAAH 512
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-551 |
7.90e-33 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 130.95 E-value: 7.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADAraivivsnfantleqivantqvkHVVLTslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalHKGRRLQ 197
Cdd:cd17649 81 EDSGA-----------------------GLLLT----------------------------------------HHPRQLA 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 YVkpfmsgediaflQYTGGTTGVAKGAILTHRNMVANvLQAKGAYGPVLREGRELVVTALPlyhvFALTVNCLLFIEMGG 277
Cdd:cd17649 98 YV------------IYTSGSTGTPKGVAVSHGPLAAH-CQATAERYGLTPGDRELQFASFN----FDGAHEQLLPPLICG 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SNLLITNPR--DIPGFVKELQKHPFTAITGVNT--LFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKItGVHL 353
Cdd:cd17649 161 ACVVLRPDElwASADELAEMVRELGVTVLDLPPayLQQLAEEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKA-PVRL 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 354 LEGYGLTEC--SPLVTGNPYDLADYSGA--IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVI 429
Cdd:cd17649 240 FNAYGPTEAtvTPLVWKCEAGAARAGASmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERF 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 430 -----NEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKiYV 502
Cdd:cd17649 320 vpdpfGAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVA-YV 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 521099036 503 VKRDPS---LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:cd17649 399 VLRAAAaqpELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-565 |
1.09e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 134.52 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 23 LSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAV 102
Cdd:PRK12467 1574 RLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLI-ALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYV 1652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 103 NVNPLYTPRELEHQLNDADARAIVivsnfantleqivanTQvkhvvlTSLGQMLPRAKGTLVDFVvkyvkgmvpkyDLPG 182
Cdd:PRK12467 1653 PLDPEYPRERLAYMIEDSGIELLL---------------TQ------SHLQARLPLPDGLRSLVL-----------DQED 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 183 A-ISMRKALHKGRRLqyvkpfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREgrelvvtALPLYH 261
Cdd:PRK12467 1701 DwLEGYSDSNPAVNL-------APQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD-------VVLQFT 1766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 262 VFALTVNC--LLFIEMGGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNeDFHELNFANMKLSVGGGMA 336
Cdd:PRK12467 1767 SFAFDVSVweLFWPLINGARLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQM-DEQVEHPLSLRRVVCGGEA 1845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQRAVAEKW-KKITGVHLLEGYGLTECSPLVTGNPYDLADYSGA----IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRG 411
Cdd:PRK12467 1846 LEVEALRPWlERLPDTGLFNLYGPTETAVDVTHWTCRRKDLEGRdsvpIGQPIANLSTYILDASLNPVPIGVAGELYLGG 1925
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 412 PQVMQGYWQRPEATKE--VINEEGWLS-----TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEV 484
Cdd:PRK12467 1926 VGLARGYLNRPALTAErfVADPFGTVGsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREA 2005
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 485 AAIGQPHEVSGEVVKiYVVKRDPSLT---------KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLrEEND 555
Cdd:PRK12467 2006 VVIAQDGANGKQLVA-YVVPTDPGLVdddeaqvalRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL-PAPD 2083
|
570
....*....|
gi 521099036 556 AQLAEQKKSA 565
Cdd:PRK12467 2084 ASELQQAYVA 2093
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
200-550 |
2.66e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 130.90 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 200 KPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVA--NVLQAKGAYGPVLREGrELVVTALPLYHVFAL--TVNCLLfieM 275
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNWVTWVVG-ETTYSPLPATHIGGLwwILTCLM---H 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGsnLLITNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGmavQRAVAEKWKKI--TGVHL 353
Cdd:PRK05857 239 GG--LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVRFIeaTGVRT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 354 LEGYGLTE--CSPLVTgnPYDLADYS----GAIGLPVPSTEVRIVDDEG---NVLNYGQT---GELQVRGPQVMQGYWQR 421
Cdd:PRK05857 314 AQVYGLSEtgCTALCL--PTDDGSIVkieaGAVGRPYPGVDVYLAATDGigpTAPGAGPSasfGTLWIKSPANMLGYWNN 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 422 PEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIY 501
Cdd:PRK05857 392 PERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLA 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 521099036 502 VV---KRDPSLT---KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:PRK05857 471 VVasaELDESAAralKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
49-446 |
2.37e-31 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 128.46 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYT-----PRELEHQLN----- 118
Cdd:PRK08180 70 LTYAEALERVRAIAQALL-DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSlvsqdFGKLRHVLElltpg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 119 -----DAD--ARAIVIVsnFANTLEQIVANTQVKHVVLTSLGQMLPRAKGTLVDfvvkyvkgmvpkydlpgaismrkALH 191
Cdd:PRK08180 149 lvfadDGAafARALAAV--VPADVEVVAVRGAVPGRAATPFAALLATPPTAAVD-----------------------AAH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 192 KGrrlqyVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVlQAKGAYGPVLREGRELVVTALPLYHVFALTVNCLL 271
Cdd:PRK08180 204 AA-----VGP----DTIAKFLFTSGSTGLPKAVINTHRMLCANQ-QMLAQTFPFLAEEPPVLVDWLPWNHTFGGNHNLGI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 272 FIEMGGSnLLITNPRDIPGFVKE----LQKHPFTAITGVNTLFNALVN----NEDFHELNFANMKLSVGGGMAVQRAVAE 343
Cdd:PRK08180 274 VLYNGGT-LYIDDGKPTPGGFDEtlrnLREISPTVYFNVPKGWEMLVPalerDAALRRRFFSRLKLLFYAGAALSQDVWD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKKITGVHLLE------GYGLTECSPLVTgNPYDLADYSGAIGLPVPSTEVRIVDDEGNVlnygqtgELQVRGPQVMQG 417
Cdd:PRK08180 353 RLDRVAEATCGErirmmtGLGMTETAPSAT-FTTGPLSRAGNIGLPAPGCEVKLVPVGGKL-------EVRVKGPNVTPG 424
|
410 420 430
....*....|....*....|....*....|
gi 521099036 418 YWQRPEATKEVINEEGWLSTGDIVRF-DEN 446
Cdd:PRK08180 425 YWRAPELTAEAFDEEGYYRSGDAVRFvDPA 454
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-551 |
2.68e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 128.04 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 12 DVPEtiNPDQYLSLVEMF--EQSVHKYADQPAFINmGSV-MTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYP 88
Cdd:PLN02479 9 DLPK--NAANYTALTPLWflERAAVVHPTRKSVVH-GSVrYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 89 VALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQivantqvkhvvltSLGQMLPRAKGTLVD--F 166
Cdd:PLN02479 85 EAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEE-------------ALKILAEKKKSSFKPplL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 167 VVKYVKGMVPKydlpgaiSMRKALHKGRrLQYVKpFMSGEDIAF-------------LQYTGGTTGVAKGAILTHRNMVA 233
Cdd:PLN02479 152 IVIGDPTCDPK-------SLQYALGKGA-IEYEK-FLETGDPEFawkppadewqsiaLGYTSGTTASPKGVVLHHRGAYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 234 NVLQAKGAYGpvLREGRELVVTaLPLYH------VFALTVNCllfiemgGSNLLItnpRDIP--GFVKELQKHPFTAITG 305
Cdd:PLN02479 223 MALSNALIWG--MNEGAVYLWT-LPMFHcngwcfTWTLAALC-------GTNICL---RQVTakAIYSAIANYGVTHFCA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 306 VNTLFNALVN---NEDFHELNFANMKLSVGGG--MAVQRAVAEKWKKITGVH-LLEGYG-LTECS--------PLVTG-- 368
Cdd:PLN02479 290 APVVLNTIVNapkSETILPLPRVVHVMTAGAAppPSVLFAMSEKGFRVTHTYgLSETYGpSTVCAwkpewdslPPEEQar 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 369 -NPYDLADYSGAIGLPV--PSTEVRIVDDegnvlnyGQT-GELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFD 444
Cdd:PLN02479 370 lNARQGVRYIGLEGLDVvdTKTMKPVPAD-------GKTmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKH 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 445 ENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE------VVKIYVVKRDPSLTKDELITHC 518
Cdd:PLN02479 442 PDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGEspcafvTLKPGVDKSDEAALAEDIMKFC 521
|
570 580 590
....*....|....*....|....*....|...
