|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-562 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 1206.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 1 MQPEFWNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAV 80
Cdd:PRK12492 1 MQPDFWNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 81 QMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPAL 160
Cdd:PRK12492 81 QMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 161 KGWLVNSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVH 240
Cdd:PRK12492 161 KGWLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 241 AQLSQLGKDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVA 320
Cdd:PRK12492 241 ACLSQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 321 LMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVI 400
Cdd:PRK12492 321 LMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 401 DEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:PRK12492 401 DDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 481 DVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
..
gi 15598496 561 IA 562
Cdd:PRK12492 561 IA 562
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1-560 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 897.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 1 MQPEFWNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAV 80
Cdd:PRK05677 1 MIENFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 81 QMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPAL 160
Cdd:PRK05677 81 QLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 161 KGWLVNSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVH 240
Cdd:PRK05677 161 KRLLINAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 241 AQL-SQLGkdglplmkEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFV 319
Cdd:PRK05677 241 ALMgSNLN--------EGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 320 ALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYgEQARLGTVGIPVVGTALKV 399
Cdd:PRK05677 313 ALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPS-QAIQVGTIGIPVPSTLCKV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 400 IDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEI 479
Cdd:PRK05677 392 IDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNEL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 480 EDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK05677 472 EDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKpGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
..
gi 15598496 559 RE 560
Cdd:PRK05677 552 RD 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
6-560 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 806.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNV 85
Cdd:PRK08974 5 WLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPALKGWLV 165
Cdd:PRK08974 85 LQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAKGTLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 NSVVKSVKKMVPDYRLPQALPFRQALKQGQGhaLQPVR--VGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQL 243
Cdd:PRK08974 165 NFVVKYIKRLVPKYHLPDAISFRSALHKGRR--MQYVKpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 244 SqlgkdglPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALME 323
Cdd:PRK08974 243 G-------PLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 324 HPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQ 403
Cdd:PRK08974 316 NEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 404 GNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVV 483
Cdd:PRK08974 396 GNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 484 MAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK08974 475 MLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
6-559 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 778.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNV 85
Cdd:PRK07059 5 WLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQ-SRGLAKGARVAIMMPNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLpALKGWLV 165
Cdd:PRK07059 84 LQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLL-GFKGHIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 NSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQL-S 244
Cdd:PRK07059 163 NFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLqP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 245 QLGKDGLPlmkeAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEH 324
Cdd:PRK07059 243 AFEKKPRP----DQLNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 325 PGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQG 404
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVM 484
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 485 AHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
6-562 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 714.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNV 85
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPALKGWLV 165
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 NSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQ 245
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKdglplMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHP 325
Cdd:PRK08751 247 TGK-----LEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 326 GFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGN 405
Cdd:PRK08751 322 GFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 406 ELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMA 485
Cdd:PRK08751 402 VLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAM 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 486 HPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK08751 482 MPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAA 558
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-559 |
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: 667.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 26 VVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNT 105
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQ-NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 106 NPLYTAREMRHQFKDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpQAL 185
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALI-------------------------------------------------------VAV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 186 PFRQALKQGQGHALQPVRVGlEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlgkdglPLMKEAQEVMIAPL 265
Cdd:cd05936 105 SFTDLLAAGAPLGERVALTP-EDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWL--------EDLLEGDDVVLAAL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 266 PLYHIYAFTANCMCMMVSGNHNVLITNPRDIpGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTAL 345
Cdd:cd05936 176 PLFHVFGLTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKG 425
Cdd:cd05936 255 PVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 426 YWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEA 505
Cdd:cd05936 335 YWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEA 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 506 VKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05936 414 VKAFVVLKEgASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
26-562 |
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: 543.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 26 VVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNT 105
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 106 NPLYTAREMRHQFKDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqal 185
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALV---------------------------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 186 pfrqalkqgqghalqpvrvgledVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlgkdGLplmkEAQEVMIAPL 265
Cdd:COG0318 102 -----------------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAL------GL----TPGDVVLVAL 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 266 PLYHIYAFTANCMCMMVSGNHNVLITNpRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTAL 345
Cdd:COG0318 149 PLFHVFGLTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPL 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQ-ARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMK 424
Cdd:COG0318 228 PPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMK 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 GYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:COG0318 308 GYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 505 AVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:COG0318 387 RVVAFVVLRPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
3-560 |
1.99e-164 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 479.88 E-value: 1.99e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 3 PEFWNDKR-----PAGVPDSLDFAAyRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDR 77
Cdd:PRK05605 7 MSAFADKPwlqsyAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGL-RALGVRPGDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 78 IAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLL 157
Cdd:PRK05605 85 VAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 158 PALKGWLVNSVVKSVKKMvpdyR------LPQALPFRQALKQ---GQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLT 228
Cdd:PRK05605 165 PLLQRLALRLPIPALRKA----RaaltgpAPGTVPWETLVDAaigGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 229 HGNLVANMLQvhaqlsqlGKDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPrDIPGFVKELKKWRF 308
Cdd:PRK05605 241 HRNLFANAAQ--------GKAWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 309 SALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTV 388
Cdd:PRK05605 312 TWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 389 GIPVVGTALKVIDEQ--GNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDL 466
Cdd:PRK05605 392 GVPFPDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 467 ILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVV-ARDPSLSVEELKAYCKENLTGYKIPRQIVLKDAL 545
Cdd:PRK05605 471 IITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVlEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDEL 550
|
570
....*....|....*
gi 15598496 546 PMTPVGKILRRELRE 560
Cdd:PRK05605 551 PRDQLGKVRRREVRE 565
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
21-560 |
5.45e-140 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 415.07 E-value: 5.45e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 21 AAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGL 100
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 101 VVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEvlpdtrieyliearMGDLLPALKgwlvnsVVKSVKKMVPDYR 180
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYS--------------ATTRLPALE------HVVICETEEDDPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 181 LPQALPFRQALKQGQGhALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhAQLSQLgkdglplmkEAQEV 260
Cdd:PRK07656 141 TEKMKTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADW-AEYLGL---------TEGDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 MIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNS 340
Cdd:PRK07656 210 YLAANPFFHVFGYKAGVNAPLMRGA-TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 341 GGTALVSATAERWKGVTGC-TVVEGYGLTECSPVVTTNPYGEQARL--GTVGIPVVGTALKVIDEQGNELPVGERGELCV 417
Cdd:PRK07656 289 GAASMPVALLERFESELGVdIVLTGYGLSEASGVTTFNRLDDDRKTvaGTIGTAIAGVENKIVNELGEEVPVGEVGELLV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 418 KGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI 497
Cdd:PRK07656 369 RGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 498 PDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07656 449 PDERLGEVGKAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
19-560 |
2.23e-134 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 401.10 E-value: 2.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 19 DFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRA 98
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRAL-GVKKGDRVAVFDWNSHEYLEAYFAVPKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 99 GLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDtrieyliearmgdlLPALKGWLVNSVVKSVKKmvpd 178
Cdd:PRK06187 80 GAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQ--------------LPTVRTVIVEGDGPAAPL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 179 yrLPQALPFRQALKQGQGHALQPvRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsQLGKDglplmkeaq 258
Cdd:PRK06187 142 --APEVGEYEELLAAASDTFDFP-DIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWL-KLSRD--------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 259 EVMIAPLPLYHIYAFTANCMCMMvSGNHNVLItnPRDIPGFVKEL-KKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKL 337
Cdd:PRK06187 209 DVYLVIVPMFHVHAWGLPYLALM-AGAKQVIP--RRFDPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 338 TNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQ-----ARLGTVGIPVVGTALKVIDEQGNELPV--G 410
Cdd:PRK06187 286 VIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEDQlpgqwTKRRSAGRPLPGVEARIVDDDGDELPPdgG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 411 ERGELCVKGPQVMKGYWQRPEATEEILDAeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVA 490
Cdd:PRK06187 366 EVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVA 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 491 SCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06187 445 EVAVIGVPDEKWGERPVAVVVLKPgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-470 |
2.67e-133 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 394.37 E-value: 2.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 30 FERSCKKFADRPAFSN-LGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPL 108
Cdd:pfam00501 1 LERQAARTPDKTALEVgEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 109 YTAREMRHQFKDAGVRALVYLNVFgkLVEEVLPDT-RIEYLIEARMGDLLPALKGWLVNSVVKSVKKmvpdyrlpqalpf 187
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALgKLEVVKLVLVLDRDPVLKEEPLPEEAKPADV------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rqalkqgqgHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHaqlsQLGKDGLPLMkeAQEVMIAPLPL 267
Cdd:pfam00501 145 ---------PPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIK----RVRPRGFGLG--PDDRVLSTLPL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 268 YHIYAFTANCMCMMVSGNHNVLI--TNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTAL 345
Cdd:pfam00501 210 FHDFGLSLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQ--ARLGTVGIPVVGTALKVIDEQ-GNELPVGERGELCVKGPQV 422
Cdd:pfam00501 290 PPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGV 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15598496 423 MKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS 470
Cdd:pfam00501 370 MKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
14-560 |
5.06e-128 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 385.47 E-value: 5.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAAyRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVF 93
Cdd:PRK08314 1 LPKSLTLPE-TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 94 GALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVylnVFGKLVEEVLP---DTRIEYLIEARMGDLLP-----ALKGWLV 165
Cdd:PRK08314 80 AILRANAVVVPVNPMNREEELAHYVTDSGARVAI---VGSELAPKVAPavgNLRLRHVIVAQYSDYLPaepeiAVPAWLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 nsvvksVKKMVPDYRLPQALPFRQALkqGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLqvhaqLSQ 245
Cdd:PRK08314 157 ------AEPPLQALAPGGVVAWKEAL--AAGLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAV-----GSV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKDGLPlmkeaQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITN-PRDIPGfvKELKKWRFSALLGLNTLFVALMEH 324
Cdd:PRK08314 224 LWSNSTP-----ESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRwDREAAA--RLIERYRVTHWTNIPTMVVDFLAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 325 PGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYgEQARLGTVGIPVVGTALKVID-EQ 403
Cdd:PRK08314 297 PGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPP-DRPKLQCLGIPTFGVDARVIDpET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 404 GNELPVGERGELCVKGPQVMKGYWQRPEATEEI---LDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 481 DVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS---LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRE 557
Cdd:PRK08314 456 NLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQ 535
|
...
gi 15598496 558 LRE 560
Cdd:PRK08314 536 LQE 538
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
47-554 |
2.48e-127 |
|
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: 381.56 E-value: 2.48e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRAL 126
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 -VYLNVFGKL---VEEVLPDTRIeYLIEARMGDLLPALKGWlvnsvvkSVKKMVPDYRLPqalPFRQALKqgqghalqpv 202
Cdd:cd05911 87 fTDPDGLEKVkeaAKELGPKDKI-IVLDDKPDGVLSIEDLL-------SPTLGEEDEDLP---PPLKDGK---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 203 rvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlgkdglPLMKEAQEVMIAPLPLYHIYAFTAnCMCMMV 282
Cdd:cd05911 146 ----DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFL--------YGNDGSNDVILGFLPLYHIYGLFT-TLASLL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGnHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGV-TGCTV 361
Cdd:cd05911 213 NG-ATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 362 VEGYGLTECSPVVTTNPYGEqARLGTVGIPVVGTALKVIDEQGNE-LPVGERGELCVKGPQVMKGYWQRPEATEEILDAE 440
Cdd:cd05911 292 KQGYGMTETGGILTVNPDGD-DKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 441 GWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVV-ARDPSLSV 519
Cdd:cd05911 371 GWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrKPGEKLTE 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 15598496 520 EELKAYCKENLTGYKIPR-QIVLKDALPMTPVGKIL 554
Cdd:cd05911 451 KEVKDYVAKKVASYKQLRgGVVFVDEIPKSASGKIL 486
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
30-555 |
6.34e-126 |
|
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: 376.18 E-value: 6.34e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 30 FERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLY 109
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 110 TAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrq 189
Cdd:cd17631 80 TPPEVAYILADSGAKVL--------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 190 alkqgqghalqpvrvgLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqVHAQLSQLGKDGlplmkeaQEVMIAPLPLYH 269
Cdd:cd17631 97 ----------------FDDLALLMYTSGTTGRPKGAMLTHRNLLWN---AVNALAALDLGP-------DDVLLVVAPLFH 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 270 IYAFTANCMCMMVSGNHNVLITNPRdiPG-FVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSA 348
Cdd:cd17631 151 IGGLGVFTLPTLLRGGTVVILRKFD--PEtVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPER 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 349 TAERWKgVTGCTVVEGYGLTECSPVVTTNPYGEQ-ARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYW 427
Cdd:cd17631 229 LLRALQ-ARGVKFVQGYGMTETSPGVTFLSPEDHrRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYW 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 428 QRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVK 507
Cdd:cd17631 308 NRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVV 386
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598496 508 LFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILR 555
Cdd:cd17631 387 AVVVPRPGAeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
6-560 |
1.69e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 374.75 E-value: 1.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAGVPDSLDFAAyRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNV 85
Cdd:PRK06710 7 WLKSYPEEIPSTISYDI-QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIMLPNC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPALKGWLV 165
Cdd:PRK06710 85 PQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLLY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 NSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLqvhaqlsq 245
Cdd:PRK06710 165 PFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTL-------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnPR-DIPGFVKELKKWRFSALLGLNTLFVALMEH 324
Cdd:PRK06710 237 MGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 325 PGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVID-EQ 403
Cdd:PRK06710 315 PLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlET 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 404 GNELPVGERGELCVKGPQVMKGYWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVV 483
Cdd:PRK06710 395 GEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 484 MAHPKVASCAAVGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06710 474 YEHEKVQEVVTIGVPDPYRGETVKAFVVLKeGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-562 |
4.11e-121 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 368.60 E-value: 4.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 2 QPEFWndkrPAGVPDSldfAAY----RSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDR 77
Cdd:PRK06178 14 QQAAW----PAGIPRE---PEYphgeRPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLR-QRGVGAGDR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 78 IAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLL 157
Cdd:PRK06178 86 VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 158 PALKGWLVNSVVKSVKKMVPDyrlpqALPFRQALkQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANML 237
Cdd:PRK06178 166 PAEPTLPLPDSLRAPRLAAAG-----AIDLLPAL-RACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 238 QVHAQLSQLGKDglplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITnpR-DIPGFVKELKKWRFSALLGLNT 316
Cdd:PRK06178 240 AAYAVAVVGGED---------SVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 LFVALMEHPGFKDVDFSNLKLTN--SGGTALVSATAERWKGVTGCTVVEG-YGLTE---CSPVVT---TNPYGEQARLGT 387
Cdd:PRK06178 309 NAVELMDHPRFAEYDLSSLRQVRvvSFVKKLNPDYRQRWRALTGSVLAEAaWGMTEthtCDTFTAgfqDDDFDLLSQPVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 388 VGIPVVGTALKVID-EQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDL 466
Cdd:PRK06178 389 VGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 467 ILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPrQIVLKDAL 545
Cdd:PRK06178 468 LKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKpGADLTAAALQAWCRENMAVYKVP-EIRIVDAL 546
|
570
....*....|....*..
gi 15598496 546 PMTPVGKILRRELREIA 562
Cdd:PRK06178 547 PMTATGKVRKQDLQALA 563
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
29-558 |
9.88e-121 |
|
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: 365.40 E-value: 9.88e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 29 VFERScKKFADRPAF--SNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTN 106
Cdd:cd05904 11 SFLFA-SAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 107 PLYTAREMRHQFKDAGVRALVYLNvfgKLVEEVLPdtrieyliearmgdllpalkgwLVNSVVksvkkMVPDYRLPqALP 186
Cdd:cd05904 89 PLSTPAEIAKQVKDSGAKLAFTTA---ELAEKLAS----------------------LALPVV-----LLDSAEFD-SLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 187 FRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAqlsqlgkdGLPLMKEAQEVMIAPLP 266
Cdd:cd05904 138 FSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVA--------GEGSNSDSEDVFLCVLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 267 LYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALV 346
Cdd:cd05904 210 MFHIYGLSSFALGLLRLGA-TVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 347 SATAERWKGV-TGCTVVEGYGLTECSPVVTT--NPYGEQARLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKGPQV 422
Cdd:cd05904 289 KELIEAFRAKfPNVDLGQGYGMTESTGVVAMcfAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 423 MKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKS 502
Cdd:cd05904 369 MKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEA 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 503 GEAVKLFVV-ARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05904 449 GEVPMAFVVrKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
208-554 |
3.33e-118 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 352.74 E-value: 3.33e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANmlqvHAQLSQLGKDGlplmkeAQEVMIAPLPLYHIYAFTANCMCMMVSGNhn 287
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAA----AAALAASGGLT------EGDVFLSTLPLFHIGGLFGLLGALLAGGT-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGL 367
Cdd:cd04433 69 VVLLPKFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 368 TECSPVVTTN-PYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEIlDAEGWLKTG 446
Cdd:cd04433 149 TETGGTVATGpPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 447 DIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS-LSVEELKAY 525
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 15598496 526 CKENLTGYKIPRQIVLKDALPMTPVGKIL 554
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
30-562 |
9.56e-104 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 323.30 E-value: 9.56e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 30 FERSCKKFADRPA--FSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:PRK08315 22 LDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALV---------YLNvfgkLVEEVLPDtrieyLIEARMGDL----LPALK-----------GW 163
Cdd:PRK08315 101 AYRLSELEYALNQSGCKALIaadgfkdsdYVA----MLYELAPE-----LATCEPGQLqsarLPELRrviflgdekhpGM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 164 LVNSVVKSVKKMVPDYRLPQalpfRQAlkqgqghALQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhAQL 243
Cdd:PRK08315 172 LNFDELLALGRAVDDAELAA----RQA-------TLDP-----DDPINIQYTSGTTGFPKGATLTHRNILNNGYFI-GEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 244 SQLG-KDGLPLmkeaqevmiaPLPLYHiyaftancmCM-MVSGN-----HNVLITNPrdIPGF--VKELK---KWRFSAL 311
Cdd:PRK08315 235 MKLTeEDRLCI----------PVPLYH---------CFgMVLGNlacvtHGATMVYP--GEGFdpLATLAaveEERCTAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 312 LGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAER------WKGVTGCtvvegYGLTECSPVVT----TNPygE 381
Cdd:PRK08315 294 YGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRvidkmhMSEVTIA-----YGMTETSPVSTqtrtDDP--L 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 382 QARLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIV 460
Cdd:PRK08315 367 EKRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 461 DRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDP-SLSVEELKAYCKENLTGYKIPRQI 539
Cdd:PRK08315 447 GRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGaTLTEEDVRDFCRGKIAHYKIPRYI 526
|
570 580
....*....|....*....|...
gi 15598496 540 VLKDALPMTPVGKILRRELREIA 562
Cdd:PRK08315 527 RFVDEFPMTVTGKIQKFKMREMM 549
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
14-562 |
2.13e-103 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 322.83 E-value: 2.13e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAAyrsvvEVFERSCKKFADRPAF-----SNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQY 88
Cdd:COG0365 4 VGGRLNIAY-----NCLDRHAEGRGDKVALiwegeDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 89 PIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALV----YLNVfGKLVEevlpdtRIEYLIEARmgDLLPALKGWL 164
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLItadgGLRG-GKVID------LKEKVDEAL--EELPSLEHVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 165 VnsvvksVKKMVPDYRLPQALPFRQALKQgQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLS 244
Cdd:COG0365 149 V------VGRTGADVPMEGDLDWDELLAA-ASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 245 QLGKDglplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLItnpRDIPGFVKELKKWRFSALLGLNTLFVA---- 320
Cdd:COG0365 222 DLKPG---------DVFWCTADIGWATGHSYIVYGPLLNGATVVLY---EGRPDFPDPGRLWELIEKYGVTVFFTAptai 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 321 --LMEHPGF--KDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTA 396
Cdd:COG0365 290 raLMKAGDEplKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKPVPGYD 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 397 LKVIDEQGNELPVGERGELCVKGPQ--VMKGYWQRPEATEEIL--DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGF 472
Cdd:COG0365 370 VAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 473 NVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-----DPSLsVEELKAYCKENLTGYKIPRQIVLKDALPM 547
Cdd:COG0365 450 RIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKpgvepSDEL-AKELQAHVREELGPYAYPREIEFVDELPK 528
|
570
....*....|....*
gi 15598496 548 TPVGKILRRELREIA 562
Cdd:COG0365 529 TRSGKIMRRLLRKIA 543
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
28-562 |
4.20e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 319.03 E-value: 4.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPA--FSNLGVTLSYAEL----DRLSAAFAAylqkqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLV 101
Cdd:PRK12583 22 DAFDATVARFPDREAlvVRHQALRYTWRQLadavDRLARGLLA-----LGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 102 VVNTNPLYTAREMRHQFKDAGVRALV---------YLNVFGKLVEEvLPDTRIEYLIEARmgdlLPALKGwlVNSVVKSV 172
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVIcadafktsdYHAMLQELLPG-LAEGQPGALACER----LPELRG--VVSLAPAP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 173 KKMVPDYRLPQALP---FRQALKQGQGhALQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKD 249
Cdd:PRK12583 170 PPGFLAWHELQARGetvSREALAERQA-SLDR-----DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 250 glplmkeaqeVMIAPLPLYHIYAFT-ANCMCMMVsGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFK 328
Cdd:PRK12583 244 ----------RLCVPVPLYHCFGMVlANLGCMTV-GACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 329 DVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVE-GYGLTECSPVV--TTNPYGEQARLGTVGIPVVGTALKVIDEQGN 405
Cdd:PRK12583 313 NFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQiAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 406 ELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMA 485
Cdd:PRK12583 393 TVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFT 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 486 HPKVASCAAVGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK12583 473 HPAVADVQVFGVPDEKYGEEIVAWVRLHpGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
21-560 |
1.37e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 314.18 E-value: 1.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 21 AAYRSVV-EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAG 99
Cdd:PRK08316 7 RARRQTIgDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLACARAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 100 LVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPALKGWLvnsvvksvkkmvpdy 179
Cdd:PRK08316 86 AVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWL--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 180 rlpqalPFRQALKQGQGHALQpVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQlgkdglplmkEAQE 259
Cdd:PRK08316 151 ------DFADWAEAGSVAEPD-VELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDM----------SADD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 260 VMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRdiPGFVKEL-KKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLT 338
Cdd:PRK08316 214 IPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPD--PELILRTiEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 339 NSGGTAL-VSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQA-RLGTVGIPVVGTALKVIDEQGNELPVGERGELC 416
Cdd:PRK08316 292 YYGASIMpVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGPEEHLrRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 417 VKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:PRK08316 372 HRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIG 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 497 IPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK08316 451 LPDPKWIEAVTAVVVPKAgATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
50-558 |
3.04e-100 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 310.18 E-value: 3.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVyl 129
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNK-GVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 nvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghalqpVRVGLEDV 209
Cdd:cd05935 79 ------------------------------------------------------------------------VGSELDDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVANMLQvhaqlSQLGKDGLPlmkeaQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVL 289
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQ-----SAVWTGLTP-----SDVILACLPLFHVTGFVGSLNTAVYVGGTYVL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 290 ITNpRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTE 369
Cdd:cd05935 157 MAR-WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 CSPVVTTNPYGEQaRLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKGPQVMKGYWQRPEATEEI---LDAEGWLKT 445
Cdd:cd05935 236 TMSQTHTNPPLRP-KLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRT 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 446 GDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDP---SLSVEEL 522
Cdd:cd05935 315 GDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDI 394
|
490 500 510
....*....|....*....|....*....|....*.
gi 15598496 523 KAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05935 395 IEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-559 |
2.71e-97 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 299.58 E-value: 2.71e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhaqlsqlgkdGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFI----------GERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCT-VVEGY 365
Cdd:cd05917 72 MVFPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKdVTIAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 366 GLTECSPVVT-TNPYGEQ-ARLGTVGIPVVGTALKVIDEQGNELP-VGERGELCVKGPQVMKGYWQRPEATEEILDAEGW 442
Cdd:cd05917 152 GMTETSPVSTqTRTDDSIeKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 443 LKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEE 521
Cdd:cd05917 232 LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEgAELTEED 311
|
330 340 350
....*....|....*....|....*....|....*...
gi 15598496 522 LKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05917 312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
32-560 |
1.05e-96 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 304.22 E-value: 1.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 32 RSCKKFADRPAFSNLGVTLSYAEL-DRLS---AAFAAYlqkqtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:PRK06188 20 SALKRYPDRPALVLGDTRLTYGQLaDRISryiQAFEAL-----GLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALVylnvfgklVEEVLPDTRIEYLIEArmgdllpalkgwlvnsvVKSVKKMVPDYRLPQALPF 187
Cdd:PRK06188 95 LGSLDDHAYVLEDAGISTLI--------VDPAPFVERALALLAR-----------------VPSLKHVLTLGPVPDGVDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 RQALKQGQGHALQPVRVGLeDVAVLQYTGGTTGVSKGAMLTHGNLVAnMLQVhaqlsQLGKDGLPlmkeAQEVMIAPLPL 267
Cdd:PRK06188 150 LAAAAKFGPAPLVAAALPP-DIAGLAYTGGTTGKPKGVMGTHRSIAT-MAQI-----QLAEWEWP----ADPRFLMCTPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 268 YHiyAFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTA--- 344
Cdd:PRK06188 219 SH--AGGAFFLPTLLRGG-TVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPmsp 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 --LVSATaERWkgvtGCTVVEGYGLTECSPVVTTNPYGE-----QARLGTVGIPVVGTALKVIDEQGNELPVGERGELCV 417
Cdd:PRK06188 296 vrLAEAI-ERF----GPIFAQYYGQTEAPMVITYLRKRDhdpddPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 418 KGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI 497
Cdd:PRK06188 371 RGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 498 PDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06188 450 PDEKWGEAVTAVVVLRpGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-560 |
3.99e-96 |
|
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: 301.54 E-value: 3.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAF--SNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMR 115
Cdd:cd05926 1 PDAPALvvPGSTPALTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 116 HQFKDAGVRALVylnvfgklveevLPDTRIEYLIEARmgdllPALKGWLVNSVVKSVKKmvpdYRLPQA--LPFRQALKQ 193
Cdd:cd05926 80 FYLADLGSKLVL------------TPKGELGPASRAA-----SKLGLAILELALDVGVL----IRAPSAesLSNLLADKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 194 GQGHALQPVRvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsQLGKDglplmkeaqEVMIAPLPLYHIYAF 273
Cdd:cd05926 139 NAKSEGVPLP---DDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTY-KLTPD---------DRTLVVMPLFHVHGL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 274 TANCMCMMVSGNhNVLITNPRDIPGFVKELKKWR---FSALlglNTLFVALMEHPGFKDVD-FSNLKLTNSGGTALVSAT 349
Cdd:cd05926 206 VASLLSTLAAGG-SVVLPPRFSASTFWPDVRDYNatwYTAV---PTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 350 AERWKGVTGCTVVEGYGLTECSPVVTTNPY-GEQARLGTVGIPVvGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQ 428
Cdd:cd05926 282 LEALEATFGAPVLEAYGMTEAAHQMTSNPLpPGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 429 RPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKL 508
Cdd:cd05926 361 NPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15598496 509 FVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05926 441 AVVLReGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
24-562 |
5.15e-96 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 305.34 E-value: 5.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAFSNL--------GVTLSYAELDRlSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGA 95
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSFLldadpldrPETWTYAELLA-DVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 96 LRAGlVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKL-----VEEV---LPDtrIEYLIEARMGDLLPALKGWLVNS 167
Cdd:PRK07529 104 EAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFPGTdiwqkVAEVlaaLPE--LRTVVEVDLARYLPGPKRLAVPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 168 VVKSVKKMVPDYrlpqalpFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAqLSQLG 247
Cdd:PRK07529 181 IRRKAHARILDF-------DAELARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGAL-LLGLG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 248 KDglplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLIT-----NPRDIPGFVKELKKWRFSALLGLNTLFVALM 322
Cdd:PRK07529 253 PG---------DTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrGPGVIANFWKIVERYRINFLSGVPTVYAALL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 323 EHPgFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVI-- 400
Cdd:PRK07529 324 QVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVVil 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 401 DEQGN---ELPVGERGELCVKGPQVMKGYwQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPN 477
Cdd:PRK07529 403 DDAGRylrDCAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 478 EIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFV-VARDPSLSVEELKAYCKENLTG-YKIPRQIVLKDALPMTPVGKILR 555
Cdd:PRK07529 482 AIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFK 561
|
....*..
gi 15598496 556 RELREIA 562
Cdd:PRK07529 562 PALRRDA 568
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
39-560 |
3.12e-95 |
|
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: 297.66 E-value: 3.12e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqgha 198
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGKDglplmkeaqEVMIAPLPLYHIYAFTANCM 278
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANL-AANVRALVDAWRWTED---------DVLLHVLPLHHVHGLVNALL 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNHNVLITNPRDIPGFVKELKKwRFSALLGLNTLFVALMEHPGFKDVD--------FSNLKLTNSGGTALVSATA 350
Cdd:cd05941 151 CPLFAGASVEFLPKFDPKEVAISRLMP-SITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 351 ERWKGVTGCTVVEGYGLTECSpVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNE-LPVGERGELCVKGPQVMKGYWQR 429
Cdd:cd05941 230 EEWEAITGHTLLERYGMTEIG-MALSNPLDGERRPGTVGMPLPGVQARIVDEETGEpLPRGEVGEIQVRGPSVFKEYWNK 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 430 PEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKL 508
Cdd:cd05941 309 PEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVA 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15598496 509 FVVARD--PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05941 389 VVVLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
19-496 |
1.91e-91 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 292.77 E-value: 1.91e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 19 DFAAYRSVVEVFERSCKKFADRPAFSNLG----VTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFG 94
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 95 ALRAGLVVVntnPLY---TAREMRHQFKDAGVRALVylnvfgklVEEvlpDTRIEYLIEARmgDLLPALKG-WLVNsvvk 170
Cdd:COG1022 85 ILAAGAVTV---PIYptsSAEEVAYILNDSGAKVLF--------VED---QEQLDKLLEVR--DELPSLRHiVVLD---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 171 svkkMVPDYRLPQALPFRQALKQGQGHALQ------PVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLs 244
Cdd:COG1022 145 ----PRGLRDDPRLLSLDELLALGREVADPaelearRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERL- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 245 qlgkdglPLmkEAQEVMIAPLPLYHIYAFTANCMCMMvSGNHNVLITNPRDIPGFVKE---------------------- 302
Cdd:COG1022 220 -------PL--GPGDRTLSFLPLAHVFERTVSYYALA-AGATVAFAESPDTLAEDLREvkptfmlavprvwekvyagiqa 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 303 -------LKKWRFSALLGLNTLF---------VALMEHPGFKDVD---FS--------NLKLTNSGGTALVSATAERWKG 355
Cdd:COG1022 290 kaeeaggLKRKLFRWALAVGRRYararlagksPSLLLRLKHALADklvFSklrealggRLRFAVSGGAALGPELARFFRA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 356 VtGCTVVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVVGTALKVideqgnelpvGERGELCVKGPQVMKGYWQRPEATEE 435
Cdd:COG1022 370 L-GIPVLEGYGLTETSPVITVNRPGDN-RIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAE 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598496 436 ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLI-LVSGFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:COG1022 438 AFDADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
47-560 |
7.79e-90 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 285.62 E-value: 7.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQmpnVLQYPIAVF---GALRAGLVVVNTNPLYTAREMRHQFKDAGV 123
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLV-ALGVKPGDRVAVQ---VEKSPEALAlylATLRAGAVFLPLNTAYTLAELDYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 124 RALV----YLNVFGKLVEEVlPDTRIEYLIEARMGDLLPAlkgwlvnsvvksvkkmvpdyrlpqalpfrqALKQGQGHAl 199
Cdd:PRK07514 102 ALVVcdpaNFAWLSKIAAAA-GAPHVETLDADGTGSLLEA------------------------------AAAAPDDFE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 200 qPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglplmkeaqeVMIAPLPLYHIYA-FTANcm 278
Cdd:PRK07514 150 -TVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDD----------VLIHALPIFHTHGlFVAT-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 cmmvsgnHNVLITNPRDI--PGF-VKELKKW--RFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERW 353
Cdd:PRK07514 217 -------NVALLAGASMIflPKFdPDAVLALmpRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 354 KGVTGCTVVEGYGLTEcSPVVTTNPYGEQARLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKGPQVMKGYWQRPEA 432
Cdd:PRK07514 290 QERTGHAILERYGMTE-TNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVA 512
Cdd:PRK07514 369 TAEEFRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598496 513 R-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07514 449 KpGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
28-562 |
8.93e-89 |
|
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: 283.58 E-value: 8.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALVYLNVFGK-----LVEEVLpdtrieyliearmgDLLPALKGWLVnsvvksvkkmvpdyrLP 182
Cdd:COG1021 108 AHRRAEISHFAEQSEAVAYIIPDRHRGfdyraLARELQ--------------AEVPSLRHVLV---------------VG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 183 QALPFR--QALKQGQGHALQPvRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmLQVHAQLSQLGkdglplmkeAQEV 260
Cdd:COG1021 159 DAGEFTslDALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYS-VRASAEICGLD---------ADTV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 MIAPLPLYHIYAFTANCM--CMMVSGnHNVLITNPRDIPGFvkEL-KKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKL 337
Cdd:COG1021 228 YLAALPAAHNFPLSSPGVlgVLYAGG-TVVLAPDPSPDTAF--PLiERERVTVTALVPPLALLWLDAAERSRYDLSSLRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 338 TNSGGTALVSATAERWKGVTGCTVVEGYGLTEcSPVVTTNPY-GEQARLGTVGIPV-VGTALKVIDEQGNELPVGERGEL 415
Cdd:COG1021 305 LQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVNYTRLDdPEEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:COG1021 384 LTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 496 GIPDEKSGEAVKLFVVARDPSLSVEELKAYCKE-NLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:COG1021 464 AMPDEYLGERSCAFVVPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
23-559 |
8.74e-87 |
|
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: 277.71 E-value: 8.74e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 23 YRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVV 102
Cdd:cd05959 3 YNAATLVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 103 VNTNPLYTAREMRHQFKDAGVRALVylnvfgklVEevlpdtrieyliearmGDLLPALKGWLVNSVVKSVKKMVPDYRLP 182
Cdd:cd05959 82 VPVNTLLTPDDYAYYLEDSRARVVV--------VS----------------GELAPVLAAALTKSEHTLVVLIVSGGAGP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 183 QA--LPFRQALKQGQGhALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVAnMLQVHAQlsQLGKdglplMKEAQEV 260
Cdd:cd05959 138 EAgaLLLAELVAAEAE-QLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYW-TAELYAR--NVLG-----IREDDVC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 MIAPlPLYHIYAFTANCMCMMVSGNHNVLITNpRDIPGFV-KELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTN 339
Cdd:cd05959 209 FSAA-KLFFAYGLGNSLTFPLSVGATTVLMPE-RPTPAAVfKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 340 SGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEqARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKG 419
Cdd:cd05959 287 SAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGR-VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 420 PQVMKGYWQRPEATEEILDAEgWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPD 499
Cdd:cd05959 366 PSSATMYWNNRDKTRDTFQGE-WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVED 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 500 EKSGEAVKLFVVAR----DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05959 445 EDGLTKPKAFVVLRpgyeDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
25-560 |
5.84e-85 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 274.32 E-value: 5.84e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 25 SVVEVFERSCKKFADRPAFS-NLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVV 103
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAK-GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 104 NTNPLYTAREMRHQFKDAGVRALVYLNVFGKlveevlpdTRIEYLIEArMGDLLPALKGWLVnsvVKSVKKMVPDYRLPQ 183
Cdd:PRK06087 103 PLLPSWREAELVWVLNKCQAKMFFAPTLFKQ--------TRPVDLILP-LQNQLPQLQQIVG---VDKLAPATSSLSLSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 184 ALPFRQALKQgqghalqPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMlqvHAQLSQLGKDglplmkeAQEVMIA 263
Cdd:PRK06087 171 IIADYEPLTT-------AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASE---RAYCARLNLT-------WQDVFMM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 264 PLPLYHIYAFTANCMCMMVSGNHNVL--ITNPRDIpgfVKELKKWRFSALLGLnTLFV-----ALMEHPgfkdVDFSNLK 336
Cdd:PRK06087 234 PAPLGHATGFLHGVTAPFLIGARSVLldIFTPDAC---LALLEQQRCTCMLGA-TPFIydllnLLEKQP----ADLSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 337 LTNSGGTALVSATAERWKGvTGCTVVEGYGLTECSPVVTTNPYGEQARLG-TVGIPVVGTALKVIDEQGNELPVGERGEL 415
Cdd:PRK06087 306 FFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESSPHAVVNLDDPLSRFMhTDGYAAAGVEIKVVDEARKTLPPGCEGEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:PRK06087 385 ASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 496 GIPDEKSGEAVKLFVVARDP--SLSVEELKAY-CKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06087 465 AMPDERLGERSCAYVVLKAPhhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-559 |
1.11e-84 |
|
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: 269.55 E-value: 1.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKQTDlQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYln 130
Cdd:cd05934 5 TYAELLRESARIAAALAALGI-RPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 vfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghalqpvrvgleDVA 210
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 211 VLQYTGGTTGVSKGAMLTHGNLVanmlqvHAQLSQLGKDGLPlmkeAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLI 290
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLT------FAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVLAALSVGATLVLL 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 291 tnPRDIP-GFVKELKKWRFSALLGLNTLFVALMEHPgfKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTE 369
Cdd:cd05934 155 --PRFSAsRFWSDVRRYGATVTNYLGAMLSYLLAQP--PSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTE 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 cSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVK---GPQVMKGYWQRPEATEEILdAEGWLKTG 446
Cdd:cd05934 231 -TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTG 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 447 DIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDP-SLSVEELKAY 525
Cdd:cd05934 309 DLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGeTLDPEELFAF 388
|
490 500 510
....*....|....*....|....*....|....
gi 15598496 526 CKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05934 389 CEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
14-560 |
2.22e-83 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 269.54 E-value: 2.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAAYrsvveVFERScKKFADRPAFSN--LGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIA 91
Cdd:PLN02246 19 IPNHLPLHDY-----CFERL-SEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLHK-LGIRQGDVVMLLLPNCPEFVLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 92 VFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVylnvfgklveevlpdtrieylIEARMGDLLPALKgwlvnsVVKS 171
Cdd:PLN02246 92 FLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLII---------------------TQSCYVDKLKGLA------EDDG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 172 VKKMVPDYRLPQALPFRqALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQvhaqlsQLGKDGL 251
Cdd:PLN02246 145 VTVVTIDDPPEGCLHFS-ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ------QVDGENP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 252 PLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVD 331
Cdd:PLN02246 218 NLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGA-AILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 332 FSNLKLTNSG----GTALVSATAERwkgVTGCTVVEGYGLTECSPVVT------TNPYgeQARLGTVGIPVVGTALKVID 401
Cdd:PLN02246 297 LSSIRMVLSGaaplGKELEDAFRAK---LPNAVLGQGYGMTEAGPVLAmclafaKEPF--PVKSGSCGTVVRNAELKIVD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 402 -EQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:PLN02246 372 pETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 481 DVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PLN02246 452 ALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSeITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
.
gi 15598496 560 E 560
Cdd:PLN02246 532 A 532
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
49-560 |
1.14e-80 |
|
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: 259.62 E-value: 1.14e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVY 128
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVFGKlveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyRLPQALPfrqalkqgqghalqpvrvglED 208
Cdd:cd05903 80 PERFRQ---------------------------------------------FDPAAMP--------------------DA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLVANmlqVHAQLSQLGKDGlplmkeaQEVMIAPLPLYHIYAFTANCMCMMVSGNHNV 288
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSAS---IRQYAERLGLGP-------GDVFLVASPMAHQTGFVYGFTLPLLLGAPVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 289 L--ITNPRDIPGFVKELkkwRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYG 366
Cdd:cd05903 165 LqdIWDPDKALALMREH---GVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYG 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 367 LTECSPVVT-TNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDaEGWLKT 445
Cdd:cd05903 242 STECPGAVTsITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRT 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 446 GDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDP-SLSVEELKA 524
Cdd:cd05903 321 GDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGaLLTFDELVA 400
|
490 500 510
....*....|....*....|....*....|....*..