gi 521099036 519 RKHLTGYKVPKLIEFrEELPKTNVGKILRRVLR 551
Cdd:PLN02479 522 RERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
23-560 |
3.53e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.90 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 23 LSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLqneLKLKKG-DR-VALMMPNLLQYPVALFGILRAGMI 100
Cdd:PRK12467 3095 RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL---IAIGVGpDVlVGVAVERSVEMIVALLAVLKAGGA 3171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 101 AVNVNPLYtPRE-LEHQLNDADARaiVIVSNfANTLEQIVANTQVKHVVLT--SLGQMLPRAKGTLVDfvvkyvkgmvpk 177
Cdd:PRK12467 3172 YVPLDPEY-PRErLAYMIEDSGVK--LLLTQ-AHLLEQLPAPAGDTALTLDrlDLNGYSENNPSTRVM------------ 3235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 178 ydlpgaismrkalhkgrrlqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHrNMVANVLQAKGAYGPVLREGRELVVTAL 257
Cdd:PRK12467 3236 ---------------------------GENLAYVIYTSGSTGKPKGVGVRH-GALANHLCWIAEAYELDANDRVLLFMSF 3287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 258 PlyhvFALTVNCLLFIEMGGSNLLIT--NPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELnfANMKLSVGGGM 335
Cdd:PRK12467 3288 S----FDGAQERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADC--ASLDIYVFGGE 3361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 336 AVQRAVAEKWK-KITGVHLLEGYGLTECSPLVT-----GNPYDLADYSgAIGLPVPSTEVRIVDDEGNVLNYGQTGELQV 409
Cdd:PRK12467 3362 AVPPAAFEQVKrKLKPRGLTNGYGPTEAVVTVTlwkcgGDAVCEAPYA-PIGRPVAGRSIYVLDGQLNPVPVGVAGELYI 3440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 410 RGPQVMQGYWQRPEATKE-------VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVL 482
Cdd:PRK12467 3441 GGVGLARGYHQRPSLTAErfvadpfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 483 EVAAIGQPHEVSGEVVKiYVVKRDPSLT-KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLrEENDAQLAE 560
Cdd:PRK12467 3521 EAVVLARDGAGGKQLVA-YVVPADPQGDwRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL-PDPDAKGSR 3597
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
49-505 |
3.58e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 127.75 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQneLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVnvnPLYTPrelehQLNDADARaivIV 128
Cdd:PRK05850 36 LTWSQLYRRTLNVAEELR--RHGSTGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVP-----QGGAHDER---VS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 SNFANTLEQivantqvkhVVLTSlgqmlprakGTLVDFVVKYVKgmVPKYDLPGAISMRKALHKGRRLQYVKPFMSGEDI 208
Cdd:PRK05850 103 AVLRDTSPS---------VVLTT---------SAVVDDVTEYVA--PQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRNMVANVLQAK----GAYGPVLREGRElVVTALPLYHVFALTVNclLFIEM-GGSNLLIT 283
Cdd:PRK05850 163 AYLQYTSGSTRTPAGVMVSHRNVIANFEQLMsdyfGDTGGVPPPDTT-VVSWLPFYHDMGLVLG--VCAPIlGGCPAVLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 NPrdipgfVKELQK------------HPFTAitGVNTLFNALV---NNEDFHELNFANMKLSVGGGMAVQRAVAEKW-KK 347
Cdd:PRK05850 240 SP------VAFLQRparwmqllasnpHAFSA--APNFAFELAVrktSDDDMAGLDLGGVLGIISGSERVHPATLKRFaDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ITGVHLLE-----GYGLTECSPLV----TGNPYDLADY----------------SGA--IGLPVP-STEVRIVDDEGNVL 399
Cdd:PRK05850 312 FAPFNLREtairpSYGLAEATVYVatrePGQPPESVRFdyeklsaghakrcetgGGTplVSYGSPrSPTVRIVDPDTCIE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 400 N-YGQTGELQVRGPQVMQGYWQRPEATKEVIN----------EEG-WLSTGDI-VRFDenGMIYIVDRKKDMILVSGFNV 466
Cdd:PRK05850 392 CpAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEGpWLRTGDLgFISE--GELFIVGRIKDLLIVDGRNH 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 521099036 467 YPNEIEDVVA--LHGKvleVAAIGQPHEVSGEVVKIYVVKR 505
Cdd:PRK05850 470 YPDDIEATIQeiTGGR---VAAISVPDDGTEKLVAIIELKK 507
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-550 |
9.59e-31 |
|
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: 125.28 E-value: 9.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQivaNTQVKHVVLTSLGQMLprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkGRRLQ 197
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSF---NKSTILLEDPSISQED------------------------------------TSNID 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 YVkpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVaNVLQAKGAYGPVLREGRELVVTALPLYHVFALTVNCLLFiemGG 277
Cdd:cd17656 123 YI---NNSDDLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLS---GG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SNLLITNP--RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMK--LSVGGGMAVQRAVAEKWKKiTGVHL 353
Cdd:cd17656 196 TLYIIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKhiITAGEQLVITNEFKEMLHE-HNVHL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 354 LEGYGLTEcSPLVTG---NPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVIN 430
Cdd:cd17656 275 HNHYGPSE-THVVTTytiNPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 431 EEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVK 504
Cdd:cd17656 354 PDPFDPnermyrTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 521099036 505 rDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17656 434 -EQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
27-550 |
1.35e-30 |
|
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: 124.20 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARaiVIVSNfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaism 186
Cdd:cd17645 81 DYPGERIAYMLADSSAK--ILLTN-------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVaNVLQAKGAYGPVLREGRELVVTALPlYHVFALT 266
Cdd:cd17645 103 ------------------PDDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSLVYASFS-FDASAWE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLFIemgGSNLLITNPR---DIPGFVKELQKHpftaitGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAE 343
Cdd:cd17645 163 IFPHLTA---GAALHVVPSErrlDLDALNDYFNQE------GITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERK 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKkitgvhLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPE 423
Cdd:cd17645 234 GYK------LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPE 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 424 ATKE------VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEV 497
Cdd:cd17645 308 LTAEkfivhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKY 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 521099036 498 VKIYVVKRDpSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17645 388 LVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-553 |
2.94e-30 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 123.62 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAI 125
Cdd:cd05940 1 DEALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 VIvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsg 205
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 eDIAFLQYTGGTTGVAKGAILTHRNMVanvLQAKGAYGPVLREGRELVVTALPLYHVFALTVnCLLFIEMGGSNLLITNP 285
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAW---RGGAFFAGSGGALPSDVLYTCLPLYHSTALIV-GWSACLASGATLVIRKK 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMavqRA-VAEKWKKITGV-HLLEGYGLTECs 363
Cdd:cd05940 157 FSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGL---RPdIWEEFKERFGVpRIAEFYAATEG- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 364 plVTGNpYDLADYSGAIG----LPVPSTEVRIV-----------DDEGNV--LNYGQTGEL--QVRGPQVMQGYWQRPEA 424
Cdd:cd05940 233 --NSGF-INFFGKPGAIGrnpsLLRKVAPLALVkydlesgepirDAEGRCikVPRGEPGLLisRINPLEPFDGYTDPAAT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 425 TKEVINE-----EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQP---HEVSGE 496
Cdd:cd05940 310 EKKILRDvfkkgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgTDGRAG 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 497 VVKIyVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:cd05940 390 MAAI-VLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
13-550 |
3.81e-30 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 126.31 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 13 VPETinpdqylSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALF 92
Cdd:PRK10252 455 IPET-------TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALH 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 93 GILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVantqvkhvvltslgqmlprakgtlvdfvvkyvK 172
Cdd:PRK10252 527 AIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVP--------------------------------D 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 173 GMVPKYDLPGAISmrkalhKGRRLQYVKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGrEL 252
Cdd:PRK10252 575 LTSLCYNAPLAPQ------GAAPLQLSQP----HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYP--LTAD-DV 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 253 VVTALPLyhVFALTVNCLLFIEMGGSNLLITNP---RDiPgfvKELQKhpFTAITGVNTL---------FNALVNNEDFH 320
Cdd:PRK10252 642 VLQKTPC--SFDVSVWEFFWPFIAGAKLVMAEPeahRD-P---LAMQQ--FFAEYGVTTThfvpsmlaaFVASLTPEGAR 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 321 ElNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNP---YDLADYSGA---IGLPVPSTEVRIVDD 394
Cdd:PRK10252 714 Q-SCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPafgEELAAVRGSsvpIGYPVWNTGLRILDA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 395 EGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYP 468
Cdd:PRK10252 793 RMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPgermyrTGDVARWLDDGAVEYLGRSDDQLKIRGQRIEL 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 469 NEIEDVVALHGKVLEVAA----IGQPHEVSGEVVKI--YVVKR-DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTN 541
Cdd:PRK10252 873 GEIDRAMQALPDVEQAVThacvINQAAATGGDARQLvgYLVSQsGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSA 952
|
....*....
gi 521099036 542 VGKILRRVL 550
Cdd:PRK10252 953 NGKLDRKAL 961
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
49-475 |
8.95e-30 |
|
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: 123.62 E-value: 8.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFA-AYLQneLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARaIVI 127
Cdd:cd05933 9 LTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN-ILV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 128 VSNfANTLEQIvanTQVKHvvltslgqMLPRAKGtlvdfVVKYVKGMVPKydLPGAISMRKALHKGR---------RLQY 198
Cdd:cd05933 86 VEN-QKQLQKI---LQIQD--------KLPHLKA-----IIQYKEPLKEK--EPNLYSWDEFMELGRsipdeqldaIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 199 VKPfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLRE-GRELVVTALPLYHVFALTVNCLLFIEMGG 277
Cdd:cd05933 147 QKP----NQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATvGQESVVSYLPLSHIAAQILDIWLPIKVGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SnLLITNPRDIPG-FVKELQKHPFTAITGVNTLFnalvnnEDFHE---LNFA--------------------NMKLSVGG 333
Cdd:cd05933 223 Q-VYFAQPDALKGtLVKTLREVRPTAFMGVPRVW------EKIQEkmkAVGAksgtlkrkiaswakgvgletNLKLMGGE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 334 -------GMAVQRaVAEKWKKITGVH--------------------------LLEGYGLTECS-PLVTGNPYDLADYSga 379
Cdd:cd05933 296 spsplfyRLAKKL-VFKKVRKALGLDrcqkfftgaapisretlefflslnipIMELYGMSETSgPHTISNPQAYRLLS-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 380 IGLPVPSTEVRIV--DDEGNvlnygqtGELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKD 457
Cdd:cd05933 373 CGKALPGCKTKIHnpDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKE 445
|
490
....*....|....*....
gi 521099036 458 MILVS-GFNVYPNEIEDVV 475
Cdd:cd05933 446 LIITAgGENVPPVPIEDAV 464
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
206-443 |
1.22e-29 |
|
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: 122.93 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYgPVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSnLLITNP 285
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTY-PFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGT-LYIDDG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKELQKH-----P---FTAITGVNTLFNALVNNEDFHELNFANMKLSV--GGGMA------VQR-AVAEKWKKI 348
Cdd:cd05921 243 KPMPGGFEETLRNlreisPtvyFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFyaGAGLSqdvwdrLQAlAVATVGERI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 349 TgvhLLEGYGLTECSPLVTgNPYDLADYSGAIGLPVPSTEVRIVDDEGNVlnygqtgELQVRGPQVMQGYWQRPEATKEV 428
Cdd:cd05921 323 P---MMAGLGATETAPTAT-FTHWPTERSGLIGLPAPGTELKLVPSGGKY-------EVRVKGPNVTPGYWRQPELTAQA 391
|
250
....*....|....*
gi 521099036 429 INEEGWLSTGDIVRF 443
Cdd:cd05921 392 FDEEGFYCLGDAAKL 406
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-544 |
1.48e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 119.79 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 204 SGEDIaFLQYTGGTTGVAKGAILTH----------RNMVA-------NVLQAKGAYGPVLRegrelvVTALPLYHvfALT 266
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVMWRQedifrmlmggADFGTgeftpseDAHKAAAAAAGTVM------FPAPPLMH--GTG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLFIEMGGSNLLITNPR-DIPGFVKELQKHPFTAITGVNT-----LFNALvnnEDFHELNFANMKLSVGGGMAVQRA 340
Cdd:cd05924 73 SWTAFGGLLGGQTVVLPDDRfDPEEVWRTIEKHKVTSMTIVGDamarpLIDAL---RDAGPYDLSSLFAISSGGALLSPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 341 VAEKW-KKITGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVriVDDEGNVLNYGQTGELQV--RGpQVMQG 417
Cdd:cd05924 150 VKQGLlELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWIarRG-HIPLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 418 YWQRPEATKE---VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVS 494
Cdd:cd05924 227 YYGDEAKTAEtfpEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERW 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 521099036 495 GEVVkIYVVKRDP--SLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGK 544
Cdd:cd05924 307 GQEV-VAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
28-558 |
2.27e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.12 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 28 MFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPL 107
Cdd:PRK12467 517 LIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 108 YtPRE-LEHQLNDADARAIVIVSNfanTLEQIVANTQVKHVVLtslgqmlprakgtlvdfvvkyvkgmvpkyDLPGAism 186
Cdd:PRK12467 596 Y-PQDrLAYMLDDSGVRLLLTQSH---LLAQLPVPAGLRSLCL-----------------------------DEPAD--- 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkaLHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMvANVLQAKGAYGPVLREGRELVVTALplyhVFALT 266
Cdd:PRK12467 640 ---LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVSTF----AFDLG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLFIEMGGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNfaNMKLSVGGGMAVQRAVAE 343
Cdd:PRK12467 712 VTELFGALASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPR--PQRALVCGGEALQVDLLA 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKKIT-GVHLLEGYGLTECSPLVTGNPYDLAD---YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYW 419
Cdd:PRK12467 790 RVRALGpGARLINHYGPTETTVGVSTYELSDEErdfGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYH 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 420 QRPEATKEVI-------NEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHE 492
Cdd:PRK12467 870 RRPALTAERFvpdpfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD 949
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099036 493 VSGEVVKiYVVKR------DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDAQL 558
Cdd:PRK12467 950 AGLQLVA-YLVPAavadgaEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAV 1020
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
27-550 |
3.67e-29 |
|
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: 120.62 E-value: 3.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARAIVivsnfantleqivanTQvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaism 186
Cdd:cd17644 83 NYPQERLTYILEDAQISVLL---------------TQ------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 rkalhkgrrlqyvkpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRELVVTALPlYHVFALT 266
Cdd:cd17644 105 ------------------PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG-ITSSDRVLQFASIA-FDVAAEE 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLFieMGGSNLLITNP--RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFAN-MKLSVGGGMAVQRAVAE 343
Cdd:cd17644 165 IYVTLL--SGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLPSsLRLVIVGGEAVQPELVR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWKKITG--VHLLEGYGLTECSplVTGNPYDLADYSGA------IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVM 415
Cdd:cd17644 243 QWQKNVGnfIQLINVYGPTEAT--IAATVCRLTQLTERnitsvpIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 416 QGYWQRPEATKE-VIN-------EEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAI 487
Cdd:cd17644 321 RGYLNRPELTAEkFIShpfnsseSERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVI 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 488 GQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17644 401 VREDQPGNKRLVAYIVpHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-550 |
1.85e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 117.44 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 211 LQYTGGTTGVAKgaiLTHRNMvANVLQAKGAYGPVLREGRELV-VTALPLYHVFALTVNCLLFIEMGGSNLLITNPRdiP 289
Cdd:PRK08308 106 LQYSSGTTGEPK---LIRRSW-TEIDREIEAYNEALNCEQDETpIVACPVTHSYGLICGVLAALTRGSKPVIITNKN--P 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 290 GFV-KELQKHPFTAITGVNTLFNALVN----NEDFHelnfANMKlsvgGGMAVQRAVAEKWKKITgVHLLEGYGLTE--C 362
Cdd:PRK08308 180 KFAlNILRNTPQHILYAVPLMLHILGRllpgTFQFH----AVMT----SGTPLPEAWFYKLRERT-TYMMQQYGCSEagC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 splVTGNPyDLADySGAIGLPVPSTEVRIVDDEGnvlnygQTGELQVRgpqvmqgywqrpeATKEVINeegwlsTGDIVR 442
Cdd:PRK08308 251 ---VSICP-DMKS-HLDLGNPLPHVSVSAGSDEN------APEEIVVK-------------MGDKEIF------TKDLGY 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 443 FDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPsLTKDELITHCRKHL 522
Cdd:PRK08308 301 KSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEE-IDPVQLREWCIQHL 379
|
330 340
....*....|....*....|....*...