gi 15598496 525 YC-KENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05903 401 YLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
50-561 |
7.46e-80 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 259.41 E-value: 7.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYL 129
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 NVFGKLVEEVLPDTRIEYLIEarmgdlLPALKGWLVNSVVKSVKKmvpdyrlpqalpfrqalkqgqghalqpvrvGLEDV 209
Cdd:PRK06839 108 KTFQNMALSMQKVSYVQRVIS------ITSLKEIEDRKIDNFVEK------------------------------NESAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVANMLQvhaqlsqlgkDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVL 289
Cdd:PRK06839 152 FIICYTSGTTGKPKGAVLTQENMFWNALN----------NTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGV-II 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 290 ITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTA----LVSATAERwkgvtGCTVVEGY 365
Cdd:PRK06839 221 VPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPcpeeLMREFIDR-----GFLFGQGF 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 366 GLTECSPVVTTNPYGEQAR-LGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDaEGWLK 444
Cdd:PRK06839 296 GMTETSPTVFMLSEEDARRkVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLC 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 445 TGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELK 523
Cdd:PRK06839 375 TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSsSVLIEKDVI 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 15598496 524 AYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:PRK06839 455 EHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
35-560 |
5.34e-79 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 258.05 E-value: 5.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 35 KKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREM 114
Cdd:PRK07470 18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 115 RHQFKDAGVRALVYLNVFGKLVEEVLpdtrieyliearmgdllpALKGWLVNSVVKSVKKMVPDYrlpQALpfrqaLKQG 194
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHAAAVR------------------AASPDLTHVVAIGGARAGLDY---EAL-----VARH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 195 QGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNL---VANMLqvhaqlsqlgKDGLPLMKEaQEVMIAPLPLYH-- 269
Cdd:PRK07470 151 LGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHL----------ADLMPGTTE-QDASLVVAPLSHga 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 270 -IYAftancMCMMVSGNHNVLITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVS 347
Cdd:PRK07470 220 gIHQ-----LCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 348 ATAERWKGVTGCTVVEGYGLTECSPVVTTNPY-------GEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGP 420
Cdd:PRK07470 295 ADQKRALAKLGKVLVQYFGLGEVTGNITVLPPalhdaedGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDE 500
Cdd:PRK07470 375 AVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 501 KSGEAVKLFVVARDP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07470 454 VWGEVGVAVCVARDGaPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
48-545 |
4.23e-78 |
|
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: 253.29 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 48 VTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLY---TAREMRHQFKDAGVR 124
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIAL-GVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 125 ALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmVPDyrlpqalpfrqalkqgqghalqpvrv 204
Cdd:cd05907 80 ALF------------------------------------------------VED-------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 205 gLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSqlgkdglplmKEAQEVMIAPLPLYHIYAFTANCMCMMVSG 284
Cdd:cd05907 86 -PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP----------ATEGDRHLSFLPLAHVFERRAGLYVPLLAG 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 285 NHNVLITNPRDIPGfvkELKKWRFSALLGLNTLF------VALMEHPGFKDVDF-----SNLKLTNSGGTALVSATAERW 353
Cdd:cd05907 155 ARIYFASSAETLLD---DLSEVRPTVFLAVPRVWekvyaaIKVKAVPGLKRKLFdlavgGRLRFAASGGAPLPAELLHFF 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 354 KGVtGCTVVEGYGLTECSPVVTTNPyGEQARLGTVGIPVVGTALKVideqgnelpvGERGELCVKGPQVMKGYWQRPEAT 433
Cdd:cd05907 232 RAL-GIPVYEGYGLTETSAVVTLNP-PGDNRIGTVGKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEAT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 434 EEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYPNEIEDVVMAHPKVASCAAVGipDEKSgeavklFVVA 512
Cdd:cd05907 300 AEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG--DGRP------FLVA 371
|
490 500 510
....*....|....*....|....*....|....*.
gi 15598496 513 ---RDPslsvEELKAYCKENLTGYKIPRQIVLKDAL 545
Cdd:cd05907 372 livPDP----EALEAWAEEHGIAYTDVAELAANPAV 403
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
51-560 |
1.40e-77 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 254.09 E-value: 1.40e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLN 130
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 VFGKLVEEVLPD-TRIEYLIEARMGDLLPALKGWLVNSVVKSVKKMVPDYRLPQaLPFRQAlkqgqghalqpvrvgledv 209
Cdd:cd12119 106 DFLPLLEAIAPRlPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAAESPEYDWPD-FDENTA------------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVanmlqVHAqLSQLGKDGLPLmkEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHnVL 289
Cdd:cd12119 166 AAICYTSGTTGNPKGVVYSHRSLV-----LHA-MAALLTDGLGL--SESDVVLPVVPMFHVNAWGLPYAAAMVGAKL-VL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 290 iTNPRDIPGFVKEL---KKWRFSAllGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWK--GVTgctVVEG 364
Cdd:cd12119 237 -PGPYLDPASLAELierEGVTFAA--GVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEerGVR---VIHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 YGLTECSPVVTTN---------PYGEQARL-GTVGIPVVGTALKVIDEQGNELPV--GERGELCVKGPQVMKGYWQRPEA 432
Cdd:cd12119 311 WGMTETSPLGTVArppsehsnlSEDEQLALrAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEiLDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVA 512
Cdd:cd12119 391 SEA-LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598496 513 RDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd12119 470 KEGAtVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
39-560 |
2.80e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 247.03 E-value: 2.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNL--GVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRH 116
Cdd:PRK09088 10 QRLAAVDLalGRRWTYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 117 QFKDAGVRALVylnvfgklveevlpdtrieyliearmGDLLPALKGWLVNSV---VKSVKKMVPDYRlPQALPfrqalkq 193
Cdd:PRK09088 89 LLQDAEPRLLL--------------------------GDDAVAAGRTDVEDLaafIASADALEPADT-PSIPP------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 194 gqghalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLvanmLQVHAQLSQLGKdglplmKEAQEVMIAPLPLYHIYAF 273
Cdd:PRK09088 135 -------------ERVSLILFTSGTSGQPKGVMLSERNL----QQTAHNFGVLGR------VDAHSSFLCDAPMFHIIGL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 274 TANCMCMMVSGNhNVLITNprdipGF-VKELKKWRFSALLGLNTLFV------ALMEHPGFKDVDFSNLKLTNSGGtALV 346
Cdd:PRK09088 192 ITSVRPVLAVGG-SILVSN-----GFePKRTLGRLGDPALGITHYFCvpqmaqAFRAQPGFDAAALRHLTALFTGG-APH 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 347 SATAERWKGVTGCTVVEGYGLTECSPV--VTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMK 424
Cdd:PRK09088 265 AAEDILGWLDDGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 GYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:PRK09088 345 GYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 505 AVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK09088 425 VGYLAIVPADGApLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
39-562 |
1.90e-73 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 243.81 E-value: 1.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAF------SNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVvvnTNPL---Y 109
Cdd:PRK13295 39 DKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLAR-LGVGRGDVVSCQLPNWWEFTVLYLACSRIGAV---LNPLmpiF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 110 TAREMRHQFKDAGVRALVYLNVFGKLVEEVLPdtrieylieARMGDLLPALKGWLV--NSVVKSVKKMVPDYRLPQAlpf 187
Cdd:PRK13295 115 RERELSFMLKHAESKVLVVPKTFRGFDHAAMA---------RRLRPELPALRHVVVvgGDGADSFEALLITPAWEQE--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rqalkQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsQLGKDGLPLMkeaqevmiaPLPL 267
Cdd:PRK13295 183 -----PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILM---------ASPM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 268 YHIYAFTANCMCMMVSGNHNVL--ITNPRDipgFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTAL 345
Cdd:PRK13295 248 AHQTGFMYGLMMPVMLGATAVLqdIWDPAR---AAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTV-GIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMK 424
Cdd:PRK13295 325 PGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERASTTdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 GYWQRPEATEEilDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:PRK13295 405 GYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGE 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 505 AVKLFVVAR-DPSLSVEELKAYCKEN-LTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK13295 483 RACAFVVPRpGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLREML 542
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
208-555 |
8.51e-73 |
|
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: 235.47 E-value: 8.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHgnlvANMLQVHAQLSQLGKdglplMKEAQEVMIAPlPLYHIYAFTANCMCMMVSGNhN 287
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAH----RQTLRAAAAWADCAD-----LTEDDRYLIIN-PFFHTFGYKAGIVACLLTGA-T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGC-TVVEGYG 366
Cdd:cd17638 70 VVPVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTVLTAYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 367 LTECSPVVTTNPYGEQARLGTVgipvVGTALKvideqGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTG 446
Cdd:cd17638 150 LTEAGVATMCRPGDDAETVATT----CGRACP-----GFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 447 DIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDP-SLSVEELKAY 525
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGvTLTEEDVIAW 300
|
330 340 350
....*....|....*....|....*....|
gi 15598496 526 CKENLTGYKIPRQIVLKDALPMTPVGKILR 555
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
35-561 |
1.41e-72 |
|
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: 241.28 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 35 KKFADRPAFSN--LGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAR 112
Cdd:cd17642 28 ASVPGTIAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 113 EMRHQFkdaGVRALVYLNVFGKLVEEVLPdtrieyliearmgdllpalkgwlVNSVVKSVKKMV-----PDYRLPQALP- 186
Cdd:cd17642 107 ELDHSL---NISKPTIVFCSKKGLQKVLN-----------------------VQKKLKIIKTIIildskEDYKGYQCLYt 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 187 -FRQALKQG-QGHALQPVRVGL-EDVAVLQYTGGTTGVSKGAMLTHGNLVANMlqVHAQLSQLGKDGLPlmkeaQEVMIA 263
Cdd:cd17642 161 fITQNLPPGfNEYDFKPPSFDRdEQVALIMNSSGSTGLPKGVQLTHKNIVARF--SHARDPIFGNQIIP-----DTAILT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 264 PLPLYHIYAFTANcMCMMVSGNHNVLITNpRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGT 343
Cdd:cd17642 234 VIPFHHGFGMFTT-LGYLICGFRVVLMYK-FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 344 ALVSATAERWK---GVTGctVVEGYGLTECSPVVTTNPYGEqARLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKG 419
Cdd:cd17642 312 PLSKEVGEAVAkrfKLPG--IRQGYGLTETTSAILITPEGD-DKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 420 PQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPD 499
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPD 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 500 EKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPR-QIVLKDALPMTPVGKILRRELREI 561
Cdd:cd17642 469 EDAGELPAAVVVLEaGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
49-560 |
3.14e-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: 236.86 E-value: 3.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVralvy 128
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 lnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghalqpvrvGLED 208
Cdd:cd05912 75 ----------------------------------------------------------------------------KLDD 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLVAnmlqvHAQLSQLGkdglpLMKEAQEVMIAPLPLYH-----------IYAFTanc 277
Cdd:cd05912 79 IATIMYTSGTTGKPKGVQQTFGNHWW-----SAIGSALN-----LGLTEDDNWLCALPLFHisglsilmrsvIYGMT--- 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 mcmmvsgnhnVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALME-HPGFKDVDFSNLKLtnSGGTA---LVSATAERw 353
Cdd:cd05912 146 ----------VYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEiLGEGYPNNLRCILL--GGGPApkpLLEQCKEK- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 354 kgvtGCTVVEGYGLTE-CSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNElpvGERGELCVKGPQVMKGYWQRPEA 432
Cdd:cd05912 213 ----GIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDA 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVA 512
Cdd:cd05912 286 TEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS 364
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15598496 513 RDPsLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05912 365 ERP-ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-559 |
4.42e-72 |
|
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: 236.85 E-value: 4.42e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVyl 129
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 nvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghalqpvrVGLEDV 209
Cdd:cd05972 78 --------------------------------------------------------------------------TDAEDP 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVANMLQVhaqlsqlgkdGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVL 289
Cdd:cd05972 84 ALIYFTSGTTGLPKGVLHTHSYPLGHIPTA----------AYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 290 ITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEhPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLT 368
Cdd:cd05972 154 YEGPRfDAERILELLERYGVTSFCGPPTAYRMLIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQT 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 369 ECSPVVTTNPyGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVK--GPQVMKGYWQRPEATEEILdAEGWLKTG 446
Cdd:cd05972 233 ETGLTVGNFP-DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 447 DIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD---PSLS-VEEL 522
Cdd:cd05972 311 DRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyePSEElAEEL 390
|
490 500 510
....*....|....*....|....*....|....*..
gi 15598496 523 KAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05972 391 QGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-562 |
7.90e-72 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 233.91 E-value: 7.90e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANMlQVHAQLSQLGKDglplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNA-WMLALNSLFDPD---------DVLLCGLPLFHVNGSVVTLLTPLASGAHV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLIT-----NPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGfkDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVV 362
Cdd:cd05944 73 VLAGpagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVELRARFEDATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 363 EGYGLTECSPVVTTNPYGEQARLGTVGIPV--VGTALKVIDEQGNEL---PVGERGELCVKGPQVMKGYWQRpEATEEIL 437
Cdd:cd05944 151 EGYGLTEATCLVAVNPPDGPKRPGSVGLRLpyARVRIKVLDGVGRLLrdcAPDEVGEICVAGPGVFGGYLYT-EGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 438 DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFV-VARDPS 516
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15598496 517 LSVEELKAYCKENLTGY-KIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:cd05944 310 VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
33-561 |
1.20e-71 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 239.36 E-value: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 33 SCKKFADRPAF--SNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYT 110
Cdd:PLN02574 48 SHHNHNGDTALidSSTGFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 111 AREMRHQFKDAGVrALVYlnvfgklveeVLPDTRIEyliearmgdlLPALkGWLVNSVVKSVKKmvpDYRLPQALPFRQA 190
Cdd:PLN02574 128 LGEIKKRVVDCSV-GLAF----------TSPENVEK----------LSPL-GVPVIGVPENYDF---DSKRIEFPKFYEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 191 LKQGQGHALQPVrVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANM-LQVHAQLSQLGKDGlplmkeAQEVMIAPLPLYH 269
Cdd:PLN02574 183 IKEDFDFVPKPV-IKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVeLFVRFEASQYEYPG------SDNVYLAALPMFH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 270 IYAFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHP-GFKDVDFSNLKLTNSGGTALVSA 348
Cdd:PLN02574 256 IYGLSLFVVGLLSLGS-TIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAAPLSGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 349 TAERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQ-ARLGTVGIPVVGTALKVID-EQGNELPVGERGELCVKGPQVMKG 425
Cdd:PLN02574 335 FIQDFvQTLPHVDFIQGYGMTESTAVGTRGFNTEKlSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 426 YWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEA 505
Cdd:PLN02574 415 YLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEI 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 506 VKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:PLN02574 495 PVAFVVRRQGStLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
47-560 |
1.41e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 237.49 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRAL 126
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 VylnvfgklveevlpdtrieylIEARMGDLLPALKGWLVNSVVKSvkkMVPDYRLPQALPFRQALKQGQGHALQPVRVGl 206
Cdd:PRK08276 88 I---------------------VSAALADTAAELAAELPAGVPLL---LVVAGPVPGFRSYEEALAAQPDTPIADETAG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 edvAVLQYTGGTTGVSKGAM--LTHGNLVANMLQVHAQLsqlgkdGLPLMKEAQEVMIAPLPLYHiyafTA-NCMCMMV- 282
Cdd:PRK08276 143 ---ADMLYSSGTTGRPKGIKrpLPGLDPDEAPGMMLALL------GFGMYGGPDSVYLSPAPLYH----TApLRFGMSAl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPgfKDV----DFSNLKLTnsggtalVSATA-------- 350
Cdd:PRK08276 210 ALGGTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKLP--EEVraryDVSSLRVA-------IHAAApcpvevkr 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 351 ---ERWkgvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTaLKVIDEQGNELPVGERGELCVKGPQVMKGYW 427
Cdd:PRK08276 281 amiDWW----GPIIHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 428 QRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVK 507
Cdd:PRK08276 356 NDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVK 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 508 LFV-----VARDPSLSvEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK08276 436 AVVqpadgADAGDALA-AELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
43-562 |
1.17e-70 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 234.92 E-value: 1.17e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 43 FSNLGVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNplYTA--REMRHQFKD 120
Cdd:cd05909 1 EDTLGTSLTYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVMLN--YTAglRELRACIKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 121 AGVRALVYLNVF---GKLV--EEVLPDTRIEYLIEARmGDLLPALKgwlvnsvVKSVKKMvpdyRLPQALPFRQALKQGQ 195
Cdd:cd05909 77 AGIKTVLTSKQFiekLKLHhlFDVEYDARIVYLEDLR-AKISKADK-------CKAFLAG----KFPPKWLLRIFGVAPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 196 ghalQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSqlgkdglplmKEAQEVMIAPLPLYHIYAFTA 275
Cdd:cd05909 145 ----QP-----DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD----------PNPEDVVFGALPFFHSFGLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 276 NCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALME--HPgfkdVDFSNLKLTNSGGTALVSATAERW 353
Cdd:cd05909 206 CLWLPLLSGIKVVFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYARaaHP----EDFSSLRLVVAGAEKLKDTLRQEF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 354 KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGN-ELPVGERGELCVKGPQVMKGYWQRPEA 432
Cdd:cd05909 282 QEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAH-PKVASCAAVGIPDEKSGEAVKLFVV 511
Cdd:cd05909 362 TSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTT 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 512 arDPSLSVEELKAYCKE----NLTgykIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:cd05909 441 --TTDTDPSSLNDILKNagisNLA---KPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
40-559 |
2.07e-69 |
|
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: 230.06 E-value: 2.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 40 RPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMrhqfk 119
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 120 dagvralvylnvfgklvEEVLPDTRIEYLIEArmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqgHAL 199
Cdd:cd05958 76 -----------------AYILDKARITVALCA---------------------------------------------HAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 200 QPVrvglEDVAVLQYTGGTTGVSKGAMLTHGNL--VANMLQVHAqlsqlgkdglpLMKEAQEVMIAPLPLYHIYAFTANC 277
Cdd:cd05958 94 TAS----DDICILAFTSGTTGAPKATMHFHRDPlaSADRYAVNV-----------LRLREDDRFVGSPPLAFTFGLGGVL 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 MCMMVSGNHNVLI--TNPRDIPGFVKELKKwrfSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKG 355
Cdd:cd05958 159 LFPFGVGASGVLLeeATPDLLLSAIARYKP---TVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKE 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 356 VTGCTVVEGYGLTECSPVVTTNPyGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQvmkGYWQRPEATEE 435
Cdd:cd05958 236 ATGIPIIDGIGSTEMFHIFISAR-PGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 436 ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-- 513
Cdd:cd05958 312 TYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpg 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598496 514 ---DPSLsVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05958 392 vipGPVL-ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
11-560 |
4.74e-69 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 232.18 E-value: 4.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 11 PAGVPDSLdfaayrSVVEVFERSCKKFADRPAF--SNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQY 88
Cdd:PLN02330 21 SVPVPDKL------TLPDFVLQDAELYADKVAFveAVTGKAVTYGEVVRDTRRFAKAL-RSLGLRKGQVVVVVLPNVAEY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 89 PIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNV-FGKLVEEVLPDTRI-EYLIEARMG--DLLPALKgwl 164
Cdd:PLN02330 94 GIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTnYGKVKGLGLPVIVLgEEKIEGAVNwkELLEAAD--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 165 vnsvvksvkkmvpdyRLPQALPFRQALKQgqghalqpvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLVANMLqvhAQLS 244
Cdd:PLN02330 171 ---------------RAGDTSDNEEILQT--------------DLCALPFSSGTTGISKGVMLTHRNLVANLC---SSLF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 245 QLGKDGLplmkeAQEVMIAPLPLYHIYAFTANCmCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEH 324
Cdd:PLN02330 219 SVGPEMI-----GQVVTLGLIPFFHIYGITGIC-CATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 325 PGFKDVDFSNLKLTNSGGTA------LVSATAERWKGVTgctVVEGYGLTECSPVVTTNPYGEQ----ARLGTVGIPVVG 394
Cdd:PLN02330 293 PIVEEFDLSKLKLQAIMTAAaplapeLLTAFEAKFPGVQ---VQEAYGLTEHSCITLTHGDPEKghgiAKKNSVGFILPN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 395 TALKVID-EQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFN 473
Cdd:PLN02330 370 LEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 474 VYPNEIEDVVMAHPKVASCAAVGIPDEKSGE-AVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGK 552
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEiPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
|
....*...
gi 15598496 553 ILRRELRE 560
Cdd:PLN02330 530 IMRRLLKE 537
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
39-560 |
1.01e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 231.20 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVylnvfgklVEEVLPDtrieylIEARMGDLLPALKgwLVNSVVKSVKKMVPDYrlpqalpfrQALKQGQGHA 198
Cdd:PRK07786 111 SDCGAHVVV--------TEAALAP------VATAVRDIVPLLS--TVVVAGGSSDDSVLGY---------EDLLAEAGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlQVHAQLSQLGKDglplmkEAQEVMIAPLPLYHIyAFTANCM 278
Cdd:PRK07786 166 HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTG---QAMTCLRTNGAD------INSDVGFVGVPLFHI-AGIGSML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNHNVLI-TNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDfsnLKLTN-SGGTALVSATAERWKGV 356
Cdd:PRK07786 236 PGLLLGAPTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRD---LALRVlSWGAAPASDTLLRQMAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 T--GCTVVEGYGLTECSPVvTTNPYGEQA--RLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEA 432
Cdd:PRK07786 313 TfpEAQILAAFGQTEMSPV-TCMLLGEDAirKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEILDAeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEaVKLFVVA 512
Cdd:PRK07786 392 TAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGE-VPVAVAA 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15598496 513 RDPS---LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07786 470 VRNDdaaLTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
40-559 |
1.49e-68 |
|
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: 227.73 E-value: 1.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 40 RPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFK 119
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 120 DAGVRALVylnvfgklveevlpdtrieylIEArmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghal 199
Cdd:cd05919 80 DCEARLVV---------------------TSA------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 200 qpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVanmlqVHAQLsqLGKDGLPLmKEAQEVMIAPlPLYHIYAFTANCMC 279
Cdd:cd05919 91 -------DDIAYLLYSSGTTGPPKGVMHAHRDPL-----LFADA--MAREALGL-TPGDRVFSSA-KMFFGYGLGNSLWF 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 280 MMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGC 359
Cdd:cd05919 155 PLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGG 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 360 TVVEGYGLTECSPVVTTNPYGeQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILdA 439
Cdd:cd05919 235 PILDGIGATEVGHIFLSNRPG-AWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-N 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 440 EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLS- 518
Cdd:cd05919 313 GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPq 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15598496 519 ---VEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05919 393 eslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
24-562 |
2.25e-68 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 239.44 E-value: 2.25e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAFSN-LGVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGALRAGLVV 102
Cdd:PRK08633 615 PPLAEAWIDTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKREL--KDEENVGILLPPSVAGALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 103 VNTNplYTARE--MRHQFKDAGVRALVYLNVF-GKL-----VEEVLPDTRIEYliearMGDLLPALkgwlvnSVVKSVKK 174
Cdd:PRK08633 693 VNLN--YTASEaaLKSAIEQAQIKTVITSRKFlEKLknkgfDLELPENVKVIY-----LEDLKAKI------SKVDKLTA 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 175 MVPDYRLPQALpfrqaLKQGQGHAlqpvrVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMlqvhAQLSQLgkdglpLM 254
Cdd:PRK08633 760 LLAARLLPARL-----LKRLYGPT-----FKPDDTATIIFSSGSEGEPKGVMLSHHNILSNI----EQISDV------FN 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 255 KEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSN 334
Cdd:PRK08633 820 LRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFAS 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 335 LKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTN-P------YGEQA--RLGTVGIPVVGTALKVID-EQG 404
Cdd:PRK08633 900 LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNlPdvlaadFKRQTgsKEGSVGMPLPGVAVRIVDpETF 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGERGELCVKGPQVMKGYWQRPEATEEIL---DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:PRK08633 980 EELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEE 1059
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 482 ---VVMAHPKVaSCAAVGIPDEKSGEavKLFVVARDPSLSVEELKAYCKE-NLTGYKIPRQIVLKDALPMTPVGKILRRE 557
Cdd:PRK08633 1060 elaKALGGEEV-VFAVTAVPDEKKGE--KLVVLHTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKG 1136
|
....*
gi 15598496 558 LREIA 562
Cdd:PRK08633 1137 LKELA 1141
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
39-561 |
4.49e-68 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 227.92 E-value: 4.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVYLNVFgklVEEVLPDTRIEYliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrQALKQGQGHA 198
Cdd:PRK03640 96 DDAEVKCLITDDDF---EAKLIPGISVKF-----------------------------------------AELMNGPKEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVR-VGLEDVAVLQYTGGTTGVSKGAMLTHGNlvanmlqvH---AQLSQLGKdGLplmkEAQEVMIAPLPLYHIYAFT 274
Cdd:PRK03640 132 AEIQEeFDLDEVATIMYTSGTTGKPKGVIQTYGN--------HwwsAVGSALNL-GL----TEDDCWLAAVPIFHISGLS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 275 AncmcMMVS---GNHNVLIT--NPRDIPGFVKELKKWRFSALLG-LNTLFVALME---HPGFKDVdfsnlkLTNSGGTAL 345
Cdd:PRK03640 199 I----LMRSviyGMRVVLVEkfDAEKINKLLQTGGVTIISVVSTmLQRLLERLGEgtyPSSFRCM------LLGGGPAPK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERWKGVTgctVVEGYGLTE-CSPVVTTNPYGEQARLGTVGIPVVGTALKvIDEQGNELPVGERGELCVKGPQVMK 424
Cdd:PRK03640 269 PLLEQCKEKGIP---VYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELK-IEKDGVVVPPFEEGEIVVKGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 GYWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:PRK03640 345 GYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQ 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 505 AVKLFVVArDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:PRK03640 424 VPVAFVVK-SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
24-558 |
1.37e-67 |
|
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: 226.44 E-value: 1.37e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVV 103
Cdd:cd05920 15 EPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 104 NTNPLYTAREMRHQFKDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmVPDyrlPQ 183
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYI------------------------------------------------VPD---RH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 184 ALPFRQALKQgQGHALQPvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLVANMlQVHAQLSQLGkdglplmkeAQEVMIA 263
Cdd:cd05920 123 AGFDHRALAR-ELAESIP------EVALFLLSGGTTGTPKLIPRTHNDYAYNV-RASAEVCGLD---------QDTVYLA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 264 PLPLYHIYAFTANCMC-MMVSGNHNVLITNPRdiPGFVKEL-KKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSG 341
Cdd:cd05920 186 VLPAAHNFPLACPGVLgTLLAGGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 342 GTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVV-GTALKVIDEQGNELPVGERGELCVKGP 420
Cdd:cd05920 264 GARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEVIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDE 500
Cdd:cd05920 344 YTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDE 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 501 KSGEAVKLFVVARDPSLSVEELKAYCKE-NLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05920 424 LLGERSCAFVVLRDPPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
24-561 |
7.13e-67 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 226.18 E-value: 7.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVV 103
Cdd:PRK06155 21 RTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 104 NTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPdtrieyliearmGDL-LPALkgWLVNSVvksvkkmvPDYRLP 182
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADP------------GDLpLPAV--WLLDAP--------ASVSVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 183 Q---ALPFRQAlkqgqGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHgnlvanmlqvhAQLSQLGKDGLPLMK-EAQ 258
Cdd:PRK06155 158 AgwsTAPLPPL-----DAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPH-----------AQFYWWGRNSAEDLEiGAD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 259 EVMIAPLPLYHIYAFTAnCMCMMVSGNHNVLitNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKL 337
Cdd:PRK06155 222 DVLYTTLPLFHTNALNA-FFQALLAGATYVL--EPRfSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 338 TNSGGT--ALVSATAERwkgvTGCTVVEGYGLTECSPVVTTnPYGEQaRLGTVGIPVVGTALKVIDEQGNELPVGERGEL 415
Cdd:PRK06155 299 ALGPGVpaALHAAFRER----FGVDLLDGYGSTETNFVIAV-THGSQ-RPGSMGRLAPGFEARVVDEHDQELPDGEPGEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQ---VMKGYWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASC 492
Cdd:PRK06155 373 LLRADEpfaFATGYFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 493 AAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:PRK06155 452 AVFPVPSELGEDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
38-559 |
1.27e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 223.71 E-value: 1.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAFSNLGVTLSYAELDRLSAAFAAylqkqtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQ 117
Cdd:PRK07787 14 DIADAVRIGGRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 118 FKDAGVRALVylnvfGKLVEEVLPDTRIEYLIEARmgdllpalkGWLvnsvvksvkkmvpdyRLPQALPfrqalkqgqgh 197
Cdd:PRK07787 88 LADSGAQAWL-----GPAPDDPAGLPHVPVRLHAR---------SWH---------------RYPEPDP----------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 alqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMlqvhaqlsqlgkDGLPLMKE--AQEVMIAPLPLYHIYAFTA 275
Cdd:PRK07787 128 ---------DAPALIVYTSGTTGPPKGVVLSRRAIAADL------------DALAEAWQwtADDVLVHGLPLFHVHGLVL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 276 NCMCMMVSGNHNVLITNPRdiPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVdFSNLKLTNSGGTALVSATAERWKG 355
Cdd:PRK07787 187 GVLGPLRIGNRFVHTGRPT--PEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAA 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 356 VTGCTVVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVVGTALKVIDEQGNELPV-GER-GELCVKGPQVMKGYWQRPEAT 433
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGER-RPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDAT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 434 EEILDAEGWLKTGDIAVIDEDGFVRIVDRKK-DLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVA 512
Cdd:PRK07787 343 AAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVG 422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598496 513 RDPSlSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK07787 423 ADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-559 |
3.63e-66 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 222.32 E-value: 3.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 60 AAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAG----LVVVNTNPLYTAREMRHQFKDAGvralvylnvfGKL 135
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAG----------GRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 136 VeevlpdtrieyLIEARMGDLLpalkgwlvnsvvksvKKMVPDYRLPQALPFRQALKqGQGHALQPVRVGLEDVAVLQYT 215
Cdd:cd05922 73 V-----------LADAGAADRL---------------RDALPASPDPGTVLDADGIR-AARASAPAHEVSHEDLALLLYT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 216 GGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGLPlmkeaqevmiAPLPLYHIYAFTANCMCMMVSGNhnvLITNPRD 295
Cdd:cd05922 126 SGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL----------TVLPLSYDYGLSVLNTHLLRGAT---LVLTNDG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 296 IP--GFVKELKKWRFSALLGLNTLFvALMEHPGFKDVDFSNLK-LTNSGG---TALVSATAErwKGVtGCTVVEGYGLTE 369
Cdd:cd05922 193 VLddAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPSLRyLTQAGGrlpQETIARLRE--LLP-GAQVYVMYGQTE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 CSPVVTTNPyGEQA--RLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGD 447
Cdd:cd05922 269 ATRRMTYLP-PERIleKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 448 IAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEkSGEAVKLFVVArDPSLSVEELKAYCK 527
Cdd:cd05922 348 LARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTA-PDKIDPKDVLRSLA 425
|
490 500 510
....*....|....*....|....*....|..
gi 15598496 528 ENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05922 426 ERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
208-555 |
3.81e-64 |
|
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: 212.90 E-value: 3.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglplmkeaqeVMIAPLPLYHIYAFTANcMCMMVSGNHN 287
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEAD----------VYLNMLPLFHIAGLNLA-LATFHAGGAN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLITnprdipgfvkelkkwRFSALLGLN-------TLFV-------ALMEHPGFKDVDFSNLKLTnsggTAL-VSATAER 352
Cdd:cd17637 70 VVME---------------KFDPAEALElieeekvTLMGsfppilsNLLDAAEKSGVDLSSLRHV----LGLdAPETIQR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 353 WKGVTGCTVVEGYGLTECSPVVTTNPYGEqaRLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEA 432
Cdd:cd17637 131 FEETTGATFWSLYGQTETSGLVTLSPYRE--RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPEL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEEILDaEGWLKTGDIAVIDEDGFVRIVDRK--KDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLfV 510
Cdd:cd17637 209 TAYTFR-NGWHHTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKA-V 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15598496 511 VARDP--SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILR 555
Cdd:cd17637 287 CVLKPgaTLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
38-558 |
1.05e-63 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 215.08 E-value: 1.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLytaremrhq 117
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYV---PL--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 118 fkDAGvralvylnvfgklveevLPDTRIEYLIEarmgDLLPALkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqgh 197
Cdd:cd05930 68 --DPS-----------------YPAERLAYILE----DSGAKL------------------------------------- 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 alqpVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLGkdglplmkeAQEVMIAPLPLYHIYAFTAnc 277
Cdd:cd05930 88 ----VLTDPDDLAYVIYTSGSTGKPKGVMVEHRGLV-NLLLWMQEAYPLT---------PGDRVLQFTSFSFDVSVWE-- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 MCMMVSGNHNVLITNP---RDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDvdFSNLKLTNSGGTALVSATAERWK 354
Cdd:cd05930 152 IFGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAA--LPSLRLVLVGGEALPPDLVRRWR 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 355 GV-TGCTVVEGYGLTECSPVVTTNPYGEQARLG---TVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRP 430
Cdd:cd05930 230 ELlPGARLVNLYGPTEATVDATYYRVPPDDEEDgrvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 431 EATEE-----ILDAEGWL-KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:cd05930 310 ELTAErfvpnPFGPGERMyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEK 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 505 AVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05930 390 RLVAYVVPDEgGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
49-559 |
1.27e-63 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 216.86 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRlSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVY 128
Cdd:PRK08008 37 RYSYLELNE-EINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVFGKLVEEVLP--DTRIEYLIEARMGdlLPALKGwlvnsvvksvkkmvpdyrlpqALPFRQALKQGQGHALQPVRVGL 206
Cdd:PRK08008 116 SAQFYPMYRQIQQedATPLRHICLTRVA--LPADDG---------------------VSSFTQLKAQQPATLCYAPPLST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQlSQLGKDglplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
Cdd:PRK08008 173 DDTAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQ-CALRDD---------DVYLTVMPAFHIDCQCTAAMAAFSAGAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLIT--NPRdipGFVKELKKWRFSALLGLNTLFVALMEHPG--------FKDVDFSnLKLTNSGGTALVsataERWkgv 356
Cdd:PRK08008 243 FVLLEkySAR---AFWGQVCKYRATITECIPMMIRTLMVQPPsandrqhcLREVMFY-LNLSDQEKDAFE----ERF--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 tGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKG---PQVMKGYWQRPEAT 433
Cdd:PRK08008 312 -GVRLLTSYGMTETIVGIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKAT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 434 EEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVV-A 512
Cdd:PRK08008 391 AKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVlN 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598496 513 RDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK08008 471 EGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
39-560 |
3.17e-63 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 215.71 E-value: 3.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAF--SNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRH 116
Cdd:PRK13391 12 DKPAVimASTGEVVTYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 117 QFKDAGVRALVylnvfgklveevlpDTRIEYLIEARMGDLLPALKGWLVnsvVKSVKKMVPDYRLPQALPfrqalkqgqg 196
Cdd:PRK13391 91 IVDDSGARALI--------------TSAAKLDVARALLKQCPGVRHRLV---LDGDGELEGFVGYAEAVA---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 197 hALQPVRVGLEDVAV-LQYTGGTTGVSKG--AMLTHGNLVANM--LQVHAQLSQLGKDglplmkeaqEVMIAPLPLYHIy 271
Cdd:PRK13391 144 -GLPATPIADESLGTdMLYSSGTTGRPKGikRPLPEQPPDTPLplTAFLQRLWGFRSD---------MVYLSPAPLYHS- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 272 AFTANCMCMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPgfKDV----DFSNLKltnsggtALVS 347
Cdd:PRK13391 213 APQRAVMLVIRLGG-TVIVMEHFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLP--EEVrdkyDLSSLE-------VAIH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 348 ATA-----------ERWkgvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTaLKVIDEQGNELPVGERGELC 416
Cdd:PRK13391 283 AAApcppqvkeqmiDWW----GPIIHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIW 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 417 VKGPQVMKgYWQRPEATEEILDAEG-WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:PRK13391 358 FEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVF 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 496 GIPDEKSGEAVKLFV-----VARDPSLSvEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK13391 437 GVPNEDLGEEVKAVVqpvdgVDPGPALA-AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
29-552 |
3.60e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 213.59 E-value: 3.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 29 VFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPL 108
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 109 YTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDT-RIEYLIEARMGDLLPALKGwlvnsvvksvkkmvpdyrlpqALPF 187
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLpKLRTLVVVEDGSGNDLLPG---------------------AVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 RQALKQGQGHALQPVRVGlEDVAVLqYTGGTTGVSKGAMLTHGNLVANML---------QVHA--QLSQLGKDGlplmkE 256
Cdd:PRK07798 146 EDALAAGSPERDFGERSP-DDLYLL-YTGGTTGMPKGVMWRQEDIFRVLLggrdfatgePIEDeeELAKRAAAG-----P 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 257 AQEVMIAPlPLYHIYAFTANCMCMMvSGNHNVLITNPRDIPGFVkelkkWRFSALLGLNTLFV-----------ALmEHP 325
Cdd:PRK07798 219 GMRRFPAP-PLMHGAGQWAAFAALF-SGQTVVLLPDVRFDADEV-----WRTIEREKVNVITIvgdamarplldAL-EAR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 326 GfkDVDFSNLKLTNSGGTALVSATAERW-KGVTGCTVVEGYGLTE---CSPVVTTNpyGEQARLG-TVGIpvvGTALKVI 400
Cdd:PRK07798 291 G--PYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSEtgfGGSGTVAK--GAVHTGGpRFTI---GPRTVVL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 401 DEQGNELPVG--ERGELCVKGPqVMKGYWQRPEATEEIL---DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVY 475
Cdd:PRK07798 364 DEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPEKTAETFptiDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVF 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 476 PNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGK 552
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREgARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
51-559 |
1.10e-60 |
|
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: 206.90 E-value: 1.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVyln 130
Cdd:cd05971 8 TFKELKTASNRFANVL-KEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 vfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvPDyrlpqalpfrqalkqgqghalqpvrvGLEDVA 210
Cdd:cd05971 84 ----------------------------------------------TD--------------------------GSDDPA 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 211 VLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGLPLMKEAQ--------EVMIA------PLPLYHIYAFTAN 276
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPADwawiggllDVLLPslyfgvPVLAHRMTKFDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 277 CMCMMVSgNHNVliTNPRDIPGFVKELKkwrfsallglntlfvalmEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGV 356
Cdd:cd05971 172 AALDLMS-RYGV--TTAFLPPTALKMMR------------------QQGEQLKHAQVKLRAIATGGESLGEELLGWAREQ 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 TGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQ--VMKGYWQRPEATE 434
Cdd:cd05971 231 FGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 435 EILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARd 514
Cdd:cd05971 311 KKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLN- 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15598496 515 PSLS-----VEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05971 389 PGETpsdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
32-560 |
1.18e-60 |
|
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: 209.79 E-value: 1.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 32 RSCKKFADRPAF------SNLGVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVnt 105
Cdd:cd05931 1 RRAAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 106 nPLYTAREMRHQ------FKDAGVRAlvylnvfgklveeVLPDTrieyliearmgDLLPALKGWLVNsvvksvkkmVPDY 179
Cdd:cd05931 77 -PLPPPTPGRHAerlaaiLADAGPRV-------------VLTTA-----------AALAAVRAFAAS---------RPAA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 180 RLPQaLPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQlgkdglplmkEAQE 259
Cdd:cd05931 123 GTPR-LLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGL----------DPGD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 260 VMIAPLPLYHIYAFTANCMCMMVSGNHNVLITnPRDipgFVKELKKW-----RFSAllglnTLFVAlmehPGF------- 327
Cdd:cd05931 192 VVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMS-PAA---FLRRPLRWlrlisRYRA-----TISAA----PNFaydlcvr 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 328 -------KDVDFSNLKLTNSGG----TALVSATAERWK--GVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTV------ 388
Cdd:cd05931 259 rvrdedlEGLDLSSWRVALNGAepvrPATLRRFAEAFApfGFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLRVdrdala 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 389 -------------------GIPVVGTALKVIDEQGN-ELPVGERGELCVKGPQVMKGYWQRPEATEEI------LDAEGW 442
Cdd:cd05931 339 gravavaaddpaarelvscGRPLPDQEVRIVDPETGrELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGW 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 443 LKTGDIAVIDEDGFVrIVDRKKDLILVSGFNVYPNEIEDVVMAHPKV---ASCAAVGIPDEKSGEAVklFVVARDPSLSV 519
Cdd:cd05931 419 LRTGDLGFLHDGELY-ITGRLKDLIIVRGRNHYPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERLV--VVAEVERGADP 495
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 15598496 520 EELKAYCKE------NLTGYKiPRQIVLK--DALPMTPVGKILRRELRE 560
Cdd:cd05931 496 ADLAAIAAAiraavaREHGVA-PADVVLVrpGSIPRTSSGKIQRRACRA 543
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
19-561 |
1.34e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 209.78 E-value: 1.34e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 19 DFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPN--VLQYPIAVFGAL 96
Cdd:PRK07788 44 DIRRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLL-ALGVRAGDGVAVLARNhrGFVLALYAAGKV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 97 RAGLVVVNTNplyTAREmrhQFKDA----GVRALVYLNVFGKLVEEVLPDtrieyliearmgdlLPALKGWLVNsvVKSV 172
Cdd:PRK07788 123 GARIILLNTG---FSGP---QLAEVaareGVKALVYDDEFTDLLSALPPD--------------LGRLRAWGGN--PDDD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 173 KKMVPDYRLPQAL-------PFRQALKQGqghalqpvrvGLedvaVLQyTGGTTGVSKGAMLTHgnlvANMLQVHAQLSq 245
Cdd:PRK07788 181 EPSGSTDETLDDLiagsstaPLPKPPKPG----------GI----VIL-TSGTTGTPKGAPRPE----PSPLAPLAGLL- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 lgkDGLPLmkEAQEVMIAPLPLYHIYAFtANCMCMMVSGNHNVLitnPR--DIPGFVKELKKWRFSALLGLNTLFVALME 323
Cdd:PRK07788 241 ---SRVPF--RAGETTLLPAPMFHATGW-AHLTLAMALGSTVVL---RRrfDPEATLEDIAKHKATALVVVPVMLSRILD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 324 HPG--FKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVID 401
Cdd:PRK07788 312 LGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 402 EQGNELPVGERGELCVKGPQVMKGYWQRPeaTEEILDaeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:PRK07788 392 ENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVED 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 482 VVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07788 468 LLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
.