gi 521099036 523 TGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:PRK08308 380 APYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
199-476 |
3.55e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 118.56 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 199 VKPFMSGED-IAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTALPLYHVFALTvnCLLFIEM-- 275
Cdd:PRK07768 144 IDPVETGEDdLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVETDVMVSWLPLFHDMGMV--GFLTVPMyf 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSNLLITnP----RDIPGFVKELQKHPFTAITGVNTLFNA----LVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKK 347
Cdd:PRK07768 220 GAELVKVT-PmdflRDPLLWAELISKYRGTMTAAPNFAYALlarrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLD 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ITGVH------LLEGYGLTEC------SPLVTGNPYDLAD-------------YSGAI------GLPVPSTEVRIVDDEG 396
Cdd:PRK07768 299 AGARFglrpeaILPAYGMAEAtlavsfSPCGAGLVVDEVDadllaalrravpaTKGNTrrlatlGPPLPGLEVRVVDEDG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 397 NVLNYGQTGELQVRGPQVMQGYwQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVA 476
Cdd:PRK07768 379 QVLPPRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAA 457
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
24-553 |
5.33e-28 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 118.31 E-value: 5.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAF-------INMGSV--MTFRKLEERSRAFAAYLQNELKlkKGDRVALMMPNLLQYPVALFGI 94
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYryldhshSAAGCAveLTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 95 LRAGMIAVnvnPLYTPR------ELEHQLNDADARAIVIVSNFANTLEQIVANtqvkhvvltslgqmLPRAKGTLVDFVv 168
Cdd:PRK12476 113 IKAGTIAV---PLFAPElpghaeRLDTALRDAEPTVVLTTTAAAEAVEGFLRN--------------LPRLRRPRVIAI- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 169 kyvkGMVPkyDLPGAismrkalhkgrrlQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLRE 248
Cdd:PRK12476 175 ----DAIP--DSAGE-------------SFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 249 GRElvVTALPLYHVFALTVncLLFIEMGGSNLLITNPRdipGFVKELQK--HPFTAITGVNTLFNALVN----------- 315
Cdd:PRK12476 236 THG--VSWLPLYHDMGLSM--IGFPAVYGGHSTLMSPT---AFVRRPQRwiKALSEGSRTGRVVTAAPNfayewaaqrgl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 316 NEDFHELNFANMKLsVGGGMAVQRAVAEKWKKITGVHLLE------GYGLTECSPLVTGNPYDL---------------- 373
Cdd:PRK12476 309 PAEGDDIDLSNVVL-IIGSEPVSIDAVTTFNKAFAPYGLPrtafkpSYGIAEATLFVATIAPDAepsvvyldreqlgagr 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 374 -----ADYSGAI-----GLPVPSTEVRIVD-DEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVIN-------EEG-- 433
Cdd:PRK12476 388 avrvaADAPNAVahvscGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlAEGsh 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 434 ---------WLSTGDI-VRFDenGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLE---VAAIGQPHEVSGEVVki 500
Cdd:PRK12476 468 adgaaddgtWLRTGDLgVYLD--GELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAEDNERLV-- 543
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 501 YVVKRDPSLTKD------ELITH--CRKHLTGYKVPKLIEfREELPKTNVGKILRRVLREE 553
Cdd:PRK12476 544 IVAERAAGTSRAdpapaiDAIRAavSRRHGLAVADVRLVP-AGAIPRTTSGKLARRACRAQ 603
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
49-456 |
5.89e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 118.54 E-value: 5.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIV 128
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLA-ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 SNFANTLEQIVANTQVKHVVLTSLGQmLP---RAKG-TLVDF--VVKyvKGMVPKYDLPGAISMRKalhkgrrlqyvkpf 202
Cdd:PTZ00216 201 GKNVPNLLRLMKSGGMPNTTIIYLDS-LPasvDTEGcRLVAWtdVVA--KGHSAGSHHPLNIPENN-------------- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 203 msgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKG----AYGPVlREGrELVVTALPLYHVFALTVNCLLFieMGGS 278
Cdd:PTZ00216 264 ---DDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDrlndLIGPP-EED-ETYCSYLPLAHIMEFGVTNIFL--ARGA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 279 NLLITNPRDI------P-GFVKELQkhPFTAItGVNTLFN------------------------------ALVNNED--- 318
Cdd:PTZ00216 337 LIGFGSPRTLtdtfarPhGDLTEFR--PVFLI-GVPRIFDtikkaveaklppvgslkrrvfdhayqsrlrALKEGKDtpy 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 319 FHELNFANMKLSVGGGMavqRAV-------AEKWKKITGVHL---LEGYGLTE---CSPL-VTGnpyDLadYSGAIGLPV 384
Cdd:PTZ00216 414 WNEKVFSAPRAVLGGRV---RAMlsgggplSAATQEFVNVVFgmvIQGWGLTEtvcCGGIqRTG---DL--EPNAVGQLL 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 385 PSTEVRIVDDEGnvlnYGQT------GELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKK 456
Cdd:PTZ00216 486 KGVEMKLLDTEE----YKHTdtpeprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-558 |
7.10e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 119.68 E-value: 7.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 6 LSRYPSDvpetinpdqyLSLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLL 85
Cdd:PRK12316 1996 PEAYPRG----------PGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSF 2064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 86 QYPVALFGILRAGMIAVNVNPLYtPRE-LEHQLNDADARAIVivsnfantleqivanTQvkhvvlTSLGQMLPRAKGtlv 164
Cdd:PRK12316 2065 ELVVALLAVLKAGGAYVPLDPNY-PAErLAYMLEDSGAALLL---------------TQ------RHLLERLPLPAG--- 2119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 165 dfvvkyvkgmVPKYDLPGAISMRkalhkGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANvLQAKGAYGP 244
Cdd:PRK12316 2120 ----------VARLPLDRDAEWA-----DYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH-CQAAGERYE 2183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 245 VLREGRELVVTALPlyhvFALTVNCLLFIEMGGSNLLITNP--RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDfHEL 322
Cdd:PRK12316 2184 LSPADCELQFMSFS----FDGAHEQWFHPLLNGARVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE-RDG 2258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 323 NFANMKLSVGGGMAVQRAVAEKWKK-ITGVHLLEGYGLTEC--SPLV-TGNPYDLADYSGA-IGLPVPSTEVRIVDDEGN 397
Cdd:PRK12316 2259 RPPAVRVYCFGGEAVPAASLRLAWEaLRPVYLFNGYGPTEAvvTPLLwKCRPQDPCGAAYVpIGRALGNRRAYILDADLN 2338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 398 VLNYGQTGELQVRGPQVMQGYWQRPEATKEVI------NEEGWL-STGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNE 470
Cdd:PRK12316 2339 LLAPGMAGELYLGGEGLARGYLNRPGLTAERFvpdpfsASGERLyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGE 2418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 471 IEDVVALHGKVLEVAAIGQpHEVSGEVVKIYVVKRDP-SLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRV 549
Cdd:PRK12316 2419 IEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKA 2497
|
....*....