gi 15598496 561 I 561
Cdd:PRK07788 548 M 548
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
50-560 |
3.41e-59 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 204.93 E-value: 3.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVyl 129
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 nvfgklveevlpdtrieylIEArmgDLLPALKGWLVNSV----VKSVKKMVPDYRLPQALP--------FRQALKQGQGH 197
Cdd:PRK12406 89 -------------------AHA---DLLHGLASALPAGVtvlsVPTPPEIAAAYRISPALLtppagaidWEGWLAQQEPY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 ALQPVrvglEDVAVLQYTGGTTGVSKGamLTHGNLVANMLQVHAQLSQLGKdGLPLmkeaQEVMIAPLPLYHiyafTA-N 276
Cdd:PRK12406 147 DGPPV----PQPQSMIYTSGTTGHPKG--VRRAAPTPEQAAAAEQMRALIY-GLKP----GIRALLTGPLYH----SApN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 277 CMCMMVSGNHNVLITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHPgfKDV----DFSNLKLTNSGG----TALVS 347
Cdd:PRK12406 212 AYGLRAGRLGGVLVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKLP--EEVrakyDVSSLRHVIHAAapcpADVKR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 348 ATAERWkgvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMK-GY 426
Cdd:PRK12406 290 AMIEWW----GPVIYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 427 WQRPEATEEIlDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAV 506
Cdd:PRK12406 366 HNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEAL 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 507 KLfVVARDP--SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK12406 445 MA-VVEPQPgaTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
39-560 |
7.49e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 203.58 E-value: 7.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGML-HARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALvylnvfgkLVEEVLpdtrieyliearmgDLLPALkgwlvnsvvkSVKKMVPDYRLPQALpfrQALKQGQGHA 198
Cdd:PRK06145 96 GDAGAKLL--------LVDEEF--------------DAIVAL----------ETPKIVIDAAAQADS---RRLAQGGLEI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQvhaQLSQLGkdglpLMKEAQEVMIAPLplYHIYAFTANCM 278
Cdd:PRK06145 141 PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSID---HVIALG-----LTASERLLVVGPL--YHVGAFDLPGI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGV-T 357
Cdd:PRK06145 211 AVLWVGG-TLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 358 GCTVVEGYGLTE-CSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEI 436
Cdd:PRK06145 290 RARYIDAYGLTEtCSGDTLMEAGREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 437 LdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-P 515
Cdd:PRK06145 370 F-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgA 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15598496 516 SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06145 449 TLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
47-558 |
2.00e-58 |
|
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: 202.35 E-value: 2.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAEL-DRLSAAFAAYLQKqtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRA 125
Cdd:cd05923 26 GLRLTYSELrARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 126 LVYLNVfgklvEEVLPDTRIEYLIEARMGDLlpalkgwlvnsvvksvkkmvPDYRLPQALpfrqalkqgqGHALQPVRVG 205
Cdd:cd05923 104 AVIAVD-----AQVMDAIFQSGVRVLALSDL--------------------VGLGEPESA----------GPLIEDPPRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 206 LEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGlplmkeaqEVMIAPLPLYHIYAFTANCMCMMVSGN 285
Cdd:cd05923 149 PEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRH--------NVVLGLMPLYHVIGFFAVLVAALALDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 286 HNVLITNprDIPGFVKEL-KKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEG 364
Cdd:cd05923 221 TYVVVEE--FDPADALKLiEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 YGLTEcspvVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNE---LPVGERGELCVK--GPQVMKGYWQRPEATEEILdA 439
Cdd:cd05923 299 YGTTE----AMNSLYMRDARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-Q 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 440 EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSV 519
Cdd:cd05923 374 DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSA 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15598496 520 EELKAYCKEN-LTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05923 454 DELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
31-560 |
3.04e-58 |
|
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: 201.76 E-value: 3.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 31 ERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYT 110
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALG-ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 111 AREMRHQFKDAGVRALvylnvfgklveevLPDTRIEYliearmGDLLPALKGWlvnsvvksvkkmvPDYRLPQalpfrqa 190
Cdd:cd12118 90 AEEIAFILRHSEAKVL-------------FVDREFEY------EDLLAEGDPD-------------FEWIPPA------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 191 lkqgqghalqpvrvGLEDVAVLQYTGGTTGVSKGAMLTH--------GNLVANMLQVHAqlsqlgkdglplmkeaqeVMI 262
Cdd:cd12118 131 --------------DEWDPIALNYTSGTTGRPKGVVYHHrgaylnalANILEWEMKQHP------------------VYL 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 263 APLPLYHiyaftANCMC----MMVSGNHNVLITNPrDIPGFVKELKKWRFSALLGLNTLFVALMEHPgfkDVDFSNLKLT 338
Cdd:cd12118 179 WTLPMFH-----CNGWCfpwtVAAVGGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAP---PSDARPLPHR 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 339 NSGGTALVSATAERWKGVT--GCTVVEGYGLTECSPVVTTN---------PYGEQARL-GTVGIPVVG-TALKVIDEQGN 405
Cdd:cd12118 250 VHVMTAGAPPPAAVLAKMEelGFDVTHVYGLTETYGPATVCawkpewdelPTEERARLkARQGVRYVGlEEVDVLDPETM 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 406 ElPV---GER-GELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:cd12118 330 K-PVprdGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEG 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 482 VVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDaLPMTPVGKILRRELRE 560
Cdd:cd12118 408 VLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
47-555 |
4.34e-58 |
|
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: 200.75 E-value: 4.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAgvral 126
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHS----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 vylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvKSVKKMVPDYrlpqalpfrqalkqgqghalqpvrvgl 206
Cdd:cd05914 79 -------------------------------------------EAKAIFVSDE--------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlgkdglplMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV----------LLGKGDKILSILPLHHIYPLTFTLLLPLLNGAH 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLITNPRD-------------------------------IPGFVKELKKWRFSALLG----LNTLFVALMEHPGfkdvd 331
Cdd:cd05914 159 VVFLDKIPSakiialafaqvtptlgvpvplviekifkmdiIPKLTLKKFKFKLAKKINnrkiRKLAFKKVHEAFG----- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 332 fSNLKLTNSGGTALVSATAERWKGVtGCTVVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVVGTALKVIDEQgnelPVGE 411
Cdd:cd05914 234 -GNIKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRI-RLGSAGKVIDGVEVRIDSPD----PATG 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 412 RGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILV-SGFNVYPNEIEDVVMAHPKVA 490
Cdd:cd05914 307 EGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVL 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 491 ScAAVGIPDEKSgeavKLFVVARDPSLSVEELK------AYCKENLTGY--------KIPRQIVLKDALPMTPVGKILR 555
Cdd:cd05914 387 E-SLVVVQEKKL----VALAYIDPDFLDVKALKqrniidAIKWEVRDKVnqkvpnykKISKVKIVKEEFEKTPKGKIKR 460
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
14-560 |
1.20e-57 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 201.57 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAayrsvVEVFERSCKKFADRPAF---SNLGVT--LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQY 88
Cdd:cd05970 12 VPENFNFA-----YDVVDAMAKEYPDKLALvwcDDAGEEriFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 89 PIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYlnVFGKLVEEVLPDTRIEYLIEARM---GDLLPalKGWLv 165
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVA--IAEDNIPEEIEKAAPECPSKPKLvwvGDPVP--EGWI- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 nSVVKSVKKMVPDYRLPQAlpfrqalkqgqghalqPVRVGLEDVAVLQYTGGTTGVSKgaMLTHGNLVANMLQVHAQLSQ 245
Cdd:cd05970 161 -DFRKLIKNASPDFERPTA----------------NSYPCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKDGlplmkeaqevmiaplPLYHIYAFT--ANCMCMMVSGN----HNVLITN-PRDIP-GFVKELKKWRFSALLGLNTL 317
Cdd:cd05970 222 NVREG---------------GLHLTVADTgwGKAVWGKIYGQwiagAAVFVYDyDKFDPkALLEKLSKYGVTTFCAPPTI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 318 FVALMeHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEqARLGTVGIPVVGTAL 397
Cdd:cd05970 287 YRFLI-REDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWME-PKPGSMGKPAPGYEI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 398 KVIDEQGNELPVGERGELCV---KGPQV--MKGYWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGF 472
Cdd:cd05970 365 DLIDREGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGY 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 473 NVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVV-ARD--PSLSVE-ELKAYCKENLTGYKIPRQIVLKDALPMT 548
Cdd:cd05970 444 RIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlAKGyePSEELKkELQDHVKKVTAPYKYPRIVEFVDELPKT 523
|
570
....*....|..
gi 15598496 549 PVGKILRRELRE 560
Cdd:cd05970 524 ISGKIRRVEIRE 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
212-560 |
1.36e-57 |
|
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: 199.91 E-value: 1.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 212 LQYTGGTTGVSKGAMLTH-GNLVANMLQVHAQLsqlgkdGLPLMKEaqEVMIAPLPLYHIYAFTAnCMCMMVSGNHNVLI 290
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpGGPPDNDTLMAAAL------GFGPGAD--SVYLSPAPLYHAAPFRW-SMTALFMGGTLVLM 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 291 TNpRDIPGFVKELKKWRFSALLGLNTLFVALMEHPG--FKDVDFSNLKltnsggtALVSATA-------ERWKGVTGCTV 361
Cdd:cd05929 201 EK-FDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLK-------RVIHAAApcppwvkEQWIDWGGPII 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 362 VEGYGLTECSPVVTTNpyGEQ--ARLGTVGIPVVGtALKVIDEQGNELPVGERGELCVKGPQVmKGYWQRPEATEEILDA 439
Cdd:cd05929 273 WEYYGGTEGQGLTIIN--GEEwlTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG-FEYTNDPEKTAAARNE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 440 EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFV----VARDP 515
Cdd:cd05929 349 GGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAG 428
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15598496 516 SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05929 429 TALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
51-558 |
5.05e-57 |
|
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: 197.29 E-value: 5.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKQTDLQpGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVralvyln 130
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRS-GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 vfgklvEEVLPDTrieyLIEARMGDLLPALKGWLVNSVVKSVKKMVPDyrlpqalpfrqalkqgqghalqpvrvglEDVA 210
Cdd:TIGR01923 73 ------QLLLTDS----LLEEKDFQADSLDRIEAAGRYETSLSASFNM----------------------------DQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 211 VLQYTGGTTGVSKGAMLTHGNLVANmlqVHAQLSQLGKDglplmkeAQEVMIAPLPLYHIYAFTANCMCMMVSGNhnVLI 290
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYAS---AVGSKENLGFT-------EDDNWLLSLPLYHISGLSILFRWLIEGAT--LRI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 291 TNPRDipGFVKELKKWRFSALLGLNTLFVALMEhpgfKDVDFSNLKLTNSGGTAlVSATAERWKGVTGCTVVEGYGLTE- 369
Cdd:TIGR01923 183 VDKFN--QLLEMIANERVTHISLVPTQLNRLLD----EGGHNENLRKILLGGSA-IPAPLIEEAQQYGLPIYLSYGMTEt 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 CSPVVTTNPYGEQARLGtVGIPVVGTALKVIDEQgnelpVGERGELCVKGPQVMKGYWQRPEATEeILDAEGWLKTGDIA 449
Cdd:TIGR01923 256 CSQVTTATPEMLHARPD-VGRPLAGREIKIKVDN-----KEGHGEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 450 VIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPsLSVEELKAYCKEN 529
Cdd:TIGR01923 329 ELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSESD-ISQAKLIAYLTEK 407
|
490 500
....*....|....*....|....*....
gi 15598496 530 LTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:TIGR01923 408 LAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
14-560 |
5.32e-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: 196.92 E-value: 5.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAAYrsVVEVFERSCK--KFADRPAF-----SNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVL 86
Cdd:cd05928 1 VPEYFNFASD--VLDQWADKEKagKRPPNPALwwvngKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 87 QYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTrieyliearmgdllPALKgwlvn 166
Cdd:cd05928 79 EWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASEC--------------PSLK----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 167 svvksVKKMVPDYRLPQALPFRQALKQG-QGHALqpVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqvhaqLSQ 245
Cdd:cd05928 140 -----TKLLVSEKSRDGWLNFKELLNEAsTEHHC--VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLG-------LKV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKDGLPLmkEAQEVMI-------APLPLYHIYAFTANCMCMMVsgnHNVlitnPR-DIPGFVKELKKWRFSALLGLNTL 317
Cdd:cd05928 206 NGRYWLDL--TASDIMWntsdtgwIKSAWSSLFEPWIQGACVFV---HHL----PRfDPLVILKTLSSYPITTFCGAPTV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 318 FVALMEHpGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTEcSPVVTTNPYGEQARLGTVGIPVVGTAL 397
Cdd:cd05928 277 YRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGMKIKPGSMGKASPPYDV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 398 KVIDEQGNELPVGERGELCVK-GPQ----VMKGYWQRPEATEEILDAEGWLkTGDIAVIDEDGFVRIVDRKKDLILVSGF 472
Cdd:cd05928 355 QIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGY 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 473 NVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVV------ARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALP 546
Cdd:cd05928 434 RIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapqflSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELP 513
|
570
....*....|....
gi 15598496 547 MTPVGKILRRELRE 560
Cdd:cd05928 514 KTVTGKIQRNELRD 527
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
38-558 |
6.55e-56 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 194.39 E-value: 6.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYtaremrhq 117
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASS-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 118 fkdagvralvylnvfgklveevlPDTRIEYLIEARMGDLLPAlkgwlvnsvvksvkkmVPDyrlpqalpfrqalkqgqgh 197
Cdd:cd05945 76 -----------------------PAERIREILDAAKPALLIA----------------DGD------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 alqpvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlqVHAQLSQLGkdglplMKEAQEVMIAPLPlyhiYAFTANC 277
Cdd:cd05945 98 ----------DNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDF------PLGPGDVFLNQAP----FSFDLSV 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 M---CMMVSGNhnVLITNPRDIPGFVKELkkWRFSALLGLNTL-----FVA-LMEHPGFKDVDFSNLKLTNSGGTALVSA 348
Cdd:cd05945 154 MdlyPALASGA--TLVPVPRDATADPKQL--FRFLAEHGITVWvstpsFAAmCLLSPTFTPESLPSLRHFLFCGEVLPHK 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 349 TAERWKGVT-GCTVVEGYGLTECSPVVTTN-----PYGEQARLgTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQV 422
Cdd:cd05945 230 TARALQQRFpDARIYNTYGPTEATVAVTYIevtpeVLDGYDRL-PIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSV 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 423 MKGYWQRPEATEEIL---DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPD 499
Cdd:cd05945 309 SKGYLNNPEKTAAAFfpdEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 500 EKSGEAVKLFVVARDPSLSV--EELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05945 389 GEKVTELIAFVVPKPGAEAGltKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
39-560 |
1.51e-55 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 195.75 E-value: 1.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPgDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQALPIGEP-RVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVYLNVFGKLVEEVLPD----TRIEyliearmgdllpalkGWLVNSVVKSVKKMVpdyrlpqalpfrqALKQG 194
Cdd:PRK13382 137 TREGVDTVIYDEEFSATVDRALADcpqaTRIV---------------AWTDEDHDLTVEVLI-------------AAHAG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 195 QghalQPVRVGLEDVAVLqYTGGTTGVSKGAML----THGNLVANMlqvhaqlsqlgkDGLPLMKEAQEVMIAPLplYHI 270
Cdd:PRK13382 189 Q----RPEPTGRKGRVIL-LTSGTTGTPKGARRsgpgGIGTLKAIL------------DRTPWRAEEPTVIVAPM--FHA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 271 YAFTANCMCMMVSgnhNVLITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHP--GFKDVDFSNLKLTNSGGTAL-- 345
Cdd:PRK13382 250 WGFSQLVLAASLA---CTIVTRRRfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASGSRMrp 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 --VSATAERWkgvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVM 423
Cdd:PRK13382 327 dvVIAFMDQF----GDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 424 KGYwqRPEATEEILDaeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSG 503
Cdd:PRK13382 403 DGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 504 EAVKLFVV-ARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK13382 479 QRLAAFVVlKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
207-555 |
1.78e-53 |
|
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: 188.34 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlqvhaQLSQLGkDGLPLmkEAQEVMIAPLPLYHIY-------AFTANCMC 279
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHANLLH-------QIRSLS-DIVPP--QPGDRFLSILPIWHSYersaeyfIFACGCSQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 280 MMVSgnhnvlitnprdIPGFVKELKKWRFSALLGLNTLFVALME--------HPGFKDVDFSNLKLTN------SGGTAL 345
Cdd:cd17640 158 AYTS------------IRTLKDDLKRVKPHYIVSVPRLWESLYSgiqkqvskSSPIKQFLFLFFLSGGifkfgiSGGGAL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSaTAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARlGTVGIPVVGTALKVIDEQGNE-LPVGERGELCVKGPQVMK 424
Cdd:cd17640 226 PP-HVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVR-GSVGRPLPGTEIKIVDPEGNVvLPPGEKGIVWVRGPQVMK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 GYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYPNEIEDVVMAHPKVASCAAVG------- 496
Cdd:cd17640 304 GYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVGqdqkrlg 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 497 ---IPD----EKSGEAVKLFVVA--RDPSLSVEELKAYCKENLT------GYK-----IPRQIVLKDALP---MTPVGKI 553
Cdd:cd17640 384 aliVPNfeelEKWAKESGVKLANdrSQLLASKKVLKLYKNEIKDeisnrpGFKsfeqiAPFALLEEPFIEngeMTQTMKI 463
|
..
gi 15598496 554 LR 555
Cdd:cd17640 464 KR 465
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
187-560 |
5.47e-53 |
|
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: 188.96 E-value: 5.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 187 FRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGlplmkeAQEVMIAPLP 266
Cdd:cd05927 94 LEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKIN------PTDVYISYLP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 267 LYHIYAFTANCMCMMV-------SGNHNVLITN------------PR-------DIPGFVKE---LKKWRFSALLG--LN 315
Cdd:cd05927 168 LAHIFERVVEALFLYHgakigfySGDIRLLLDDikalkptvfpgvPRvlnriydKIFNKVQAkgpLKRKLFNFALNykLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 316 TLFVALME-HPGFKDVDFS--------NLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQaRLG 386
Cdd:cd05927 248 ELRSGVVRaSPFWDKLVFNkikqalggNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDT-SVG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 387 TVGIPVVGTALKVID-EQGNELPVGE--RGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRK 463
Cdd:cd05927 327 HVGGPLPCAEVKLVDvPEMNYDAKDPnpRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRK 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 464 KDLI-LVSGFNVYPNEIEDVVMAHPKVASC-----------AAVGIPD---------EKSGEAVKLFVVARDPSLS---V 519
Cdd:cd05927 407 KNIFkLSQGEYVAPEKIENIYARSPFVAQIfvygdslksflVAIVVPDpdvlkewaaSKGGGTGSFEELCKNPEVKkaiL 486
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15598496 520 EELKAYCKEN-LTGYKIPRQIVLKDAL------PMTPVGKILRRELRE 560
Cdd:cd05927 487 EDLVRLGKENgLKGFEQVKAIHLEPEPfsvengLLTPTFKLKRPQLKK 534
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
30-559 |
7.30e-53 |
|
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: 187.55 E-value: 7.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 30 FERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLY 109
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 110 TAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGWLVnsvvksvkkmvPDYRLPQALPFRQ 189
Cdd:cd17651 80 PAERLAFMLADAGPVLV---------------------LTHPALAGELAVELVAVT-----------LLDQPGAAAGADA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 190 ALkqgqghalqPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGkdglPLMKEAQEVMIA-PLPLY 268
Cdd:cd17651 128 EP---------DPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASSLG----PGARTLQFAGLGfDVSVQ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 269 HIyaFTANCmcmmvSGNHNVLITNP--RDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALV 346
Cdd:cd17651 194 EI--FSTLC-----AGATLVLPPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 347 --SATAERWKGVTGCTVVEGYGLTEcSPVVT----TNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGP 420
Cdd:cd17651 267 ltEDLREFCAGLPGLRLHNHYGPTE-THVVTalslPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMKGYWQRPEATEEILDAEGWL------KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAA 494
Cdd:cd17651 346 GLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVV 425
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 495 VGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd17651 426 LAREDRPGEKRLVAYVVGDpEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
28-558 |
4.29e-51 |
|
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: 182.40 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALVYLNVFGKLVEEvlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrLPQALPF 187
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLTDRSLAGRAGG------------------------------------------LEVAVVI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 RQALKQGQGHALqPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlqvhaqlsqLGKDGLPLMKEAQEVMI--APL 265
Cdd:cd12117 118 DEALDAGPAGNP-AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR-----------LVKNTNYVTLGPDDRVLqtSPL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 266 plyhiyAFTANCMCM---MVSGNHNVLIT--NPRDIPGFVKELKKWRFSALLGLNTLFVALMEHpgfkDVD-FSNLKLTN 339
Cdd:cd12117 186 ------AFDASTFEIwgaLLNGARLVLAPkgTLLDPDALGALIAEEGVTVLWLTAALFNQLADE----DPEcFAGLRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 340 SGGTALVSATAERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGT---VGIPVVGTALKVIDEQGNELPVGERGEL 415
Cdd:cd12117 256 TGGEVVSPPHVRRVlAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGsipIGRPIANTRVYVLDEDGRPVPPGVPGEL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEEILDAEGWL------KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKV 489
Cdd:cd12117 336 YVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 490 ASCAAVGIPDEKSGEAVKLFVVARDPsLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd12117 416 REAVVVVREDAGGDKRLVAYVVAEGA-LDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
51-494 |
5.87e-50 |
|
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: 177.46 E-value: 5.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVyln 130
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 VFGKLVEEVLPDTRIEYLIEARMGDLLPAlkgwlvnsvvksvkkmvpdyRLPQALPfrqalkqgqghalqPVRVGLEDVA 210
Cdd:TIGR01733 78 TDSALASRLAGLVLPVILLDPLELAALDD--------------------APAPPPP--------------DAPSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 211 VLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLGKDglplmkeaqEVMIAplplYHIYAF----TANCMCMMVSGNH 286
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLV-NLLAWLARRYGLDPD---------DRVLQ----FASLSFdasvEEIFGALLAGATL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLITNP-RDIPGFVKELKKWRF-SALLGLNTLFVALMEHPGFkdvDFSNLKLTNSGGTALVSATAERWKGVTG-CTVVE 363
Cdd:TIGR01733 190 VVPPEDEeRDDAALLAALIAEHPvTVLNLTPSLLALLAAALPP---ALASLRLVILGGEALTPALVDRWRARGPgARLIN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 364 GYGLTECSPVVTTNPYG----EQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE---- 435
Cdd:TIGR01733 267 LYGPTETTVWSTATLVDpddaPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvp 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 436 ----ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAA 494
Cdd:TIGR01733 347 dpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
25-560 |
1.83e-49 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 179.31 E-value: 1.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 25 SVVEVFERSCKKFADRPA--FSNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVV 102
Cdd:PRK05852 17 RIADLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTR-SGLLPGDRVALRMGSNAEFVVALLAASRADLVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 103 VNTNPLYTAREMRHQFKDAGVRALvylnvfgkLVEEVLPDTRIEyliearmgdllPALKGWLVNSVVKSVKK-----MVP 177
Cdd:PRK05852 96 VPLDPALPIAEQRVRSQAAGARVV--------LIDADGPHDRAE-----------PTTRWWPLTVNVGGDSGpsggtLSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 178 DYRLPQALPFRQALKQGQGHalqpvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqVHAQLS--QLGKdglplmk 255
Cdd:PRK05852 157 HLDAATEPTPATSTPEGLRP----------DDAMIMFTGGTTGLPKMVPWTHANIASS---VRAIITgyRLSP------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 256 eaQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSN 334
Cdd:PRK05852 217 --RDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 335 --LKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTT----------NPygeQARLGTVGiPVVGTALKVIDE 402
Cdd:PRK05852 295 aaLRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTtqiegigqteNP---VVSTGLVG-RSTGAQIRIVGS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 403 QGNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDV 482
Cdd:PRK05852 371 DGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGV 449
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 483 VMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK05852 450 LASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
27-558 |
3.98e-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: 177.08 E-value: 3.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 27 VEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTN 106
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 107 PLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALkgwlvnsvvksvkkmvpdyrLPQALP 186
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVV---------------------LTTADLAARLPAG--------------------GDVALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 187 FRQALKQGQGHALQPVrVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDG---------------- 250
Cdd:cd17646 119 GDEALAAPPATPPLVP-PRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRvlqktplsfdvsvwel 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 251 -LPLMKEAQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKD 329
Cdd:cd17646 198 fWPLVAGARLVVARP-------------------GGH-------RDPAYLAALIREHGVTTCHFVPSMLRVFLAEPAAGS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 330 VDfsNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGI--PVVGTALKVIDEQGNEL 407
Cdd:cd17646 252 CA--SLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIgrPVPNTRLYVLDDALRPV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 408 PVGERGELCVKGPQVMKGYWQRPEATEEI-----LDAEGWL-KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:cd17646 330 PVGVPGELYLGGVQLARGYLGRPALTAERfvpdpFGPGSRMyRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEA 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 482 VVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD--PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17646 410 ALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-562 |
1.87e-48 |
|
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: 174.23 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLYTAremrhqfkdagvralvyl 129
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSA------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 nvFGklvEEVLPDtRIEyLIEARMGDLLPALKgwlvnsvvksvKKMVPdyrlpqalpfrqalkqgqghalqpvrvglEDV 209
Cdd:cd05969 59 --FG---PEAIRD-RLE-NSEAKVLITTEELY-----------ERTDP-----------------------------EDP 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVANMLQvhaqlsqlGKDGLPLMKE------AQEVMIAPLpLYHIYAFTANCMCMMVS 283
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFT--------GKYVLDLHPDdiywctADPGWVTGT-VYGIWAPWLNGVTNVVY 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 284 GNHnvliTNPRDIPGFVKELK--KWRF--SALLGLNTLFVALMEHpgfkdVDFSNLKLTNSGGTALvSATAERW-KGVTG 358
Cdd:cd05969 163 EGR----FDAESWYGIIERVKvtVWYTapTAIRMLMKEGDELARK-----YDLSSLRFIHSVGEPL-NPEAIRWgMEVFG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 359 CTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKG--PQVMKGYWQRPEATEEI 436
Cdd:cd05969 233 VPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNS 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 437 LdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR--- 513
Cdd:cd05969 313 F-IDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKegf 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15598496 514 DPSLSV-EELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:cd05969 392 EPSDELkEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
39-558 |
3.44e-48 |
|
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: 174.02 E-value: 3.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALvylnvfgkLVEEVLPDTRIEYLieARMGDLLPALKGwlvnsvvksvkkmVPDYRLPQALPfrqalkqgqgha 198
Cdd:cd12116 81 EDAEPALV--------LTDDALPDRLPAGL--PVLLLALAAAAA-------------APAAPRTPVSP------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLGKDG------------------LPLMKEAQeV 260
Cdd:cd12116 126 --------DDLAYVIYTSGSTGRPKGVVVSHRNLV-NFLHSMRERLGLGPGDrllavttyafdisllellLPLLAGAR-V 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 MIAPLPLYHiyafTANCMCMMVSgNHNvlITNPRDIPGFVKELKKWRFSALLGLNTLfvalmehpgfkdvdfsnlkltnS 340
Cdd:cd12116 196 VIAPRETQR----DPEALARLIE-AHS--ITVMQATPATWRMLLDAGWQGRAGLTAL----------------------C 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 341 GGTALVSATAERWKGvTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGP 420
Cdd:cd12116 247 GGEALPPDLAARLLS-RVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMKGYWQRPEATEEIL-------DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCA 493
Cdd:cd12116 326 GVAQGYLGRPALTAERFvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 494 AVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd12116 406 VVVREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
8-561 |
7.79e-48 |
|
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: 174.78 E-value: 7.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 8 DKRPAGVPDSLDFAAYRSVvevfERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQ 87
Cdd:cd05906 2 LHRPEGAPRTLLELLLRAA----ERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 88 YPIAVFGALRAGLVVVNTNPLYTAREMRHQfkdagVRALvylnvfgKLVEEVLPDTRIeyLIEARMgdlLPALKGWLVNS 167
Cdd:cd05906 77 FIPAFWACVLAGFVPAPLTVPPTYDEPNAR-----LRKL-------RHIWQLLGSPVV--LTDAEL---VAEFAGLETLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 168 VVKSVKKMVPDYRlpqalpfRQALKQGQGHALQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVAnMLQVHAQLSQLG 247
Cdd:cd05906 140 GLPGIRVLSIEEL-------LDTAADHDLPQSRP-----DDLALLMLTSGSTGFPKAVPLTHRNILA-RSAGKIQHNGLT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 248 kdglplmkeAQEVMIAPLPL--------YHIYAFTANCMCMMVSGNHnvLITNPRDipgFVKELKKWRFSALLGLN---T 316
Cdd:cd05906 207 ---------PQDVFLNWVPLdhvgglveLHLRAVYLGCQQVHVPTEE--ILADPLR---WLDLIDRYRVTITWAPNfafA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 LFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERW------KGVTGCTVVEGYGLTE-CSPVV-----TTNPYGEQAR 384
Cdd:cd05906 273 LLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLlrllepYGLPPDAIRPAFGMTEtCSGVIysrsfPTYDHSQALE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 385 LGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDeDGFVRIVDRKK 464
Cdd:cd05906 353 FVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTITGRTK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 465 DLILVSGFNVYPNEIEDVVMAHPKVAS--CAAVGIPDEKSG--EAVKLFVVARDPSLS-VEELKAYCKE--NLTGYKIPR 537
Cdd:cd05906 432 DTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAEteELAIFFVPEYDLQDAlSETLRAIRSVvsREVGVSPAY 511
|
570 580
....*....|....*....|....*
gi 15598496 538 QIVL-KDALPMTPVGKILRRELREI 561
Cdd:cd05906 512 LIPLpKEEIPKTSLGKIQRSKLKAA 536
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
6-560 |
1.57e-47 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 178.90 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDkrpagvpDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNV 85
Cdd:COG1020 465 WNA-------TAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERS 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVntnPLytaremrhqfkDAGvralvylnvfgklveevLPDTRIEYLIE-ARMGDLL--PALKG 162
Cdd:COG1020 537 LEMVVALLAVLKAGAAYV---PL-----------DPA-----------------YPAERLAYMLEdAGARLVLtqSALAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 163 WLvnsvvksvkkmvPDYRLPQaLPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQ 242
Cdd:COG1020 586 RL------------PELGVPV-LALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV-NLLAWMQR 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 243 LSQLGkdglplmkeAQEVMiaplPLYHIYAF---TANCMCMMVSGNHNVLITN--PRDIPGFVKELKKWRFSALLGLNTL 317
Cdd:COG1020 652 RYGLG---------PGDRV----LQFASLSFdasVWEIFGALLSGATLVLAPPeaRRDPAALAELLARHRVTVLNLTPSL 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 318 FVALMEHPGFkdvDFSNLKLTNSGGTALVSATAERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLG---TVGIPVV 393
Cdd:COG1020 719 LRALLDAAPE---ALPSLRLVLVGGEALPPELVRRWrARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIA 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 394 GTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE--ILDAEG-----WLKTGDIAVIDEDGFVRIVDRKKDL 466
Cdd:COG1020 796 NTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfVADPFGfpgarLYRTGDLARWLPDGNLEFLGRADDQ 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 467 ILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYC-KENLTGYKIPRQIVLKDAL 545
Cdd:COG1020 876 VKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPL 955
|
570
....*....|....*
gi 15598496 546 PMTPVGKILRRELRE 560
Cdd:COG1020 956 PLTGNGKLDRLALPA 970
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
207-558 |
3.72e-47 |
|
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: 172.01 E-value: 3.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhaqlsqlgKDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMvsgnH 286
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGL--------GDRVPELLGPDDRYLAYLPLAHIFELAAENVCLY----R 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLI--TNPRDIP--------GFVKELKKWRFSA------------LLGLN-------TLF-------VALMEH----PG 326
Cdd:cd17639 156 GGTIgyGSPRTLTdkskrgckGDLTEFKPTLMVGvpaiwdtirkgvLAKLNpmgglkrTLFwtayqskLKALKEgpgtPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 327 FKDVDFS--------NLKLTNSGGTALvSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVVGTALK 398
Cdd:cd17639 236 LDELVFKkvraalggRLRYMLSGGAPL-SADTQEFLNIVLCPVIQGYGLTETCAGGTVQDPGDL-ETGRVGPPLPCCEIK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 399 VID-EQGNELPVGE--RGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLI-------- 467
Cdd:cd17639 314 LVDwEEGGYSTDKPppRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVklqngeyi 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 468 ----LVSGF--NVYPNEIedVVMAHPKVASCAAVGIPDEKSGE--AVKLFVV-ARDPSL--SVEELKAYCKE-------- 528
Cdd:cd17639 394 alekLESIYrsNPLVNNI--CVYADPDKSYPVAIVVPNEKHLTklAEKHGVInSEWEELceDKKLQKAVLKSlaetaraa 471
|
410 420 430
....*....|....*....|....*....|....*.
gi 15598496 529 NLTGYKIPRQIVLKDAL--P----MTPVGKILRREL 558
Cdd:cd17639 472 GLEKFEIPQGVVLLDEEwtPenglVTAAQKLKRKEI 507
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
214-551 |
8.02e-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: 166.71 E-value: 8.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 214 YTGGTTGVSKGAMLTHGNLVANMLqVHAQLSQLgkdglplmkEAQEVMIAPLPLYHIyAFTANCMCMMVSGNHNVLI--T 291
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQAL-VLAVLQAI---------DEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVrrV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 292 NPRDIPGFVkELKKWRfSALLGLNTLfVALMEHPGFKDVDFSNLKLTNS--GGTALVSATAERWkgvtgCTVVEGYGLTE 369
Cdd:cd17636 76 DAEEVLELI-EAERCT-HAFLLPPTI-DQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPW-----GRKPGGYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 CSPVVTTNPYGEQArLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIA 449
Cdd:cd17636 148 VMGLATFAALGGGA-IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 450 VIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKE 528
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVTEAELIEHCRA 305
|
330 340
....*....|....*....|...
gi 15598496 529 NLTGYKIPRQIVLKDALPMTPVG 551
Cdd:cd17636 306 RIASYKKPKSVEFADALPRTAGG 328
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
38-559 |
1.43e-46 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 171.62 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAF----SNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVvntNPLYTA-- 111
Cdd:PRK04319 58 KDKVALryldASRKEKYTYKELKELSNKFANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEAfm 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 112 -REMRHQFKDAGVRALVylnvfgklveevlpdtRIEYLIEARMGDLLPALKGWLVnsvVKSVKKMVPDYrlpqaLPFRQA 190
Cdd:PRK04319 134 eEAVRDRLEDSEAKVLI----------------TTPALLERKPADDLPSLKHVLL---VGEDVEEGPGT-----LDFNAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 191 LKQGqGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNlvanMLQVHaqlsQLGKDGLPLmkEAQEV---------- 260
Cdd:PRK04319 190 MEQA-SDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA----MLQHY----QTGKYVLDL--HEDDVywctadpgwv 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 ------MIAPLplyhiyaftancmcmmVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPG--FKDVDF 332
Cdd:PRK04319 259 tgtsygIFAPW----------------LNGATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGDdlVKKYDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 333 SNLKLTNSGGTALvSATAERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGE 411
Cdd:PRK04319 323 SSLRHILSVGEPL-NPEVVRWgMKVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 412 RGELCVKG--PQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKV 489
Cdd:PRK04319 402 MGNLAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 490 ASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELK----AYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK04319 481 AEAGVIGKPDPVRGEIIKAFVALRPGYEPSEELKeeirGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
28-562 |
1.58e-46 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 170.94 E-value: 1.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKkfADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTnp 107
Cdd:PRK10946 29 DILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNA-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTaremrHQFKDagvralvyLNVFGKLVEEVLpdtrieyLIEARMGDLLPAlkgwlvNSVVKSVKKMVPDYRL------ 181
Cdd:PRK10946 104 LFS-----HQRSE--------LNAYASQIEPAL-------LIADRQHALFSD------DDFLNTLVAEHSSLRVvlllnd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 182 PQALPFRQALKQGQGHaLQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHgNLVANMLQVHAQLSQLGkdglplmkeAQEVM 261
Cdd:PRK10946 158 DGEHSLDDAINHPAED-FTATPSPADEVAFFQLSGGSTGTPKLIPRTH-NDYYYSVRRSVEICGFT---------PQTRY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 262 IAPLPLYHIYAFTA-NCMCMMVSGNHNVLITNPRDIPGF-VKELKKWRFSALL-GLNTLFVALMEHPGFKDvDFSNLKLT 338
Cdd:PRK10946 227 LCALPAAHNYPMSSpGALGVFLAGGTVVLAPDPSATLCFpLIEKHQVNVTALVpPAVSLWLQAIAEGGSRA-QLASLKLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 339 NSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGT-ALKVIDEQGNELPVGERGELCV 417
Cdd:PRK10946 306 QVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSPDdEVWVADADGNPLPQGEVGRLMT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 418 KGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI 497
Cdd:PRK10946 386 RGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 498 PDEKSGEAVKLFVVARDPsLSVEELKAYCKE-NLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK10946 466 EDELMGEKSCAFLVVKEP-LKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWL 530
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
49-554 |
1.77e-46 |
|
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: 171.99 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVy 128
Cdd:cd17634 84 TISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 lnvfgklveevlpdTRIEYLIEARMGDLLP------ALKGWLVNSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPV 202
Cdd:cd17634 162 --------------TADGGVRAGRSVPLKKnvddalNPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 203 RVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGL-------------------PLMKEAQEVMIA 263
Cdd:cd17634 228 AMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIywctadvgwvtghsyllygPLACGATTLLYE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 264 PLPLYHiyafTANCMCMMVSgNH--NVLITNPRDIPGFVKELKKWrfsallglntlfvalmehpgFKDVDFSNLKLTNSG 341
Cdd:cd17634 308 GVPNWP----TPARMWQVVD-KHgvNILYTAPTAIRALMAAGDDA--------------------IEGTDRSSLRILGSV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 342 GTALvSATAERWK----GVTGCTVVEGYGLTECSPVVTTN-PYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELC 416
Cdd:cd17634 363 GEPI-NPEAYEWYwkkiGKEKCPVVDTWWQTETGGFMITPlPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 417 VKG--PQVMKGYWQRPEATEEILDA--EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASC 492
Cdd:cd17634 442 ITDpwPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 493 AAVGIPDEKSGEAVKLFVVAR----DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKIL 554
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
39-559 |
4.50e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 169.03 E-value: 4.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAF--SNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRH 116
Cdd:PRK13390 12 DRPAVivAETGEQVSYRQLDDDSAALARVLY-DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 117 QFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARM---GDLLPALKGwlvnsvvksvkkmvpdyrlpqalpfrqalkQ 193
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIdgfGSFEAALAG------------------------------A 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 194 GQGHALQPVRvgledvAVLQYTGGTTGVSKGamlthgnlvanmLQVHAQLSQLGKDGLPLMKEAQ--------EVMIAPL 265
Cdd:PRK13390 141 GPRLTEQPCG------AVMLYSSGTTGFPKG------------IQPDLPGRDVDAPGDPIVAIARafydisesDIYYSSA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 266 PLYHIYAFTANCMCMMVSGNhnVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGfkDV----DFSNLKltnsg 341
Cdd:PRK13390 203 PIYHAAPLRWCSMVHALGGT--VVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLKLDA--DVrtryDVSSLR----- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 342 gtALVSATAE----------RWkgvTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTaLKVIDEQGNELPVGE 411
Cdd:PRK13390 274 --AVIHAAAPcpvdvkhamiDW---LGPIVYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGR 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 412 RGELCVKGPQVMKGYWQRPEATEEILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKV 489
Cdd:PRK13390 348 IGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAV 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 490 ASCAAVGIPDEKSGEAVKL---FVVARDPSLSV-EELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK13390 428 HDVAVIGVPDPEMGEQVKAviqLVEGIRGSDELaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
38-562 |
1.00e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 168.77 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAFSNL---GVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREM 114
Cdd:PRK06164 21 RARPDAVALideDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 115 RHQFKDAGVRALVYLNVFGKL-----VEEVLPDtrieyliearmgdLLPALKGWLVnsvvksVKKMVPDyrLPQALPFRQ 189
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGIdfaaiLAAVPPD-------------ALPPLRAIAV------VDDAADA--TPAPAPGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 190 ----ALKQGQGHALQPVRVGLEDVAVLQYT-GGTTGVSKGAMLTHGNLVANMLQVHAQLSQlgkdglplmkEAQEVMIAP 264
Cdd:PRK06164 159 vqlfALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGY----------DPGAVLLAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 265 LPLYHIYAFtaNCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGfKDVDFSNLKLTnsGGTA 344
Cdd:PRK06164 229 LPFCGVFGF--STLLGALAGGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAG-ERADFPSARLF--GFAS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 LVSATAE--RWKGVTGCTVVEGYGLTECSPVVTTNPYG--EQARLGTVGIPVVGTA-LKVIDEQGNE-LPVGERGELCVK 418
Cdd:PRK06164 304 FAPALGElaALARARGVPLTGLYGSSEVQALVALQPATdpVSVRIEGGGRPASPEArVRARDPQDGAlLPDGESGEIEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 419 GPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIP 498
Cdd:PRK06164 384 APSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 499 DEKSGEAVKlFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVG---KILRRELREIA 562
Cdd:PRK06164 464 RDGKTVPVA-FVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMA 530
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
72-560 |
2.29e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 167.96 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 72 LQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDtrieyliea 151
Cdd:PRK07008 61 VEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDLTFLPLVDALAPQ--------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 152 rmgdlLPALKGWLVnsvvksvkkMVPDYRLP-QALPFR--QALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLT 228
Cdd:PRK07008 132 -----CPNVKGWVA---------MTDAAHLPaGSTPLLcyETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 229 HGNLVanmlqVHAQLSQLgKDGLPLmkEAQEVMIAPLPLYHIYAFTANCMCMMVSGNhnvLITNPRDIPG-FVKEL---K 304
Cdd:PRK07008 198 HRSTV-----LHAYGAAL-PDAMGL--SARDAVLPVVPMFHVNAWGLPYSAPLTGAK---LVLPGPDLDGkSLYELieaE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 305 KWRFSAllGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTN------- 377
Cdd:PRK07008 267 RVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCklkwkhs 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 378 --PYGEQ-ARLGTVGIPVVGTALKVIDEQGNELPVGER--GELCVKGPQVMKGYWQRpEATEEIldaEGWLKTGDIAVID 452
Cdd:PRK07008 345 qlPLDEQrKLLEKQGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYFRG-DASPLV---DGWFPTGDVATID 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 453 EDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAvKLFVVARDPSLSV--EELKAYCKENL 530
Cdd:PRK07008 421 ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDER-PLLVVVKRPGAEVtrEELLAFYEGKV 499
|
490 500 510
....*....|....*....|....*....|
gi 15598496 531 TGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07008 500 AKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
208-562 |
3.43e-45 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 162.12 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglplmkeaqeVMIAPLPLYHI--YAFTANCMcmmVSGN 285
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD----------SWLLSLPLYHVggLAILVRSL---LAGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 286 HNVLITNPRDipgFVKELKKWRFSALLGLNTLFVALMEHPGFKDvDFSNLKLTNSGGTALVSATAERW--KGVTGCTvve 363
Cdd:cd17630 68 ELVLLERNQA---LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAadRGIPLYT--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 364 GYGLTECSPVVTTNPYGEQARlGTVGIPVVGTALKVIDeqgnelpvgeRGELCVKGPQVMKGYWQRPEatEEILDAEGWL 443
Cdd:cd17630 141 TYGMTETASQVATKRPDGFGR-GGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL--VPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 444 KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPsLSVEELK 523
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP-ADPAELR 286
|
330 340 350
....*....|....*....|....*....|....*....