gi 521099036 550 LREENDAQL 558
Cdd:PRK12316 2498 LPKPDVSQL 2506
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
214-550 |
8.28e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 117.02 E-value: 8.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 214 TGGTTGVAKGailthrnmVANVLQAKGAYG--------PVLREGRELVVtALPLYHVFALTVnCLLFIEMGGSnLLITNP 285
Cdd:PRK13383 182 TSGTTGKPKG--------VPRAPQLRSAVGvwvtildrTRLRTGSRISV-AMPMFHGLGLGM-LMLTIALGGT-VLTHRH 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 286 RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDfhELNFAN----MKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTE 361
Cdd:PRK13383 251 FDAEAALAQASLHRADAFTAVPVVLARILELPP--RVRARNplpqLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 362 CSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYwqRPEATKEVIneEGWLSTGDIV 441
Cdd:PRK13383 329 VGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY--TDGGGKAVV--DGMTSTGDMG 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 442 RFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPS-LTKDELITHCRK 520
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSgVDAAQLRDYLKD 484
|
330 340 350
....*....|....*....|....*....|
gi 521099036 521 HLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-550 |
2.78e-27 |
|
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: 115.06 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIvivsnfantleqIVANTQVKHVVLTSLGQMLPRAKGTLVDFVVKyvkgmvpkydlpgaismrkalhkgrrlq 197
Cdd:cd12114 81 ADAGARLV------------LTDGPDAQLDVAVFDVLILDLDALAAPAPPPP---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yVKPFMSgeDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREGRELVVTAL----PLYHVFALTVncllfi 273
Cdd:cd12114 121 -VDVAPD--DLAYVIFTSGSTGTPKGVMISHRA-ALNTILDINRRFAVGPDDRVLALSSLsfdlSVYDIFGALS------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 274 eMGGSnLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVN---NEDFHELNFANMKLSvGGGMAVQ--RAVAEKW 345
Cdd:cd12114 191 -AGAT-LVLPDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDvleAAQALLPSLRLVLLS-GDWIPLDlpARLRALA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 346 KKITGVHLleGyGLTECSplVTGNPYDLAD---YSGAI--GLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQ 420
Cdd:cd12114 268 PDARLISL--G-GATEAS--IWSIYHPIDEvppDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLG 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 421 RPEATKE--VINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAI--GQPHEVS 494
Cdd:cd12114 343 DPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVvlGDPGGKR 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 521099036 495 geVVKIYVVKRD-PSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd12114 423 --LAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-550 |
4.37e-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: 114.10 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIvsnfantleqivantqvkhvvltslgqmlprakgtlvdfvvkyvkgmvpkydLPgaismrkalhkgrrlq 197
Cdd:cd17650 81 EDSGAKLLLT----------------------------------------------------QP---------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGRELVVTALPLYHVFALTVNCLLFiemGG 277
Cdd:cd17650 93 --------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLN---GG 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 278 SnlLITNPRDI----PGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGmavqRAVAEKWKK------ 347
Cdd:cd17650 162 T--LVICPDEVkldpAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS----DGCKAQDFKtlaarf 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 348 ITGVHLLEGYGLTECSPLVTGNPYDLADYSGA----IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPE 423
Cdd:cd17650 236 GQGMRIINSYGVTEATIDSTYYEEGRDPLGDSanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 424 ATKEVINEEGWLS------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQpHEVSGEV 497
Cdd:cd17650 316 LTAERFVENPFAPgermyrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVR-EDKGGEA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 521099036 498 -VKIYVVKRDpSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17650 395 rLCAYVVAAA-TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-552 |
5.60e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 109.36 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 175 VPKYDLPGAISMRKALHKGRRLQyvkpfmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANvlqAKGAYGPVLREGRELVv 254
Cdd:PRK07824 12 VPAQDERRAALLRDALRVGEPID--------DDVALVVATSGTTGTPKGAMLTAAALTAS---ADATHDRLGGPGQWLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 255 tALPLYHVFALTVncLLFIEMGGSNLLIT------NPRDIPGFVKELQ-KHPFTAITGVNtLFNALVNNEDFHELNFANM 327
Cdd:PRK07824 80 -ALPAHHIAGLQV--LVRSVIAGSEPVELdvsagfDPTALPRAVAELGgGRRYTSLVPMQ-LAKALDDPAATAALAELDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 328 KLsVGGGmAVQRAVAEKWKKItGVHLLEGYGLTECSplvTGNPYDladysgaiGLPVPSTEVRIVDdegnvlnygqtGEL 407
Cdd:PRK07824 156 VL-VGGG-PAPAPVLDAAAAA-GINVVRTYGMSETS---GGCVYD--------GVPLDGVRVRVED-----------GRI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 408 QVRGPQVMQGYwqRPEATKEVINEEGWLSTGDIVRFDeNGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAI 487
Cdd:PRK07824 211 ALGGPTLAKGY--RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 488 GQPHEVSGE-VVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK07824 288 GLPDDRLGQrVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-552 |
7.30e-26 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 111.37 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVS 129
Cdd:cd05915 26 TYAEVYQRARRLMGGL-RALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVAntqvkhvVLTSLGQMlPRAKGtlvdfvvkyvkgmvpKYDlpgaiSMRKALHKGR-RLQYVKPFMSGEDI 208
Cdd:cd05915 105 NLLPLVEAIRG-------ELKTVQHF-VVMDE---------------KAP-----EGYLAYEEALgEEADPVRVPERAAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AfLQYTGGTTGVAKGAILTHRNMVANVlQAKGAYGPVLREGRELVVTALPLYHV----FALTVNCLlfiemGGSNLLITN 284
Cdd:cd05915 157 G-MAYTTGTTGLPKGVVYSHRALVLHS-LAASLVDGTALSEKDVVLPVVPMFHVnawcLPYAATLV-----GAKQVLPGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 285 PRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFAnMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSP 364
Cdd:cd05915 230 RLDPASLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLK-TLRRLVVGGSAAPRSLIARFERMGVEVRQGYGLTETSP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 365 LVTGNPY-------------------DLADYSGAIGLPVPSTEVriVDDEGNVLNYgqtgeLQVRGPQVMQGYWQRPEAT 425
Cdd:cd05915 309 VVVQNFVkshleslseeekltlkaktGLPIPLVRLRVADEEGRP--VPKDGKALGE-----VQLKGPWITGGYYGNEEAT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 426 KEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKR 505
Cdd:cd05915 382 RSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR 461
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 506 DPSLTKDELITHCRKHLTGYK-VPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:cd05915 462 GEKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
37-558 |
9.18e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 111.77 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 37 ADQPAFI----NMGSV--MTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTP 110
Cdd:PRK00174 81 GDKVAIIwegdDPGDSrkITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 111 RELEHQLNDADARAIV----------IVSNFANTLEQIVANTQVKHVVltslgqmlprakgtlvdfVVKYVKGMVPkydl 180
Cdd:PRK00174 160 EALADRIIDAGAKLVItadegvrggkPIPLKANVDEALANCPSVEKVI------------------VVRRTGGDVD---- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 181 pgaismrkaLHKGRRLQY----------VKP-FMSGEDIAFLQYTGGTTGVAKGailthrnmvanVLQAKGAYgpvlreg 249
Cdd:PRK00174 218 ---------WVEGRDLWWhelvagasdeCEPePMDAEDPLFILYTSGSTGKPKG-----------VLHTTGGY------- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 250 reLVVTALPLYHVFALTVN----C-----------------LLfieMGGSNLL---ITNPRDIPGFVKELQKHP----FT 301
Cdd:PRK00174 271 --LVYAAMTMKYVFDYKDGdvywCtadvgwvtghsyivygpLA---NGATTLMfegVPNYPDPGRFWEVIDKHKvtifYT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 302 AITGVNTLF---NALVNNEDFHELnfanmKL--SVG------GGMAVQRAVAEK--------WKKITGVHLLegygltec 362
Cdd:PRK00174 346 APTAIRALMkegDEHPKKYDLSSL-----RLlgSVGepinpeAWEWYYKVVGGErcpivdtwWQTETGGIMI-------- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 SPLvtgnPydladysGAI-------GLPVPSTEVRIVDDEGNVLNYGQTGELQVRG--PQVMQGYWQRPEATKEVI--NE 431
Cdd:PRK00174 413 TPL----P-------GATplkpgsaTRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHERFVKTYfsTF 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 432 EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRD---PS 508
Cdd:PRK00174 482 KGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGgeePS 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 521099036 509 LT-KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE--ENDAQL 558
Cdd:PRK00174 562 DElRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKiaEGEEIL 614
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
213-446 |
9.95e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 111.68 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 213 YTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVLREGRELVVTALPLYHVFALTV--NCLLFiemGGSNLLITNPRDIPG 290
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNAnfNGLLW---GGGTLYIDDGKPLPG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 291 FVKELQKH-----P---FTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWK----KITG--VHLLEG 356
Cdd:PRK12582 304 MFEETIRNlreisPtvyGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQalavRTTGhrIPFYTG 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTECSPLVTGNPYDlADYSGAIGLPVPSTEVRIVDDegnvlnyGQTGELQVRGPQVMQGYWQRPEATKEVINEEGWLS 436
Cdd:PRK12582 384 YGATETAPTTTGTHWD-TERVGLIGLPLPGVELKLAPV-------GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYR 455
|
250
....*....|.
gi 521099036 437 TGDIVRF-DEN 446
Cdd:PRK12582 456 LGDAARFvDPD 466
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
49-550 |
3.79e-25 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 108.26 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIViv 128
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 snfantleqivanTQVKhvvltslgqmlprakgtlvdfvvkyvkgmvpkydlpgaismrkalhkgrrlqyvkpfmsgeDI 208
Cdd:cd17648 91 -------------TNST-------------------------------------------------------------DL 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 AFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpVLREGRElVVTALPLYhVFALTVNCLLFIEMGGSNLLITNPR-- 286
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDE-AVLFFSNY-VFDFFVEQMTLALLNGQKLVVPPDEmr 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 -DIPGFVKELQKHPFTAITGVNTLfnalVNNEDFHELNFANMKLSVGggMAVQRAVAEKWKKITGVHLLEGYGLTECSPL 365
Cdd:cd17648 174 fDPDRFYAYINREKVTYLSGTPSV----LQQYDLARLPHLKRVDAAG--EEFTAPVFEKLRSRFAGLIINAYGPTETTVT 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 366 VTGNPYDLAD-YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKE--VIN-----EEGWLS- 436
Cdd:cd17648 248 NHKRFFPGDQrFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAErfLPNpfqteQERARGr 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 437 ------TGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKI-----YVVKR 505
Cdd:cd17648 328 narlykTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylvgYYLPE 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 521099036 506 DPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:cd17648 408 PGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
24-459 |
4.77e-25 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 109.82 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQP----------AFINMGSVMTFRKLE-------------ERSRAFAAYLQNeLKLKKGDRVALM 80
Cdd:PLN02387 59 TLAALFEQSCKKYSDKRllgtrklisrEFETSSDGRKFEKLHlgeyewitygqvfERVCNFASGLVA-LGHNKEERVAIF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 81 MPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVAN-TQVKHVV-LTSLGQMLPR 158
Cdd:PLN02387 138 ADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQlETVKRVIyMDDEGVDSDS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 159 AKGTLVDFVVKyvkgmvpkydlpgAISMRKALHKGRRLQYVKPfmSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVlQA 238
Cdd:PLN02387 218 SLSGSSNWTVS-------------SFSEVEKLGKENPVDPDLP--SPNDIAVIMYTSGSTGLPKGVMMTHGNIVATV-AG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 239 KGAYGPVLrEGRELVVTALPLYHVFALTVNCLLF---IEMG-GSNLLITN-----PRDIPGFVKELQKHPFTAI------ 303
Cdd:PLN02387 282 VMTVVPKL-GKNDVYLAYLPLAHILELAAESVMAavgAAIGyGSPLTLTDtsnkiKKGTKGDASALKPTLMTAVpaildr 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 304 --TGV-----------NTLFN-------ALVNNEDF----------HELNFANMKLSVGG-------GMAVQRAVAEKWK 346
Cdd:PLN02387 361 vrDGVrkkvdakgglaKKLFDiaykrrlAAIEGSWFgawglekllwDALVFKKIRAVLGGrirfmlsGGAPLSGDTQRFI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 347 KIT-GVHLLEGYGLTECSPLVTGNPYDlaDYS-GAIGLPVPSTEVRIVD-DEGNVLNYGQT---GELQVRGPQVMQGYWQ 420
Cdd:PLN02387 441 NIClGAPIGQGYGLTETCAGATFSEWD--DTSvGRVGPPLPCCYVKLVSwEEGGYLISDKPmprGEIVIGGPSVTLGYFK 518
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 521099036 421 RPEATKEV--INEEG--WLSTGDIVRFDENGMIYIVDRKKDMI 459
Cdd:PLN02387 519 NQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-553 |
5.69e-25 |
|
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: 108.92 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 46 GSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAI 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 VIVSNFANTLEQIVANTQVKHVVLTSLGQ-MLPRAKGTLVDFVVKYVKGMVPKyDLPGAISMRkalhkgrrlqyvkpfms 204
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSVWYLSHtSNTEGVISLLDKVDAASDEPVPA-SLRAHVTIK----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 geDIAFLQYTGGTTGVAKGAILTHRN--MVANVLQAKGAygpvlrEGRELVVTALPLYHVFALTVNCLLFIEMGGSnlLI 282
Cdd:cd05938 145 --SPALYIYTSGTTGLPKAARISHLRvlQCSGFLSLCGV------TADDVIYITLPLYHSSGFLLGIGGCIELGAT--CV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNPR-DIPGFVKELQKHPFTAITGVNTLFNALVN-----NEDFHelnfaNMKLSVGGGMAvqravAEKWK----KITGVH 352
Cdd:cd05938 215 LKPKfSASQFWDDCRKHNVTVIQYIGELLRYLCNqpqspNDRDH-----KVRLAIGNGLR-----ADVWReflrRFGPIR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 LLEGYGLTE-----------CSPLVTGN-------PYDLADYSgaiglpvPSTEVRIVDDEGNVLNY--GQTGEL--QVR 410
Cdd:cd05938 285 IREFYGSTEgnigffnytgkIGAVGRVSylykllfPFELIKFD-------VEKEEPVRDAQGFCIPVakGEPGLLvaKIT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 411 GPQVMQGYWQRPEATKEV----INEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEV 484