gi 15598496 524 AYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
207-559 |
6.88e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 166.90 E-value: 6.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLqvhAQLSQLGKDglplmkeAQEVMIAPLPLYHIYAFTAnCMCMMVSGNH 286
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSL---AKIAIVGYG-------EDDVYLHTAPLCHIGGLSS-ALAMLMVGAC 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLItnprdiPGF-----VKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSN---LKLTNSGGTALVSATAERWKGVTG 358
Cdd:PLN02860 241 HVLL------PKFdakaaLQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFpsvRKILNGGGSLSSRLLPDAKKLFPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 359 CTVVEGYGLTE-CS--------------PVVTTNPYGEQARLGT-------VGIPVVGTALKV-IDEQGNElpvgerGEL 415
Cdd:PLN02860 315 AKLFSAYGMTEaCSsltfmtlhdptlesPKQTLQTVNQTKSSSVhqpqgvcVGKPAPHVELKIgLDESSRV------GRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:PLN02860 389 LTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 496 GIPDEKSGEAVKLFVVARDP---------------SLSVEELKAYCKE-NLTGYKIPRQIVL-KDALPMTPVGKILRREL 558
Cdd:PLN02860 469 GVPDSRLTEMVVACVRLRDGwiwsdnekenakknlTLSSETLRHHCREkNLSRFKIPKLFVQwRKPFPLTTTGKIRRDEV 548
|
.
gi 15598496 559 R 559
Cdd:PLN02860 549 R 549
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
214-555 |
1.22e-44 |
|
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: 160.65 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 214 YTGGTTGVSKGAMLTHGNLVANMlqvhaqlsQLGKDGLPLMKEaqEVMIAPLPLYHIYAFTAnCMCMMVSGNhNVLITNP 293
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESF--------VCNEDLFNISGE--DAILAPGPLSHSLFLYG-AISALYLGG-TFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 294 RDIPGFVKELKKWRFSALLGLNTLFVALMEHpgfkDVDFSNLKLTNSGGTALVSATAERWK-GVTGCTVVEGYGLTECSp 372
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALART----LEPESKIKSIFSSGQKLFESTKKKLKnIFPKANLIEFYGTSELS- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 373 VVTTNPYGEQARLGTVGIPVVGTALKVIDEQGnelpvGERGELCVKGPQVMKGYwqrpeATEEILDAEGWLKTGDIAVID 452
Cdd:cd17633 150 FITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGY-----VRGGFSNPDGWMSVGDIGYVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 453 EDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVkLFVVARDpSLSVEELKAYCKENLTG 532
Cdd:cd17633 220 EEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGD-KLTYKQLKRFLKQKLSR 297
|
330 340
....*....|....*....|...
gi 15598496 533 YKIPRQIVLKDALPMTPVGKILR 555
Cdd:cd17633 298 YEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
51-560 |
8.65e-44 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 163.38 E-value: 8.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLN 130
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 VFGKLVEEVLpdtrieyliearmgDLLPALKGWlvnsVVKSVKKMVPDYRLPQALPFRQALKQGQGHalqpVRVGLED-- 208
Cdd:PRK06018 120 TFVPILEKIA--------------DKLPSVERY----VVLTDAAHMPQTTLKNAVAYEEWIAEADGD----FAWKTFDen 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 -VAVLQYTGGTTGVSKGAMLTHGnlvANMLqvHAqLSQLGKDGLPLmkEAQEVMIAPLPLYHI----YAFTANCMcmmvs 283
Cdd:PRK06018 178 tAAGMCYTSGTTGDPKGVLYSHR---SNVL--HA-LMANNGDALGT--SAADTMLPVVPLFHAnswgIAFSAPSM----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 284 gNHNVLITNPRDIPGFVKEL---KKWRFSAllGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVtGCT 360
Cdd:PRK06018 245 -GTKLVMPGAKLDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 361 VVEGYGLTECSPVVT----TNPYGE---QARLG---TVGIPVVGTALKVIDEQGNELPVGER--GELCVKGPQVMKGYWQ 428
Cdd:PRK06018 321 VRHAWGMTEMSPLGTlaalKPPFSKlpgDARLDvlqKQGYPPFGVEMKITDDAGKELPWDGKtfGRLKVRGPAVAAAYYR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 429 rpeATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKL 508
Cdd:PRK06018 401 ---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15598496 509 FVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK06018 478 IVQLKpGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
8-562 |
5.43e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 161.27 E-value: 5.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 8 DKRPAG-VPDS-LDFaayrsvvevFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNV 85
Cdd:PRK08162 9 DRNAANyVPLTpLSF---------LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALA-RRGIGRGDTVAVLLPNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLpdtrieylieARMGDLLPAlkgwlv 165
Cdd:PRK08162 79 PAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREAL----------ALLPGPKPL------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 nsVVKSVKKMVPDYRLPQALPFRQALKQGQ-GHALQPVRVGLEDVAvLQYTGGTTGVSKGAMLTH--------GNLVANM 236
Cdd:PRK08162 143 --VIDVDDPEYPGGRFIGALDYEAFLASGDpDFAWTLPADEWDAIA-LNYTSGTTGNPKGVVYHHrgaylnalSNILAWG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 237 LQVHAqlsqlgkdglplmkeaqeVMIAPLPLYHiyaftANCMC----MMVSGNHNVLITnprdipgfvkelkkwRFSAll 312
Cdd:PRK08162 220 MPKHP------------------VYLWTLPMFH-----CNGWCfpwtVAARAGTNVCLR---------------KVDP-- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 313 glNTLFVALMEHpgfkdvdfsnlKLTNSGG-----TALVSATAErWKG-----VTGCT--------VVEG---------- 364
Cdd:PRK08162 260 --KLIFDLIREH-----------GVTHYCGapivlSALINAPAE-WRAgidhpVHAMVagaappaaVIAKmeeigfdlth 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 -YGLTECSPVVTTN---------PYGEQARL-GTVGIP-VVGTALKVID-EQGNELPV-GER-GELCVKGPQVMKGYWQR 429
Cdd:PRK08162 326 vYGLTETYGPATVCawqpewdalPLDERAQLkARQGVRyPLQEGVTVLDpDTMQPVPAdGETiGEIMFRGNIVMKGYLKN 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 430 PEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLF 509
Cdd:PRK08162 406 PKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAF 484
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 15598496 510 VVARD-PSLSVEELKAYCKENLTGYKIPRQIVLkDALPMTPVGKILRRELREIA 562
Cdd:PRK08162 485 VELKDgASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQA 537
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
28-560 |
5.77e-43 |
|
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: 159.01 E-value: 5.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTdLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnP 107
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLG-VVPGDVVPLLSDRSLEMLVAILAILKAGAAYV---P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LytaremrhqfkDAGvralvylnvfgklveevLPDTRIEYLIEARMGDLLpalkgwlvnsvvksvkkmvpdyrLPQALPf 187
Cdd:cd17653 77 L-----------DAK-----------------LPSARIQAILRTSGATLL-----------------------LTTDSP- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rqalkqgqghalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQL-SQLGKDGLPLMKEAQEVMIAPLp 266
Cdd:cd17653 105 -------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLdVGPGSRVAQVLSIAFDACIGEI- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 267 lyhiyaftANCMCmmvSGNHNVLITNPRDIPGFVKELKkwrfsallglntlfvALMEHPGF----KDVDFSNLKLTNSGG 342
Cdd:cd17653 165 --------FSTLC---NGGTLVLADPSDPFAHVARTVD---------------ALMSTPSIlstlSPQDFPNLKTIFLGG 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 343 TALVSATAERWKGvtGCTVVEGYGLTECSPVVTTnpygEQARLG---TVGIPVVGTALKVIDEQGNELPVGERGELCVKG 419
Cdd:cd17653 219 EAVPPSLLDRWSP--GRRLYNAYGPTECTISSTM----TELLPGqpvTIGKPIPNSTCYILDADLQPVPEGVVGEICISG 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 420 PQVMKGYWQRPEATEE----ILDAEGWL--KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCA 493
Cdd:cd17653 293 VQVARGYLGNPALTASkfvpDPFWPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQA 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 494 AVGIpdekSGEAVKLFVVardP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd17653 373 AAIV----VNGRLVAFVT---PeTVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
49-562 |
8.63e-42 |
|
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: 159.02 E-value: 8.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLV--VVNTNplYTAREMRHQFKDAGVRAL 126
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGG--FAAKELASRIDDAKPKLI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 VYLNvFGklveeVLPDTRIEYLiearmgdllPALKGWLVNSVVKSVKKMVpdYRLPQA----------LPFRQALKQGQG 196
Cdd:cd05967 159 VTAS-CG-----IEPGKVVPYK---------PLLDKALELSGHKPHHVLV--LNRPQVpadltkpgrdLDWSELLAKAEP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 197 HAlqPVRVGLEDVAVLQYTGGTTGVSKGAML-THGNLVAnmlqVHAQLSQL--GKDG--------------------LPL 253
Cdd:cd05967 222 VD--CVPVAATDPLYILYTSGTTGKPKGVVRdNGGHAVA----LNWSMRNIygIKPGdvwwaasdvgwvvghsyivyGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 254 MKEAQEVMIAPLPLYHiyaftancmcmmvsgnhnvlitnPrDIPGFVKELKKWRFSALLGLNTLFVALMEHP----GFKD 329
Cdd:cd05967 296 LHGATTVLYEGKPVGT-----------------------P-DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkYIKK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 330 VDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQA---RLGTVGIPVVGTALKVIDEQGNE 406
Cdd:cd05967 352 YDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPlpiKAGSPGKPVPGYQVQVLDEDGEP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 407 LPVGERGELCVKGP---QVMKGYWQRPEATEEILDAE--GWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:cd05967 432 VGPNELGNIVIKLPlppGCLLTLWKNDERFKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEE 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 482 VVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-----DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRR 556
Cdd:cd05967 512 SVLSHPAVAECAVVGVRDELKGQVPLGLVVLKegvkiTAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRR 591
|
....*.
gi 15598496 557 ELREIA 562
Cdd:cd05967 592 TLRKIA 597
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-562 |
4.76e-41 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 159.36 E-value: 4.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 46 LGVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRA 125
Cdd:PRK06814 655 VNGPLTYRKLLTGAFVLGRKLKKNT--PPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKT 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 126 LVYLNVF------GKLVEEVLPDTRIEYLIEARMG-DLLPALKGWLvnsvvksvkkmvpDYRLPQ-ALPFRQAlkqgqgh 197
Cdd:PRK06814 733 VLTSRAFiekarlGPLIEALEFGIRIIYLEDVRAQiGLADKIKGLL-------------AGRFPLvYFCNRDP------- 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 alqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlgkdglPLmkEAQEVMIAPLPLYHIYAFTANC 277
Cdd:PRK06814 793 ---------DDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI--------DF--SPEDKVFNALPVFHSFGLTGGL 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 MCMMVSGNHNVLITNP---RDIPGFVKELKKwrfSALLGLNTLFV--ALMEHPgfkdVDFSNLKLTNSGGTALVSATAER 352
Cdd:PRK06814 854 VLPLLSGVKVFLYPSPlhyRIIPELIYDTNA---TILFGTDTFLNgyARYAHP----YDFRSLRYVFAGAEKVKEETRQT 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 353 WKGVTGCTVVEGYGLTECSPVVTTN-PYgeQARLGTVGipvvgTALKVIDEQGNELP-VGERGELCVKGPQVMKGYW--Q 428
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETAPVIALNtPM--HNKAGTVG-----RLLPGIEYRLEPVPgIDEGGRLFVRGPNVMLGYLraE 999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 429 RPEATEEIldAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKL 508
Cdd:PRK06814 1000 NPGVLEPP--ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIIL 1077
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 509 FVVARDpsLSVEELKAYCKEN-LTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK06814 1078 LTTASD--ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYVAVTKLA 1130
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-559 |
2.27e-40 |
|
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: 151.90 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLYTA---REMRHQFKDAGVRAL 126
Cdd:cd05973 1 LTFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTAfgpKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 VylnvfgklveevlpdtrieyliearmgdllpalkgwlVNSvvksvkkmvpdyrlpqalpfrqalkqGQGHALQpvrvgl 206
Cdd:cd05973 77 V-------------------------------------TDA--------------------------ANRHKLD------ 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGamlthgnlVANMLQVHAQLSQLGKDGLPLMKEAQEVMIA-PLPLYHIYAFTANCMCMmvsGN 285
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKG--------VPVPLRALAAFGAYLRDAVDLRPEDSFWNAAdPGWAYGLYYAITGPLAL---GH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 286 HNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFS-NLKLTNSGGTALvsaTAE--RWKGVT-GCTV 361
Cdd:cd05973 157 PTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPL---TPEviRWFDAAlGVPI 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 362 VEGYGLTECSPVVTtNPYG--EQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCV---KGPQV-MKGYWQRPEATEe 435
Cdd:cd05973 234 HDHYGQTELGMVLA-NHHAleHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTPAI- 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 436 ildAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD- 514
Cdd:cd05973 312 ---DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGg 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598496 515 ----PSLSvEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05973 389 hegtPALA-DELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
26-562 |
3.51e-40 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 152.31 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 26 VVEVFERSCKKFADRPA-FSNLGvTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVn 104
Cdd:cd05918 1 VHDLIEERARSQPDAPAvCAWDG-SLTYAELDRLSSRLAHHLRSL-GVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 105 tnPLytaremrhqfkDAGvralvylnvfgklveevLPDTRIEYLIEArmgdllpalkgwlVNSVVksvkkmvpdyrlpqa 184
Cdd:cd05918 78 --PL-----------DPS-----------------HPLQRLQEILQD-------------TGAKV--------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 185 lpfrqALkqgqghALQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQvHAQLSQLGKDGLPLmkeaqevmiap 264
Cdd:cd05918 100 -----VL------TSSP-----SDAAYVIFTSGSTGKPKGVVIEHRALSTSALA-HGRALGLTSESRVL----------- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 265 lpLYHIYAFTA---NCMCMMVSG----------NHNvlitnprDIPGFVKELKkwrfsallgLNTLF----VALMEHPGf 327
Cdd:cd05918 152 --QFASYTFDVsilEIFTTLAAGgclcipseedRLN-------DLAGFINRLR---------VTWAFltpsVARLLDPE- 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 328 kdvDFSNLKLTNSGGTALVSATAERWKGvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALkVIDEQGNE- 406
Cdd:cd05918 213 ---DVPSLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCW-VVDPDNHDr 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 407 -LPVGERGELCVKGPQVMKGYWQRPEATEEI-LDAEGWL------------KTGDIAVIDEDGFVRIVDRKKDLILVSGF 472
Cdd:cd05918 287 lVPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQ 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 473 NVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKL---FVVARDPSLS------------------VEELKAYCKENLT 531
Cdd:cd05918 367 RVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlvaFVVLDGSSSGsgdgdslflepsdefralVAELRSKLRQRLP 446
|
570 580 590
....*....|....*....|....*....|.
gi 15598496 532 GYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:cd05918 447 SYMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
26-561 |
7.26e-40 |
|
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: 153.41 E-value: 7.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 26 VVEVFERSCKKFADRPAFSNLG-----VTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGL 100
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 101 VVVNTNPLYTAREMRHQFKDAGVRALVYLNVF---GKLVE---------EVLPDTRiEYLIEARMGDLLPALKGwlvnsv 168
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFtrrGREVNlkeeadkacAQCPTVE-KVVVVRHLGNDFTPAKG------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 169 vksvkkmvpDYRLPQalpfrqalKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGK 248
Cdd:cd05968 215 ---------RDLSYD--------EEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 249 DGLPLMKEAQEVMIAPLPLYHiyAFTANCMCMMVSGnhnvlitnprdIPGFVKELKKWRFSA-----LLGLN-TLFVALM 322
Cdd:cd05968 278 GDLLTWFTDLGWMMGPWLIFG--GLILGATMVLYDG-----------APDHPKADRLWRMVEdheitHLGLSpTLIRALK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 323 EHpGFKDV---DFSNLKLTNSGGTALvsaTAERWK------GVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVV 393
Cdd:cd05968 345 PR-GDAPVnahDLSSLRVLGSTGEPW---NPEPWNwlfetvGKGRNPIINYSGGTEISGGILGNVLIKPIKPSSFNGPVP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 394 GTALKVIDEQGNELPvGERGELCVKGPQV--MKGYWQRPEateEILDA-----EGWLKTGDIAVIDEDGFVRIVDRKKDL 466
Cdd:cd05968 421 GMKADVLDESGKPAR-PEVGELVLLAPWPgmTRGFWRDED---RYLETywsrfDNVWVHGDFAYYDEEGYFYILGRSDDT 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 467 ILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-----PSLSvEELKAYCKENLTGYKIPRQIVL 541
Cdd:cd05968 497 INVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtptEALA-EELMERVADELGKPLSPERILF 575
|
570 580
....*....|....*....|
gi 15598496 542 KDALPMTPVGKILRRELREI 561
Cdd:cd05968 576 VKDLPKTRNAKVMRRVIRAA 595
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
28-560 |
1.16e-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: 150.94 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTL-REKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALVylnVFGKLVEEVLPDTRIEYLIEarmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpf 187
Cdd:cd17655 80 DYPEERIQYILEDSGADILL---TQSHLQPPIAFIGLIDLLDE------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rQALKQGQGHALQPVrVGLEDVAVLQYTGGTTGVSKGAMLTHGNLV-----ANMLQVHAQLSQLgkdglplmkeaqevmi 262
Cdd:cd17655 120 -DTIYHEESENLEPV-SKSDDLAYVIYTSGSTGKPKGVMIEHRGVVnlvewANKVIYQGEHLRV---------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 263 aplPLYHIYAFTANCMCM---MVSGNHNVLITNPRDIPG--FVKELKKWRFSALLGLNTLFVALMEHpgfKDVDFSNLKL 337
Cdd:cd17655 182 ---ALFASISFDASVTEIfasLLSGNTLYIVRKETVLDGqaLTQYIRQNRITIIDLTPAHLKLLDAA---DDSEGLSLKH 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 338 TNSGGTALVSATAERWKGV--TGCTVVEGYGLTECSPVVTTNPYGEQARLGT---VGIPVVGTALKVIDEQGNELPVGER 412
Cdd:cd17655 256 LIVGGEALSTELAKKIIELfgTNPTITNAYGPTETTVDASIYQYEPETDQQVsvpIGKPLGNTRIYILDQYGRPQPVGVA 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 413 GELCVKGPQVMKGYWQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAH 486
Cdd:cd17655 336 GELYIGGEGVARGYLNRPELTAEkfvddpFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQH 415
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 487 PKVASCAAVGIPDEkSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd17655 416 PDIKEAVVIARKDE-QGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPE 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
39-558 |
3.06e-39 |
|
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: 148.55 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYtaremrhqf 118
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAAR-GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 kdagvralvylnvfgklveevlPDTRIEYLIEarmgDLLPALkgwLVNSVvksvkkmvpdyrlpqalpfrqalkqgqgha 198
Cdd:cd17652 72 ----------------------PAERIAYMLA----DARPAL---LLTTP------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGKDGLPLMkeaqevmiaplplYHIYAFTANC- 277
Cdd:cd17652 93 --------DNLAYVIYTSGSTGRPKGVVVTHRGL-ANLAAAQIAAFDVGPGSRVLQ-------------FASPSFDASVw 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 -MCM-MVSGNHNVLITNPRDIPG--FVKELKKWRFSALlglnTLF-VALMEHPGFKDVDFSNLKltnSGGTALVSATAER 352
Cdd:cd17652 151 eLLMaLLAGATLVLAPAEELLPGepLADLLREHRITHV----TLPpAALAALPPDDLPDLRTLV---VAGEACPAELVDR 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 353 WkgVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEA 432
Cdd:cd17652 224 W--APGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGL 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 433 TEE--ILD-----AEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAScAAVGIPDEKSGEA 505
Cdd:cd17652 302 TAErfVADpfgapGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDK 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 506 --VKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17652 381 rlVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
39-558 |
3.54e-39 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 149.00 E-value: 3.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqGQGha 198
Cdd:cd17643 81 ADSGPSLLL------------------------------------------------------------------TDP-- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVAnmLQVHAQLsqlgkdglPLMKEAQEVMIaplpLYHIYAFTANCM 278
Cdd:cd17643 93 --------DDLAYVIYTSGSTGRPKGVVVSHANVLA--LFAATQR--------WFGFNEDDVWT----LFHSYAFDFSVW 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CM---MVSGNHNVLITN-----PRDipgFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATA 350
Cdd:cd17643 151 EIwgaLLHGGRLVVVPYevarsPED---FARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAML 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 351 ERW---KGVTGCTVVEGYGLTECSPVVT----TNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVM 423
Cdd:cd17643 228 RPWagrFGLDRPQLVNMYGITETTVHVTfrplDAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVA 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 424 KGYWQRPEATEE--ILDAEG-----WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:cd17643 308 RGYLGRPELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV 387
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 497 IPDEKSGEAVKLFVVARDPSLSV-EELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17643 388 REDEPGDTRLVAYVVADDGAAADiAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
296-562 |
8.02e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 148.77 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 296 IPGFVKE-LKKWRFSALLGLNTLFVALMEHPGFKDvdfSNLKLTNSG---GTALVSATAERWKGVTgctVVEGYGLTECS 371
Cdd:PRK07638 219 IPNQVLDkLETENISVMYTVPTMLESLYKENRVIE---NKMKIISSGakwEAEAKEKIKNIFPYAK---LYEFYGASELS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 372 PVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEiLDAEGWLKTGDIAVI 451
Cdd:PRK07638 293 FVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVGYE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 452 DEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVvarDPSLSVEELKAYCKENLT 531
Cdd:PRK07638 372 DEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQLKSFCLQRLS 448
|
250 260 270
....*....|....*....|....*....|.