Cdd:cd05938 358 QQSPFLGYAGDKEQTEKKllrdVFKKGdvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521099036 485 AAIGQP---HEvsGEVVKIYVVKRDP-SLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:cd05938 438 NVYGVTvpgHE--GRIGMAAVKLKPGhEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
27-561 |
6.84e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.43 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 27 EMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNP 106
Cdd:PRK12316 3061 RLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-ERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDP 3139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 107 LYTPRELEHQLNDADARaivivsnfantleqivantqvkhVVLTSLGQMLPRAKGtlvdfvvkyVKGMVPKYDLPGAISM 186
Cdd:PRK12316 3140 EYPEERLAYMLEDSGAQ-----------------------LLLSQSHLRLPLAQG---------VQVLDLDRGDENYAEA 3187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 187 RKALHkgrrlqyvkpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTALPLYHVFALT 266
Cdd:PRK12316 3188 NPAIR-----------TMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYG--LGVGDRVLQFTTFSFDVFVEE 3254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNCLLfieMGGSNLLITNPR---DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELnfANMKLSVGGGMAVQRAVAE 343
Cdd:PRK12316 3255 LFWPL---MSGARVVLAGPEdwrDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHRC--TSLKRIVCGGEALPADLQQ 3329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 344 KWkkITGVHLLEGYGLTECSplVTGNPYDLADYSGA---IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQ 420
Cdd:PRK12316 3330 QV--FAGLPLYNLYGPTEAT--ITVTHWQCVEEGKDavpIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHN 3405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 421 RPEATKE------VINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIgqphEVS 494
Cdd:PRK12316 3406 RPGLTAErfvpdpFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL----AVD 3481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 495 GEVVKIYVVKRDPSLT-KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLrEENDAQLAEQ 561
Cdd:PRK12316 3482 GRQLVAYVVPEDEAGDlREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL-PRPDAALLQQ 3548
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-553 |
1.16e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.84 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 38 DQPAFINMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQL 117
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 118 NDADARAIVIVSNFANTLEQIVANTQVKHVVLTSLGQMLPRAKGTLVDFVVkyvkgmvpkydlpgaismrkalhkgrrlq 197
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRV----------------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 198 yvkpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMV--ANVLQAKGAYGPvlregRELVVTALPLYHVFALTVNCLLFIEM 275
Cdd:PRK07867 149 -----ADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsaGVMLAQRFGLGP-----DDVCYVSMPLFHSNAVMAGWAVALAA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 276 GGSnllITNPR--DIPGFVKELQKHPFTAITGVNTLFNALVNNEDfhELNFANMKLSVG-GGMAVQRAVAEKWKKItGVH 352
Cdd:PRK07867 219 GAS---IALRRkfSASGFLPDVRRYGATYANYVGKPLSYVLATPE--RPDDADNPLRIVyGNEGAPGDIARFARRF-GCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 353 LLEGYGLTECSPLVTGNPydlADYSGAIGLPVPstEVRIVD------------DEGNVLNYGQ-TGEL-QVRGPQVMQGY 418
Cdd:PRK07867 293 VVDGFGSTEGGVAITRTP---DTPPGALGPLPP--GVAIVDpdtgtecppaedADGRLLNADEaIGELvNTAGPGGFEGY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 419 WQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVV 498
Cdd:PRK07867 368 YNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 499 KIYVV-KRDPSLTKDEL--ITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK07867 447 MAALVlAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
190-487 |
5.87e-24 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 106.26 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 190 LHKGRRLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMV---ANVLQAKGAYGPVLREgRELVVTALPLYHVFALT 266
Cdd:PLN02614 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVtliAGVIRLLKSANAALTV-KDVYLSYLPLAHIFDRV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VN-CllFIEMGGS--------NLLITN------------PRDIP-----------------------------GFVKELQ 296
Cdd:PLN02614 286 IEeC--FIQHGAAigfwrgdvKLLIEDlgelkptifcavPRVLDrvysglqkklsdggflkkfvfdsafsykfGNMKKGQ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 297 KHpftaiTGVNTLFNALVNNEDFHELNfANMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTE-CSPLVTGNPYDLaD 375
Cdd:PLN02614 364 SH-----VEASPLCDKLVFNKVKQGLG-GNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLPDEL-D 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 376 YSGAIGLPVPSTEVR---IVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIV 452
Cdd:PLN02614 437 MLGTVGPPVPNVDIRlesVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKII 515
|
330 340 350
....*....|....*....|....*....|....*.
gi 521099036 453 DRKKDMI-LVSGFNVYPNEIEDVvalHGKVLEVAAI 487
Cdd:PLN02614 516 DRKKNIFkLSQGEYVAVENIENI---YGEVQAVDSV 548
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
331-552 |
6.17e-24 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 104.57 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 331 VGGGMAVQRAVAEKWKKITGVHLLEGYGLTECSPLVTGNPYDLADySGAIGLPVPSTEVRIVDDEGNVLNYGQ-TGELQV 409
Cdd:cd05974 206 VGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVK-AGSMGRPLPGYRVALLDPDGAPATEGEvALDLGD 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 410 RGPQ-VMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIG 488
Cdd:cd05974 285 TRPVgLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVP 363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 489 QPHEVSGEVVKIYVV-----KRDPSLTKDeLITHCRKHLTGYKVPKLIEFReELPKTNVGKILRRVLRE 552
Cdd:cd05974 364 SPDPVRLSVPKAFIVlragyEPSPETALE-IFRFSRERLAPYKRIRRLEFA-ELPKTISGKIRRVELRR 430
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
49-527 |
1.29e-23 |
|
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: 104.08 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLqNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIviv 128
Cdd:cd05910 3 LSFRELDERSDRIAQGL-TAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 snfantleqivantqvkhvvltsLGqmlprakgtlvdfvvkyvkgmVPKYDLPGAISmrkalhkgrrlqyvkpfmsgedi 208
Cdd:cd05910 79 -----------------------IG---------------------IPKADEPAAIL----------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 209 aflqYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPVlREGRELvvTALPLYHVFALTVNCLLFI-EMGGSNLLITNPRD 287
Cdd:cd05910 92 ----FTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR-PGEVDL--ATFPLFALFGPALGLTSVIpDMDPTRPARADPQK 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 288 IPGFvkeLQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKIT--GVHLLEGYGLTECSPL 365
Cdd:cd05910 165 LVGA---IRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 366 VTGNPYDLADYSGA---------IGLPVPSTEVRIV--DDEG-------NVLNYGQTGELQVRGPQVMQGYWQRPEAT-- 425
Cdd:cd05910 242 SSIGSRELLATTTAatsggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTPTYVNRPVATal 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 426 -KEVINEEG-WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVA--AIGQPhevsGEVVKIY 501
Cdd:cd05910 322 aKIDDNSEGfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSAlvGVGKP----GCQLPVL 397
|
490 500 510
....*....|....*....|....*....|..
gi 521099036 502 VVKRDPSLTKD------ELITHCRKHLTGYKV 527
Cdd:cd05910 398 CVEPLPGTITPrarleqELRALAKDYPHTQRI 429
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
206-553 |
1.54e-22 |
|
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: 100.58 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILT-HRNMVANVLQAKGAygpVLREGrELVVTALPLYHVFAL---TVNCLlfieMGGSNLL 281
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISwRRTLVTSNLLSHDL---NLKNG-DRTYTCMPLYHGTAAflgACNCL----MSGGTLA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 282 ITNPRDIPGFVKELQKHPFTAITGVNTLFNALVN-----NEDFHelnfaNMKLSVGGGMAVQraVAEKWKKITGVHLL-E 355
Cdd:cd05937 159 LSRKFSASQFWKDVRDSGATIIQYVGELCRYLLStppspYDRDH-----KVRVAWGNGLRPD--IWERFRERFNVPEIgE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 356 GYGLTEcSPLVTGNPYDLADYSGAIGL--------------PV---PSTEVRIVDDEGN---VLNYGQTGELQVRGP--- 412
Cdd:cd05937 232 FYAATE-GVFALTNHNVGDFGAGAIGHhglirrwkfenqvvLVkmdPETDDPIRDPKTGfcvRAPVGEPGEMLGRVPfkn 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 413 -QVMQGYWQRPEATK----EVINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVA 485
Cdd:cd05937 311 rEAFQGYLHNEDATEsklvRDVFRKGdiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAN 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 486 AIG---QPHE--VSGEVVKIYVVKRDPS-LTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:cd05937 391 VYGvkvPGHDgrAGCAAITLEESSAVPTeFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
50-553 |
2.16e-22 |
|
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: 100.19 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNElKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIvs 129
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 nfantleqivantqvkhvvltslgqmlprakgTLVDFVVKYVKGMVPKYDLPGAISmrkalhkgrRLQYVkpfmsgedia 209
Cdd:cd05939 82 --------------------------------NLLDPLLTQSSTEPPSQDDVNFRD---------KLFYI---------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 flqYTGGTTGVAKGAILTHRNMVAnvLQAKGAYGPVLREgRELVVTALPLYHVFALTV---NCLLFiemgGSNLLITNPR 286
Cdd:cd05939 111 ---YTSGTTGLPKAAVIVHSRYYR--IAAGAYYAFGMRP-EDVVYDCLPLYHSAGGIMgvgQALLH----GSTVVIRKKF 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 287 DIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAvqravAEKWKKITG----VHLLEGYGLTEC 362
Cdd:cd05939 181 SASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLR-----PQIWEQFVRrfgiPQIGEFYGATEG 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 363 splvTGNPYDLADYSGAIG-LPV------PSTEVRIVDDEGNVL----------NYGQTGEL-----QVRGPQVMQGYWQ 420
Cdd:cd05939 256 ----NSSLVNIDNHVGACGfNSRilpsvyPIRLIKVDEDTGELIrdsdglcipcQPGEPGLLvgkiiQNDPLRRFDGYVN 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 421 RPEATKEVINE-----EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQ--PHeV 493
Cdd:cd05939 332 EGATNKKIARDvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPG-V 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099036 494 SGEV--VKIYVVKRDPSLtkDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:cd05939 411 EGRAgmAAIVDPERKVDL--DRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
69-454 |
6.12e-22 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 99.51 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 69 LKLKK--GDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKH 146
Cdd:PRK06334 60 TKVSKypDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGEDAEYP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 147 VVLTSLGQMlpRAKGTLVDfvvKYVKGMVPKYDLPGAISMRKALHKGRrlqyvkpfmsgEDIAFLQYTGGTTGVAKGAIL 226
Cdd:PRK06334 140 FSLIYMEEV--RKELSFWE---KCRIGIYMSIPFEWLMRWFGVSDKDP-----------EDVAVILFTSGTEKLPKGVPL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 227 THRNMVANVLQAKGAYGPvlrEGRELVVTALPLYHVFALTVNCLLFIEMGGSNLLITNPRDIPGFVKELQKHPFTAITGV 306
Cdd:PRK06334 204 THANLLANQRACLKFFSP---KEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPLYPKKIVEMIDEAKVTFLGST 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 307 NTLFNALVNNEDFHELNFANMKLSVGGGMAVQRAVAEKWKKI-TGVHLLEGYGLTECSPLVTGNPYDLADYSGAIGLPVP 385
Cdd:PRK06334 281 PVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTECSPVITINTVNSPKHESCVGMPIR 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 386 STEVRIVDDEGNV-LNYGQTGELQVRGPQVMQGYWQRPEATKEV-INEEGWLSTGDIVRFDENGMIYIVDR 454
Cdd:PRK06334 361 GMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDRHGELFLKGR 431
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
350-553 |
9.58e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 98.95 E-value: 9.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 350 GVHLLEGYGLTECSPLVTGNPydlADYSGAIGLPVPSteVRIVDDE-------------GNVLNYGQT-GEL-QVRGPQV 414
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREP---GTPPGSIGRGAPG--VAIYNPEtltecavarfdahGALLNADEAiGELvNTAGAGF 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 415 MQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVS 494
Cdd:PRK13388 363 FEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521099036 495 GEVVKIYVVKRDP-SLTKDELIT--HCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREE 553
Cdd:PRK13388 442 GDQVMAALVLRDGaTFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
24-553 |
1.63e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 98.04 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 24 SLVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVAL---MMPNLLqypVALFGILRAG-- 98
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFID-SLKLPDKSPIIVfghMSPEML---ATFLGAVKAGha 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 99 MIAVNVnplYTPRE-LEHQLNDADARAIVIVSNFANTLEQIvantqvkHVVltslgqmlprakgTLVDFVVKYVKGMVPK 177
Cdd:PRK04813 79 YIPVDV---SSPAErIEMIIEVAKPSLIIATEELPLEILGI-------PVI-------------TLDELKDIFATGNPYD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 178 YDlpgaismrkalhkgrrlQYVKpfmsGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVvtAL 257
Cdd:PRK04813 136 FD-----------------HAVK----GDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFA--LPEGPQFL--NQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 258 PLYHvFALTV----NCLLfieMGGSnlLITNPRDIPGFVKELqkhpFTAItgVNTLFNALVN----------NEDFHELN 323
Cdd:PRK04813 191 APYS-FDLSVmdlyPTLA---SGGT--LVALPKDMTANFKQL----FETL--PQLPINVWVStpsfadmcllDPSFNEEH 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 324 FANMKLSVGGGMAVQRAVAEKWK-KITGVHLLEGYGLTECSPLVTG---NPYDLADY-SGAIGLPVPSTEVRIVDDEGNV 398
Cdd:PRK04813 259 LPNLTHFLFCGEELPHKTAKKLLeRFPSATIYNTYGPTEATVAVTSieiTDEMLDQYkRLPIGYAKPDSPLLIIDEEGTK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 399 LNYGQTGELQVRGPQVMQGYWQRPEATKEVINE-EGWLS--TGDIVRFDeNGMIYIVDRKKDMIlvsGFNVYPNEIEDVV 475
Cdd:PRK04813 339 LPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTfDGQPAyhTGDAGYLE-DGLLFYQGRIDFQI---KLNGYRIELEEIE 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 476 ALHGKVLEV-AAIGQPHEVSGEVVKI--YVVKRDPSLTKDELITHCRK-----HLTGYKVPKLIEFREELPKTNVGKILR 547
Cdd:PRK04813 415 QNLRQSSYVeSAVVVPYNKDHKVQYLiaYVVPKEEDFEREFELTKAIKkelkeRLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
....*.
gi 521099036 548 RVLREE 553
Cdd:PRK04813 495 KALIEE 500
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
357-562 |
1.78e-21 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 97.37 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 357 YGLTE-CSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDdegnvlnyGQTGELQVRGPQVMQGYWQrpeatkEVINEEGWL 435
Cdd:PRK07445 261 YGMTEtASQIATLKPDDFLAGNNSSGQVLPHAQITIPA--------NQTGNITIQAQSLALGYYP------QILDSQGIF 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 436 STGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGE-VVKIYVVKrDPSLTKDEL 514
Cdd:PRK07445 327 ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEvVTAIYVPK-DPSISLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521099036 515 ITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLReendaQLAEQK 562
Cdd:PRK07445 406 KTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ-----QIAVQR 448
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
50-486 |
4.62e-21 |
|
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: 97.03 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 50 TFRKLEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARaiVIVS 129
Cdd:cd05905 16 TWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR--VALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 130 NFANTLEQIVANTQVKHVVLTSLGQMLPRakgtLVDFVvkyvkgmvpkydlpgAISMRKALHKgrRLQYVKPFMSGEDIA 209
Cdd:cd05905 94 VEACLKGLPKKLLKSKTAAEIAKKKGWPK----ILDFV---------------KIPKSKRSKL--KKWGPHPPTRDGDTA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELvVTALPLYHVFALTVNCLLFIEMGGSNLLI------T 283
Cdd:cd05905 153 YIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACE--LYESRPL-VTVLDFKSGLGLWHGCLLSVYSGHHTILIppelmkT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 NPrdiPGFVKELQKHP-FTAITGVNTLFNALVN------NEDFHELNFANMK-LSVGGGMAVQRAVAEKWKKITGVHlle 355
Cdd:cd05905 230 NP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDlsstlaSLKNRDVNLSSLRmCMVPCENRPRISSCDSFLKLFQTL--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 356 GYGLTECSPLVTG--NPY-DLADYSGAI--------------------------------GLPVPSTEVRIVDDEG-NVL 399
Cdd:cd05905 304 GLSPRAVSTEFGTrvNPFiCWQGTSGPEpsrvyldmralrhgvvrlderdkpnslplqdsGKVLPGAQVAIVNPETkGLC 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 400 NYGQTGELQVRGPQVMQGYWQRPEATK------------EVINEEGWLSTGDI----------VRFDENGMIYIVDRKKD 457
Cdd:cd05905 384 KDGEIGEIWVNSPANASGYFLLDGETNdtfkvfpstrlsTGITNNSYARTGLLgflrptkctdLNVEEHDLLFVVGSIDE 463
|
490 500 510
....*....|....*....|....*....|
gi 521099036 458 MILVSGFNVYPNEIED-VVALHGKVLEVAA 486
Cdd:cd05905 464 TLEVRGLRHHPSDIEAtVMRVHPYRGRCAV 493
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
470-544 |
2.03e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 85.29 E-value: 2.03e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 470 EIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVV-KRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGK 544
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVlKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
204-561 |
3.60e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.07 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 204 SGED-IAFLQYTGGTTGVAKGAILTHRNMVANVLqAKGAYgPVLREGRELVVTAlplYHVFALTVNCLLFIEMGGSNLLI 282
Cdd:PRK05691 3866 SGPDnLAYVIYTSGSTGLPKGVMVEQRGMLNNQL-SKVPY-LALSEADVIAQTA---SQSFDISVWQFLAAPLFGARVEI 3940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TnPRDIP----GFVKELQKHPFTAITGVNTLFNALVNNEdfhELNFANMKLSVGGGMAVQRAVAEKW-KKITGVHLLEGY 357
Cdd:PRK05691 3941 V-PNAIAhdpqGLLAHVQAQGITVLESVPSLIQGMLAED---RQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAY 4016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 358 GLTECSPLVTGNPYDLADYSGA---IGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINE--- 431
Cdd:PRK05691 4017 GPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPhpf 4096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 432 ----EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEvAAIGQPHEVSGEVVKIYVVKRDP 507
Cdd:PRK05691 4097 gapgERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQT 4175
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 508 SLTKDELITHCRKHLTG----YKVPKLIEFREELPKTNVGKILRRVLREENDAQLAEQ 561
Cdd:PRK05691 4176 VLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ 4233
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
37-551 |
9.88e-18 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 86.54 E-value: 9.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 37 ADQPAFI------NMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTP 110
Cdd:PRK10524 67 PEQLALIavstetDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFAS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 111 RELEHQLNDADARAIVI---------VSNFANTLEQIVANTQVK--HVVLTSLG-QMLPRAKGTLVDFVvkyvkgmvpky 178
Cdd:PRK10524 146 HSLAARIDDAKPVLIVSadagsrggkVVPYKPLLDEAIALAQHKprHVLLVDRGlAPMARVAGRDVDYA----------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 179 dlpgaiSMRkALHKGRRLQYVkpFMSGEDIAFLQYTGGTTGVAKGailthrnmvanVLQAKGAYGPVLREGRELVVTALP 258
Cdd:PRK10524 215 ------TLR-AQHLGARVPVE--WLESNEPSYILYTSGTTGKPKG-----------VQRDTGGYAVALATSMDTIFGGKA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 259 ----------------LYHVFALTVNCLLFIEMGGsnlLITNPRdiPGFVKEL-QKHP----FTAITGVNTLFN---ALV 314
Cdd:PRK10524 275 getffcasdigwvvghSYIVYAPLLAGMATIMYEG---LPTRPD--AGIWWRIvEKYKvnrmFSAPTAIRVLKKqdpALL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 315 NNEDFHELnfanmKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTEcsplvTGNPY--------DLADYSGAIGLPVPS 386
Cdd:PRK10524 350 RKHDLSSL-----RALFLAGEPLDEPTASWISEALGVPVIDNYWQTE-----TGWPIlaiargveDRPTRLGSPGVPMYG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 387 TEVRIVDDE-GNVLNYGQTGELQVRGP--------------QVMQGYWQRpeatkevINEEGWlSTGDIVRFDENGMIYI 451
Cdd:PRK10524 420 YNVKLLNEVtGEPCGPNEKGVLVIEGPlppgcmqtvwgdddRFVKTYWSL-------FGRQVY-STFDWGIRDADGYYFI 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 452 VDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKD---------ELITHCRKHL 522
Cdd:PRK10524 492 LGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlalekEIMALVDSQL 571
|
570 580
....*....|....*....|....*....
gi 521099036 523 TGYKVPKLIEFREELPKTNVGKILRRVLR 551
Cdd:PRK10524 572 GAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-560 |
1.21e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.49 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 49 MTFRKLEERSRAFAAYLQNeLKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAIVIv 128
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 129 snfANTLEQIVANTQVKHVVLTSLGQmlPRAKGTLVDFVVKYvkgmvpkydlPGAISMRKALHK---GRRL--QYVKP-- 201
Cdd:PLN02654 199 ---CNAVKRGPKTINLKDIVDAALDE--SAKNGVSVGICLTY----------ENQLAMKREDTKwqeGRDVwwQDVVPny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 202 -------FMSGEDIAFLQYTGGTTGVAKGailthrnmvanVLQAKGAYgpvlregreLVVTALPLYHVFAL--------T 266
Cdd:PLN02654 264 ptkceveWVDAEDPLFLLYTSGSTGKPKG-----------VLHTTGGY---------MVYTATTFKYAFDYkptdvywcT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNC--------LLFIEM--GGSNLLITNPRDIP--GFVKEL-QKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGG 333
Cdd:PLN02654 324 ADCgwitghsyVTYGPMlnGATVLVFEGAPNYPdsGRCWDIvDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLRVLG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 334 --GMAVQRAVAEKWKKITG---VHLLEGYGLTECSP-LVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNVLNYGQTGEL 407
Cdd:PLN02654 404 svGEPINPSAWRWFFNVVGdsrCPISDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYL 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 408 QVRGP-----QVMQGYWQRPEAT--KEVineEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGK 480
Cdd:PLN02654 484 CVKKSwpgafRTLYGDHERYETTyfKPF---AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 481 VLEVAAIGQPHEVSGEVVKIYVVKRDPSLTKDE----LITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLREENDA 556
Cdd:PLN02654 561 CAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrksLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIASR 640
|
....
gi 521099036 557 QLAE 560
Cdd:PLN02654 641 QLDE 644
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-561 |
1.73e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNV 104
Cdd:PRK05691 2190 LHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALR-ERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPL 2268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 105 NPLYtPRELEHQLNDaDARAIVIVSNFAntleqivantqvkhvVLTSLGQmLPR--AKGTLVDfvvkyvkgmvpkyDLPG 182
Cdd:PRK05691 2269 DPEY-PLERLHYMIE-DSGIGLLLSDRA---------------LFEALGE-LPAgvARWCLED-------------DAAA 2317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 183 AISMRKAlhkgrrlqyVKPFMSGED-IAFLQYTGGTTGVAKGAILTHrNMVANVLQAkgaygpVLRE-GRELVVTALPLY 260
Cdd:PRK05691 2318 LAAYSDA---------PLPFLSLPQhQAYLIYTSGSTGKPKGVVVSH-GEIAMHCQA------VIERfGMRADDCELHFY 2381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 261 HV-FALTVNCLLFIEMGGSNLLIT-----NPRDIPGFVKELQkhpfTAITGVNTLFNALVNNEDFHELNFANMKLSVGGG 334
Cdd:PRK05691 2382 SInFDAASERLLVPLLCGARVVLRaqgqwGAEEICQLIREQQ----VSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGG 2457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 335 MAVqraVAEKWKKITGV----HLLEGYGLTE--CSPLVTGNPYDLADYSGA--IGLPVPSTEVRIVDDEGNVLNYGQTGE 406
Cdd:PRK05691 2458 EAL---TGEHLQRIRQAfapqLFFNAYGPTEtvVMPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGE 2534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 407 LQVRGPQVMQGYWQRPEATKE------VINEEGWL-STGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHG 479
Cdd:PRK05691 2535 LYVGGAGLAQGYHDRPGLTAErfvadpFAADGGRLyRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHP 2614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 480 KVLE--VAAIGQPhevSGEVVKIYVVKRDPSLTKDE-------LITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVL 550
Cdd:PRK05691 2615 AVREavVLALDTP---SGKQLAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
570
....*....|.
gi 521099036 551 REENDAQLAEQ 561
Cdd:PRK05691 2692 PAPDPELNRQA 2702
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-552 |
1.79e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 25 LVEMFEQSVHKYADQPAFINMGSVMTFRKLEERSRAFAAYLQNelklkKG----DRVALMMPNLLQYPVALFGILRAGMI 100
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRD-----KGvgpdVCVAIAAERSPQLLVGLLAILKAGGA 1207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 101 AVNVNPLYTPRELEHQLNDADARAIVivsnfantleqivanTQvkhvvlTSLGQMLPRAKGTLVDfvvkyvkgMVPKYDL 180
Cdd:PRK05691 1208 YVPLDPDYPAERLAYMLADSGVELLL---------------TQ------SHLLERLPQAEGVSAI--------ALDSLHL 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 181 PGAISMRKALHkgrrlqyvkpfMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGpvLREGRELVVTAlPLy 260
Cdd:PRK05691 1259 DSWPSQAPGLH-----------LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDSDVLMQKA-PI- 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 261 hVFALTV-NCLLFIeMGGSNLLITNP---RDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNfaNMKLSVGGGMA 336
Cdd:PRK05691 1324 -SFDVSVwECFWPL-ITGCRLVLAGPgehRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACT--SLRRLFSGGEA 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQRAVAEK-WKKITGVHLLEGYGLTECSPLVTGNPYDLAD-YSGAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVRGPQV 414
Cdd:PRK05691 1400 LPAELRNRvLQRLPQVQLHNRYGPTETAINVTHWQCQAEDgERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGL 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 415 MQGYWQRPEATKE-----VINEEG--WLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEdvvalhGKVLEVAAI 487
Cdd:PRK05691 1480 ARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQ------ARLLAQPGV 1553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521099036 488 GQP----HE--VSGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE 552
Cdd:PRK05691 1554 AQAavlvREgaAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
195-462 |
2.42e-17 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 85.66 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 195 RLQYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKgaygPVLREGRELVVTA------LPLYHVFALTVN 268
Cdd:PLN02861 209 SLDCELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTD----HLLKVTDRVATEEdsyfsyLPLAHVYDQVIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 269 cLLFIEMGGSnllITNPR-DIPGFVKELQKHPFTAITGVNTLFNALVNNedfhelnfANMKLSVGGGMA----------- 336
Cdd:PLN02861 285 -TYCISKGAS---IGFWQgDIRYLMEDVQALKPTIFCGVPRVYDRIYTG--------IMQKISSGGMLRkklfdfaynyk 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 ----------------VQRAVAEKWKKITG--VHLL------------------------EGYGLTE-CSPLVT--GNPY 371
Cdd:PLN02861 353 lgnlrkglkqeeasprLDRLVFDKIKEGLGgrVRLLlsgaaplprhveeflrvtscsvlsQGYGLTEsCGGCFTsiANVF 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 372 DLAdysGAIGLPVPSTEVRI--VDDEG-NVLNYGQTGELQVRGPQVMQGYWQRPEATKEVINEeGWLSTGDIVRFDENGM 448
Cdd:PLN02861 433 SMV---GTVGVPMTTIEARLesVPEMGyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGA 508
|
330
....*....|....
gi 521099036 449 IYIVDRKKDMILVS 462
Cdd:PLN02861 509 MKIIDRKKNIFKLS 522
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
200-462 |
1.02e-16 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 83.71 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 200 KPFmsgeDIAFLQYTGGTTGVAKGAILTHRNmVANVLQAKGAYGPVLREG---RELVVTALPLYHVFAlTVNCLLFIEMG 276
Cdd:PLN02430 218 KPL----DICTIMYTSGTSGDPKGVVLTHEA-VATFVRGVDLFMEQFEDKmthDDVYLSFLPLAHILD-RMIEEYFFRKG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 277 GS--------------------NLLITNPRDIPGFVKELQKhpftAITGVNTL----FNALVNNE--------------- 317
Cdd:PLN02430 292 ASvgyyhgdlnalrddlmelkpTLLAGVPRVFERIHEGIQK----ALQELNPRrrliFNALYKYKlawmnrgyshkkasp 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 318 --DFheLNFANMK--------LSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTE-CSPLVTGNPYDLAdYSGAIGLPVPS 386
Cdd:PLN02430 368 maDF--LAFRKVKaklggrlrLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTEtLGPTTLGFPDEMC-MLGTVGAPAVY 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 387 TEVRI--VDDEG-NVLNYGQTGELQVRGPQVMQGYWQRPEATKEVInEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS 462
Cdd:PLN02430 445 NELRLeeVPEMGyDPLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
206-548 |
1.47e-16 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 82.51 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 206 EDIAFLQYTGGTTGVAKGAILTHRNMVANV--LQAKGAYGPvlreGRELVVTALPLYHVFALTVncLLFIEMGGSNLLIT 283
Cdd:PRK05851 152 GGPAVLQGTAGSTGTPRTAILSPGAVLSNLrgLNARVGLDA----ATDVGCSWLPLYHDMGLAF--LLTAALAGAPLWLA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 284 nprdiPgfVKELQKHPF-----------TAITGVNTLFNALVNNED-FHELNFANMKLSVGGGMAVQRAVAEKWKKIT-- 349
Cdd:PRK05851 226 -----P--TTAFSASPFrwlswlsdsraTLTAAPNFAYNLIGKYARrVSDVDLGALRVALNGGEPVDCDGFERFATAMap 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 350 -----GVhLLEGYGLTECSPLVT------GNPYD---LADYSGA-----IGLPVPSTEVRIVDDEGNVLNYGQT-GELQV 409
Cdd:PRK05851 299 fgfdaGA-AAPSYGLAESTCAVTvpvpgiGLRVDevtTDDGSGArrhavLGNPIPGMEVRISPGDGAAGVAGREiGEIEI 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 410 RGPQVMQGYW-QRPeatkevINEEGWLSTGDIVRFDENGMIyIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLE--VAA 486
Cdd:PRK05851 378 RGASMMSGYLgQAP------IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREgaVVA 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521099036 487 IG------QPhevsGEVVKIYVVKRDPSLTKDELI----THCrkhltGYkVPKLIEFRE--ELPKTNVGKiLRR 548
Cdd:PRK05851 451 VGtgegsaRP----GLVIAAEFRGPDEAGARSEVVqrvaSEC-----GV-VPSDVVFVApgSLPRTSSGK-LRR 513
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
210-560 |
1.32e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 80.17 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 210 FLQYTGGTTGVAKGAIlthRNMVANVLQAKGAYGPVLREGRELVVTALP-----LYHVF---ALTVNCLLFIEMGGsnll 281
Cdd:PTZ00237 258 YILYTSGTTGNSKAVV---RSNGPHLVGLKYYWRSIIEKDIPTVVFSHSsigwvSFHGFlygSLSLGNTFVMFEGG---- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 282 ITNPRDIP-GFVKELQKHPFTAITGVNTLFNALVNN----EDFH-ELNFANMKLSVGGGMAVQRAVAEKWKKITGVHLLE 355
Cdd:PTZ00237 331 IIKNKHIEdDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeaTIIRsKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 356 GYGLTE--CSPLVT----GNPYDladysgAIGLPVPSTEVRIVDDEGNVLNYGQTGELQVR---GPQVMQGYWQRPEATK 426
Cdd:PTZ00237 411 GYGQTEigITYLYCyghiNIPYN------ATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 427 EVINE-EGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEVSGEV-VKIYVVK 504
Cdd:PTZ00237 485 QLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVpIGLLVLK 564
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 505 RDPSLT-------KDELITHCRKHLTGYKVPKLIEFREELPKTNVGKILRRVLRE---ENDAQLAE 560
Cdd:PTZ00237 565 QDQSNQsidlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKflnDSNYQLPD 630
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
23-462 |
8.12e-15 |
|
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: 77.50 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 23 LSLVEMFEQSVHKYADQPAF--------------------INMGSVMTFRKLEERSRAFAAYLQNELKLKKGDRVALMMP 82
Cdd:cd17632 22 LRLAQIIATVMTGYADRPALgqratelvtdpatgrttlrlLPRFETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 83 NLLQYPVALFGILRAGmiAVNVnPLYT---PRELEHQLNDADARAI-VIVSNFANTLEQIVANTQVKHVV-------LTS 151
Cdd:cd17632 102 TSPDYATVDLALTRLG--AVSV-PLQAgasAAQLAPILAETEPRLLaVSAEHLDLAVEAVLEGGTPPRLVvfdhrpeVDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 152 LGQMLPRAKGTLVDFVVKYVkgmvpkydLPGAISMRkalhkGRRLQYVKPFMSGED---IAFLQYTGGTTGVAKGAILTH 228
Cdd:cd17632 179 HRAALESARERLAAVGIPVT--------TLTLIAVR-----GRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 229 RNMVANVLQAKGAYGPvlREGRELVVTALPLYHvfaltvncllfieMGGSNLLITNprdipgfvkeLQKHP---FTAITG 305
Cdd:cd17632 246 RLVATFWLKVSSIQDI--RPPASITLNFMPMSH-------------IAGRISLYGT----------LARGGtayFAAASD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 306 VNTLFN--ALVNNEDF----------HELNFANM-KLSVGGGMAV---QRAVAEKWKKITG------------------- 350
Cdd:cd17632 301 MSTLFDdlALVRPTELflvprvcdmlFQRYQAELdRRSVAGADAEtlaERVKAELRERVLGgrllaavcgsaplsaemka 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 351 -------VHLLEGYGLTECSPLVTgnpydladySGAIGLPvPSTEVRIVDdegnV--LNYGQT------GELQVRGPQVM 415
Cdd:cd17632 381 fmeslldLDLHDGYGSTEAGAVIL---------DGVIVRP-PVLDYKLVD----VpeLGYFRTdrphprGELLVKTDTLF 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 521099036 416 QGYWQRPEATKEVINEEGWLSTGDIV-RFDENGMIYiVDRKKDMILVS 462
Cdd:cd17632 447 PGYYKRPEVTAEVFDEDGFYRTGDVMaELGPDRLVY-VDRRNNVLKLS 493
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
208-462 |
7.02e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 74.75 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 208 IAFLQYTGGTTGVAKGAILTHRNMVANVLQA-----KGAYGPvlregrELVVTALPLYHVFALTVNCLLFieMGGSNLLI 282
Cdd:PTZ00342 306 ITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLckhsiFKKYNP------KTHLSYLPISHIYERVIAYLSF--MLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNpRDIPGFVKELQKHPFTAITGVNTLFNALVNN-----------------------EDFHELNFA-------------- 325
Cdd:PTZ00342 378 WS-KDINYFSKDIYNSKGNILAGVPKVFNRIYTNimteinnlpplkrflvkkilslrKSNNNGGFSkflegithisskik 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 326 -----NMKLSVGGGMAVQRAVAEKWKKITGVHLLEGYGLTECS-PLVTGNPYDlaDYSGAIGLPV-PSTEVRIVDDEgnv 398
Cdd:PTZ00342 457 dkvnpNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFVQHADD--NNTESIGGPIsPNTKYKVRTWE--- 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521099036 399 lNYGQT-----GELQVRGPQVMQGYWQRPEATKEVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVS 462
Cdd:PTZ00342 532 -TYKATdtlpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
356-558 |
4.37e-12 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 68.36 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 356 GYGLTECSPLVTGNPydlADYSGAIGLPVPSTEVRIVDDegnvlnygqtgELQVRGPQVMQGYWQ----RPeatkeVINE 431
Cdd:PRK09029 270 GYGLTEMASTVCAKR---ADGLAGVGSPLPGREVKLVDG-----------EIWLRGASLALGYWRqgqlVP-----LVND 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 432 EGWLSTGDIVRFDeNGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEV-------AAIGQ-PhevsgevvkIYVV 503
Cdd:PRK09029 331 EGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVfvvpvadAEFGQrP---------VAVV 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521099036 504 KRDPSLTKDELITHCRKHLTGYKVPklIEFrEELPKT--NVG-KILRRVLREENDAQL 558
Cdd:PRK09029 401 ESDSEAAVVNLAEWLQDKLARFQQP--VAY-YLLPPElkNGGiKISRQALKEWVAQQL 455
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
205-545 |
5.44e-12 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 67.88 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 GEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGaygpVLREGRELVVTALPLYHVFALTVNCLLFIEMGGSnlLITN 284
Cdd:cd17654 117 DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRS----LFNITSEDILFLTSPLTFDPSVVEIFLSLSSGAT--LLIV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 285 PRDIPGFVKELQKHPFTA--ITGVN---TLFNALvNNEDFHELNFANMK----LSVGGGMAVQRAVAEKW-KKITGVHLL 354
Cdd:cd17654 191 PTSVKVLPSKLADILFKRhrITVLQatpTLFRRF-GSQSIKSTVLSATSslrvLALGGEPFPSLVILSSWrGKGNRTRIF 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 355 EGYGLTECSPLVTGNPYDLADYSGAIGLPVPSTEVRIVDDEGNvlnyGQTGELQVRGPQ---VMQGYWQRPEATkevine 431
Cdd:cd17654 270 NIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGS----EGTGQVFLGGLNrvcILDDEVTVPKGT------ 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 432 egWLSTGDIVRFdENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEvsgevvKIYVVKRDPSLTK 511
Cdd:cd17654 340 --MRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ------RLIAFIVGESSSS 410
|
330 340 350
....*....|....*....|....*....|....*..
gi 521099036 512 DeliTHCRKHLTG---YKVPKLIEFREELPKTNVGKI 545
Cdd:cd17654 411 R---IHKELQLTLlssHAIPDTFVQIDKLPLTSHGKV 444
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
205-540 |
4.70e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 52.80 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 205 GEDIAFLQYTG-GTTGVAKgAILTHRNMVANVLQAKGAygpvlREGRELVVTAL-PLYHVFALTVNcLLFIEMGGSNLLI 282
Cdd:PRK07868 605 ARDLAFIAFSTaGGELVAK-QITNYRWALSAFGTASAA-----ALDRRDTVYCLtPLHHESGLLVS-LGGAVVGGSRIAL 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 283 TNPRDIPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKLSVGGGMAvqravAEKWKKITGV----HLLEGYG 358
Cdd:PRK07868 678 SRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMP-----TGLWERVVEAfapaHVVEFFA 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 359 LTECSPLvtgnpydLADYSGA----IGLPVPST-EV----------RIVDDEGNVLNYGQTGELQV-----RGP-----Q 413
Cdd:PRK07868 753 TTDGQAV-------LANVSGAkigsKGRPLPGAgRVelaaydpehdLILEDDRGFVRRAEVNEVGVllaraRGPidptaS 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 414 VMQGYWQRPEAtkevineegWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEVAAIGQPHEV 493
Cdd:PRK07868 826 VKRGVFAPADT---------WISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGG 896
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 521099036 494 SGEVVKIYVVKRDPSLTKDELITHCRKHLTGYKvPKLIEFREELPKT 540
Cdd:PRK07868 897 RQLAVAAVTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLS 942
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
47-553 |
4.79e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 46.23 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 47 SVMTFRKLEERSRAfAAYLQNELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLYTPRELEHQLNDADARAI- 125
Cdd:PLN03052 207 NRMTLSELRSQVSR-VANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIf 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 126 ---VIVSNfANTL---EQIVANTQVKHVVLTslgqmlprAKGTLVDFVVKyvkgmvpkydlPGAISMRKALHKGRRL--- 196
Cdd:PLN03052 286 tqdVIVRG-GKSIplySRVVEAKAPKAIVLP--------ADGKSVRVKLR-----------EGDMSWDDFLARANGLrrp 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 197 -QYVKPFMSGEDIAFLQYTGGTTGVAKGAILTHrnmVANVLQAKGAYGPV-LREGRelvVTALPL--------YHVFALT 266
Cdd:PLN03052 346 dEYKAVEQPVEAFTNILFSSGTTGEPKAIPWTQ---LTPLRAAADAWAHLdIRKGD---IVCWPTnlgwmmgpWLVYASL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 267 VNcllfiemgGSNLLITN--PRDiPGFVKELQKHPFTAITGVNTLFNALVNNEDFHELNFANMKL--SVGGGMAVQ---- 338
Cdd:PLN03052 420 LN--------GATLALYNgsPLG-RGFAKFVQDAKVTMLGTVPSIVKTWKNTNCMAGLDWSSIRCfgSTGEASSVDdylw 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 339 ---RAvaeKWKKItgvhlLEGYGLTEC-SPLVTGN---PYDLADYSGaiglPVPSTEVRIVDDEGNVLNYGQ--TGELQV 409
Cdd:PLN03052 491 lmsRA---GYKPI-----IEYCGGTELgGGFVTGSllqPQAFAAFST----PAMGCKLFILDDSGNPYPDDApcTGELAL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 410 rGPQVMQG------------YWQ-RPeatkeVINEEGWLSTGDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVV- 475
Cdd:PLN03052 559 -FPLMFGAsstllnadhykvYFKgMP-----VFNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCn 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 476 ALHGKVLEVAAIGQPHEVSG--EVVKIYVVKRDPSLTKD--EL----ITHCRKHLTG-YKVPKLIEFrEELPKTNVGKIL 546
Cdd:PLN03052 633 AADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDlnELkkifNSAIQKKLNPlFKVSAVVIV-PSFPRTASNKVM 711
|
....*..
gi 521099036 547 RRVLREE 553
Cdd:PLN03052 712 RRVLRQQ 718
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
34-546 |
2.27e-04 |
|
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: 44.18 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 34 HKYADQPAFINMGS-----VMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNLLQYPVALFGILRAGMIAVNVNPLY 108
Cdd:cd05943 79 HADADDPAAIYAAEdgertEVTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 109 TPRELEHQLNDADARAIVIVSNFANTLEQIVANTQVKHVVltslgQMLPRAKGT-LVDFVVKYVKGMVPKYDLPGAISMR 187
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELV-----KGLPSLLAVvVVPYTVAAGQPDLSKIAKALTLEDF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 188 KALHKGRRLQYVK-PFmsgEDIAFLQYTGGTTGVAKGAILTHRNMVANVLQAKGAYGPvLREGREL---VVTALPLYH-- 261
Cdd:cd05943 233 LATGAAGELEFEPlPF---DHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCD-LRPGDRLfyyTTCGWMMWNwl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 262 VFALTVNCLLFIEMGgsNLLITNPRDIPGFVKELQkhpfTAITGVNTLFNALVNNEDF-----HELNFANMKLSVGGGMA 336
Cdd:cd05943 309 VSGLAVGATIVLYDG--SPFYPDTNALWDLADEEG----ITVFGTSAKYLDALEKAGLkpaetHDLSSLRTILSTGSPLK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 337 VQ--RAVAEKWKKitGVHLLEGYGLTE-CSPLVTGNPyDLADYSGAIGLPVPSTEVRIVDDEGNVLnYGQTGELQVRGPQ 413
Cdd:cd05943 383 PEsfDYVYDHIKP--DVLLASISGGTDiISCFVGGNP-LLPVYRGEIQCRGLGMAVEAFDEEGKPV-WGEKGELVCTKPF 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 414 VMQ--GYWQRPEATKEvinEEGWLST-------GDIVRFDENGMIYIVDRKKDMILVSGFNVYPNEIEDVVALHGKVLEV 484
Cdd:cd05943 459 PSMpvGFWNDPDGSRY---RAAYFAKypgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDS 535
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 485 AAIGQPHEVSGEVVKIYVVKRDPSLTKDELITH----CRKHLTGYKVPKLIEFREELPKTNVGKIL 546
Cdd:cd05943 536 LVVGQEWKDGDERVILFVKLREGVELDDELRKRirstIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
328-475 |
2.30e-04 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 43.60 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 328 KLSVGGGM---AVQRAVAEKWkkitGVHLLEGYGLTECSPLVTGNPYDLAdysgaiGLPVPSTE--VRIVDDE-GNVLNY 401
Cdd:COG1541 207 KGIFGGEPwseEMRKEIEERW----GIKAYDIYGLTEVGPGVAYECEAQD------GLHIWEDHflVEIIDPEtGEPVPE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 402 GQTGELqvrgpqVM-----QGYwqrPeatkeVINeegwLSTGDIVRFDENG---------MIYIVDRKKDMILVSGFNVY 467
Cdd:COG1541 277 GEEGEL------VVttltkEAM---P-----LIR----YRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVF 338
|
....*...
gi 521099036 468 PNEIEDVV 475
Cdd:COG1541 339 PSQIEEVL 346
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
34-84 |
1.47e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.32 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 521099036 34 HKYADQPAFINMG-----SVMTFRKLEERSRAFAAYLQnELKLKKGDRVALMMPNL 84
Cdd:PRK03584 95 HRRDDRPAIIFRGedgprRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNI 149
|
|
| Pchlide_reductase_N |
cd01979 |
Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide) ... |
54-138 |
6.47e-03 |
|
Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.
Pssm-ID: 238937 [Multi-domain] Cd Length: 396 Bit Score: 39.27 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521099036 54 LEERSRAFAAYLQNELKLKKGDRVALMMPNLLQYPVALFgILRAGMIAVNVNPLYTPREL---EHQLNDADARaIVIVSN 130
Cdd:cd01979 256 LAEREARAWRALEPYLDLLRGKSIFFMGDNLLEIPLARF-LTRCGMIVVEVGTPYLDKRFqaaELELLPPMVR-IVEKPD 333
|
....*...
gi 521099036 131 FANTLEQI 138
Cdd:cd01979 334 NYRQLDRI 341
|
|
| |