gi 15598496 532 GYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEAKSWI 479
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
6-552 |
1.63e-38 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 149.86 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAGVPDSL-----DFAAYRSVVEVFERSCKKFADRPAfsnLGVT------------LSYAEL-DRLSAAFAAYLQ 67
Cdd:PLN02736 21 WNVYRSARSPLKLvsrfpDHPEIGTLHDNFVYAVETFRDYKY---LGTRirvdgtvgeykwMTYGEAgTARTAIGSGLVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 68 KqtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLYT---AREMRHQFKDAGVRAlvylnVFgkLVEEVLPdTR 144
Cdd:PLN02736 98 H--GIPKGACVGLYFINRPEWLIVDHACSAYSYVSV---PLYDtlgPDAVKFIVNHAEVAA-----IF--CVPQTLN-TL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 145 IEYLIEarmgdlLPALKgWLVnsVVKSVKKMVPDyrLPQA-----LPFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTT 219
Cdd:PLN02736 165 LSCLSE------IPSVR-LIV--VVGGADEPLPS--LPSGtgveiVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 220 GVSKGAMLTHGNLVANmlqvhAQLSQLGKDGLPlmkeaQEVMIAPLPLYHIYAFTANCMCM-------MVSGNH------ 286
Cdd:PLN02736 234 GTPKGVVLTHGNLIAN-----VAGSSLSTKFYP-----SDVHISYLPLAHIYERVNQIVMLhygvavgFYQGDNlklmdd 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 ------NVLITNPR-------DIPGFVKE---LKKWRFSAllGLNTLFVALME----HPGFKDVDFSNLK--------LT 338
Cdd:PLN02736 304 laalrpTIFCSVPRlynriydGITNAVKEsggLKERLFNA--AYNAKKQALENgknpSPMWDRLVFNKIKaklggrvrFM 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 339 NSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQArLGTVGIPVVGTALKVID----EQGNELPVGERGE 414
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNL-SGHVGSPNPACEVKLVDvpemNYTSEDQPYPRGE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 415 LCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLI-LVSGFNVYPNEIEDVVMAHPKVASCA 493
Cdd:PLN02736 461 ICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQCF 540
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 494 AVGipDEKSGEAVKlfVVARDPslsvEELKAYCKENLTGYKIPRQI---------VLKDalpMTPVGK 552
Cdd:PLN02736 541 VYG--DSLNSSLVA--VVVVDP----EVLKAWAASEGIKYEDLKQLcndprvraaVLAD---MDAVGR 597
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
207-555 |
2.28e-38 |
|
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: 143.94 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlqvhaQLSQLGKDGLPLMKEaqEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA-------VPDILQKEGLNWVVG--DVTYLPLPATHIGGLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 nVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAE--RWKGVTgcTVVEG 364
Cdd:cd17635 72 -VTGGENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRfiEATGLT--NTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 YGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLK 444
Cdd:cd17635 149 YGLSETGTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 445 TGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR--DPSLSVEEL 522
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASaeLDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 15598496 523 KAYCKENLTGYKIPRQIVLKDALPMTPVGKILR 555
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
48-496 |
7.62e-38 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 146.07 E-value: 7.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 48 VTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALV 127
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRAL-GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 128 ylnvFGKL-----VEEVLPDTRIEYLieARMGDLLPALKGWlvnsvvksvkkmvpdyrlpQALPFRQALKQGQghalqPV 202
Cdd:cd05932 84 ----VGKLddwkaMAPGVPEGLISIS--LPPPSAANCQYQW-------------------DDLIAQHPPLEER-----PT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 203 RvGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhaqLSQLGKDGlplmkeaQEVMIAPLPLYHIYAFTANCMCMMV 282
Cdd:cd05932 134 R-FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAG---IEHIGTEE-------NDRMLSYLPLAHVTERVFVEGGSLY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGnhnVLITNPRDIPGFVKELKKWRFSALLGLNTLFV-------------------------ALMEHPGFKDVDFSNLKL 337
Cdd:cd05932 203 GG---VLVAFAESLDTFVEDVQRARPTLFFSVPRLWTkfqqgvqdkipqqklnlllkipvvnSLVKRKVLKGLGLDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 338 TNSgGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVvgtalkvideQGNELPVGERGELCV 417
Cdd:cd05932 280 AGC-GSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHLNYPGRD-KIGTVGNAG----------PGVEVRISEDGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 418 KGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
28-558 |
3.43e-37 |
|
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: 143.23 E-value: 3.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAA-GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYTAREMRHQFKDAGVRALVylnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpf 187
Cdd:cd12115 82 AYPPERLRFILEDAQARLVL------------------------------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rqalkqgqghalqpvrVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQlsQLGKDGLPLMKEAQEVMIaPLPL 267
Cdd:cd12115 102 ----------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAA-AFLQWAAA--AFSAEELAGVLASTSICF-DLSV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 268 YHIYAFTANCMCMMVSGNHNVLITNPRdipgfvkelkkwRFSALLgLNT---LFVALMEHPGFKdvdfSNLKLTNSGGTA 344
Cdd:cd12115 162 FELFGPLATGGKVVLADNVLALPDLPA------------AAEVTL-INTvpsAAAELLRHDALP----ASVRVVNLAGEP 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 LVSATAER-WKGVTGCTVVEGYGLTECSPVVTTNPYGEQA-RLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQV 422
Cdd:cd12115 225 LPRDLVQRlYARLQVERVVNLYGPSEDTTYSTVAPVPPGAsGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGV 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 423 MKGYWQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:cd12115 305 ARGYLGRPGLTAErflpdpFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 497 IPDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd12115 385 IGDAAGERRLVAYIVAEPGAaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-558 |
5.68e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 147.41 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 4 EFWNDKrPAGVPDSldfaayRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMP 83
Cdd:PRK12316 4538 ALWNRT-DAGYPAT------RCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAME 4609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 84 NVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGw 163
Cdd:PRK12316 4610 RSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL---------------------LTQSHLLQRLPIPDG- 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 164 lvnsvvksVKKMVPDyrlpqalpfRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQL 243
Cdd:PRK12316 4668 --------LASLALD---------RDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV-NHLHATGER 4729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 244 SQLGKDGLPLMKEAQEVMIAPLPLYHIYAfTANCMCMMVSGNHnvlitnprDIPGFVKELKKWRFSALLGLNTLFVALME 323
Cdd:PRK12316 4730 YELTPDDRVLQFMSFSFDGSHEGLYHPLI-NGASVVIRDDSLW--------DPERLYAEIHEHRVTVLVFPPVYLQQLAE 4800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 324 HPGfKDVDFSNLKLTNSGGTALVSATAER-WKGVTGCTVVEGYGLTECSPVVTTnpygEQARLGT--------VGIPVVG 394
Cdd:PRK12316 4801 HAE-RDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLL----WKARDGDacgaaympIGTPLGN 4875
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 395 TALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE-----ILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLI 467
Cdd:PRK12316 4876 RSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQV 4955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 468 LVSGFNVYPNEIEDVVMAHPKVAScaAVGIPDEKS-GEAVKLFVVARDPSLS---------VEELKAYCKENLTGYKIPR 537
Cdd:PRK12316 4956 KIRGFRIELGEIEARLREHPAVRE--AVVIAQEGAvGKQLVGYVVPQDPALAdadeaqaelRDELKAALRERLPEYMVPA 5033
|
570 580
....*....|....*....|.
gi 15598496 538 QIVLKDALPMTPVGKILRREL 558
Cdd:PRK12316 5034 HLVFLARMPLTPNGKLDRKAL 5054
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-558 |
1.21e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 146.46 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 21 AAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGL 100
Cdd:PRK12467 509 YAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGG 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 101 VVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPalkgwlvnsvvksvkkmVPDyR 180
Cdd:PRK12467 588 AYVPLDPEYPQDRLAYMLDDSGVRLL---------------------LTQSHLLAQLP-----------------VPA-G 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 181 LPqALPFRQALKQGQGHALQ--PVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGKDGLPLMkeaq 258
Cdd:PRK12467 629 LR-SLCLDEPADLLCGYSGHnpEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDSMLM---- 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 259 eVMIAPLPLYHIYAFTANCmcmmvSGNhNVLITNP---RDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVdfSNL 335
Cdd:PRK12467 703 -VSTFAFDLGVTELFGALA-----SGA-TLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALP--RPQ 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 336 KLTNSGGTALVSATAERWKGVT-GCTVVEGYGLTECSPVVTTNPYGEQARLGT---VGIPVVGTALKVIDEQGNELPVGE 411
Cdd:PRK12467 774 RALVCGGEALQVDLLARVRALGpGARLINHYGPTETTVGVSTYELSDEERDFGnvpIGQPLANLGLYILDHYLNPVPVGV 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 412 RGELCVKGPQVMKGYWQRPEATEEIL-------DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVM 484
Cdd:PRK12467 854 VGELYIGGAGLARGYHRRPALTAERFvpdpfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLL 933
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 485 AHPKVASCAAVGIPDEKSGEAVKLFVVAR-----DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK12467 934 AQPGVREAVVLAQPGDAGLQLVAYLVPAAvadgaEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
39-558 |
1.35e-35 |
|
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: 139.33 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLytaremrhqf 118
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYV---PV---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 kDAGvralvylnvfgklveevLPDTRIEYLIEARMGDLLPALKGWLVNSVvksvkkmvpdyrLPQALPFRQALKQGQGHA 198
Cdd:cd12114 68 -DID-----------------QPAARREAILADAGARLVLTDGPDAQLDV------------AVFDVLILDLDALAAPAP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHG---NLVANMLQVHA--------QLSQLGKD-------GlPLMKEAQEV 260
Cdd:cd12114 118 PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRaalNTILDINRRFAvgpddrvlALSSLSFDlsvydifG-ALSAGATLV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 261 MIAPLplyhiYAFTANCMCMMVSgNHNVLITNprDIPgfvkelkkwrfsALLGLntlfvaLMEHPGFKDVDFSNLKLT-N 339
Cdd:cd12114 197 LPDEA-----RRRDPAHWAELIE-RHGVTLWN--SVP------------ALLEM------LLDVLEAAQALLPSLRLVlL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 340 SG---GTALVSATAERWKGvtgCTVVEGYGLTECS------PVVTTN------PYGeqarlgtvgIPVVGTALKVIDEQG 404
Cdd:cd12114 251 SGdwiPLDLPARLRALAPD---ARLISLGGATEASiwsiyhPIDEVPpdwrsiPYG---------RPLANQRYRVLDPRG 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGERGELCVKGPQVMKGYWQRPEATEE----ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAArfvtHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIE 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 481 DVVMAHPKVASCAAVGIpDEKSGEAVKLFVVAR--DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd12114 399 AALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDndGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
49-558 |
1.50e-35 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 139.15 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVY 128
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVfgklVEEVLPDTRIEYLIEarmGDLLPALKGWLVNSVVKSvkkmvpdyrlpqalpfrqalkqgqghalqpvrvglED 208
Cdd:cd17656 92 QRH----LKSKLSFNKSTILLE---DPSISQEDTSNIDYINNS-----------------------------------DD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLGKDGLPLMKEAQEVMIAplplYHiYAFTANCmcmmvSGNHNV 288
Cdd:cd17656 130 LLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFEREKTNINFSDKVLQFATCSFDVC----YQ-EIFSTLL-----SGGTLY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 289 LITNP--RDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLK-LTNSGGTALVSATAERWKGVTGCTVVEGY 365
Cdd:cd17656 199 IIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKhIITAGEQLVITNEFKEMLHEHNVHLHNHY 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 366 GLTEcSPVVTT---NPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILDAEGW 442
Cdd:cd17656 279 GPSE-THVVTTytiNPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 443 ------LKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVaSCAAVGIPDEKSGEAVKLFVVARDPS 516
Cdd:cd17656 358 dpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGV-SEAVVLDKADDKGEKYLCAYFVMEQE 436
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15598496 517 LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17656 437 LNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-562 |
1.72e-35 |
|
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: 140.77 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 31 ERSCKKFADRPAF------SNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLV--V 102
Cdd:cd05966 60 DRHLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVhsV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 103 VNTNplYTAREMRHQFKDAGVRALVYLNVF---GKLVEevLPDTRIEYLIEArmgdllPALKGWLVNSVVKSVKKMVPDY 179
Cdd:cd05966 139 VFAG--FSAESLADRINDAQCKLVITADGGyrgGKVIP--LKEIVDEALEKC------PSVEKVLVVKRTGGEVPMTEGR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 180 RLPQalpfrQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGnlvANMLQVHAQLSQL--GKDG------- 250
Cdd:cd05966 209 DLWW-----HDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTG---GYLLYAATTFKYVfdYHPDdiywcta 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 251 -------------LPLMKEAQEVMIAPLPLYHiyafTANCMCMMVsgnhnvlitnprdipgfvkelKKWRFSALLGLNTL 317
Cdd:cd05966 281 digwitghsyivyGPLANGATTVMFEGTPTYP----DPGRYWDIV---------------------EKHKVTIFYTAPTA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 318 FVALM----EHPgfKDVDFSNLKLTNSGGTAlVSATAERW-KGVTG---CTVVEGYGLTEC-SPVVTTNPYGEQARLGTV 388
Cdd:cd05966 336 IRALMkfgdEWV--KKHDLSSLRVLGSVGEP-INPEAWMWyYEVIGkerCPIVDTWWQTETgGIMITPLPGATPLKPGSA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 389 GIPVVGTALKVIDEQGNELPVGERGELCVKG--PQVMKGYWQRPEATEEIL--DAEGWLKTGDIAVIDEDGFVRIVDRKK 464
Cdd:cd05966 413 TRPFFGIEPAILDEEGNEVEGEVEGYLVIKRpwPGMARTIYGDHERYEDTYfsKFPGYYFTGDGARRDEDGYYWITGRVD 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 465 DLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD---PSLSVE-ELKAYCKENLTGYKIPRQIV 540
Cdd:cd05966 493 DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeePSDELRkELRKHVRKEIGPIATPDKIQ 572
|
570 580
....*....|....*....|..
gi 15598496 541 LKDALPMTPVGKILRRELREIA 562
Cdd:cd05966 573 FVPGLPKTRSGKIMRRILRKIA 594
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
51-552 |
5.54e-35 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 140.23 E-value: 5.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNplYTA--REMRHQFKDAGVRALVY 128
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYS--VEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YTAgvKGLTSAITAAEIKTIFT 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVF---GKL--VEEVLPDTRIEYLiEARMGDLLPALKGWLVNSVVksvkkmvpdyrlpqaLPFRQALKQgqghalQPvr 203
Cdd:PRK08043 309 SRQFldkGKLwhLPEQLTQVRWVYL-EDLKDDVTTADKLWIFAHLL---------------MPRLAQVKQ------QP-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 204 vglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVH--AQLSqlgkdglplmkeAQEVMIAPLPLYHIYAFTANCMCMM 281
Cdd:PRK08043 365 ---EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKtiADFT------------PNDRFMSALPLFHSFGLTVGLFTPL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 282 VSGNHNVLITNP---RDIPGFVKELKkwrFSALLGLNTLF--VALMEHPgfkdVDFSNLKLTNSGGTALVSATAERWKGV 356
Cdd:PRK08043 430 LTGAEVFLYPSPlhyRIVPELVYDRN---CTVLFGTSTFLgnYARFANP----YDFARLRYVVAGAEKLQESTKQLWQDK 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 TGCTVVEGYGLTECSPVVTTN-PYGeqARLGTVGIPVVGTALKVIDEQGNElpvgERGELCVKGPQVMKGYW--QRP--- 430
Cdd:PRK08043 503 FGLRILEGYGVTECAPVVSINvPMA--AKPGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPNIMNGYLrvEKPgvl 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 431 -----EATEEILDAeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEA 505
Cdd:PRK08043 577 evptaENARGEMER-GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEA 655
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15598496 506 VKLFVVarDPSLSVEELKAYCKEN-LTGYKIPRQIVLKDALPMTPVGK 552
Cdd:PRK08043 656 LVLFTT--DSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
39-558 |
7.56e-35 |
|
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: 136.44 E-value: 7.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYtaremrhqf 118
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLR-GLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 kdagvralvylnvfgklveevlPDTRIEYLIEARMGDLLpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghA 198
Cdd:cd17650 72 ----------------------PAERLQYMLEDSGAKLL----------------------------------------L 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNlVANMlqVHAQLSQLGKDGLPlmkeaqeVMIAPLPLYHIYAFTANCM 278
Cdd:cd17650 90 TQP-----EDLAYVIYTSGTTGKPKGVMVEHRN-VAHA--AHAWRREYELDSFP-------VRLLQMASFSFDVFAGDFA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNHNVLITNPR--DIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTalvSATAERWKGV 356
Cdd:cd17650 155 RSLLNGGTLVICPDEVklDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGSD---GCKAQDFKTL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 T-----GCTVVEGYGLTECSpVVTTNPYGEQARLGT-----VGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGY 426
Cdd:cd17650 232 AarfgqGMRIINSYGVTEAT-IDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGY 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 427 WQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAScAAVGIPDE 500
Cdd:cd17650 311 LNRPELTAErfvenpFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVRED 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 501 KSGEA-VKLFVVARDpSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17650 390 KGGEArLCAYVVAAA-TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
49-525 |
1.30e-34 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 137.72 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPlytarEMrhqfkdaGVRALVy 128
Cdd:PRK09274 41 ELSFAELDARSDAIAHGL-NAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDP-----GM-------GIKNLK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 lnvfgKLVEEVLPDTRIEyLIEARMGDLLpalKGWlvnsVVKSVKKMVPDYR--LPQALPFRQALKQGQGHALQPVRVGL 206
Cdd:PRK09274 107 -----QCLAEAQPDAFIG-IPKAHLARRL---FGW----GKPSVRRLVTVGGrlLWGGTTLATLLRDGAAAPFPMADLAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlQVHAQLSQLGKdglplmkEAQEVMIAPLPLYHIYAfTANCMCMMVsgnh 286
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEA---QIEALREDYGI-------EPGEIDLPTFPLFALFG-PALGMTSVI---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 nvlitnPrDI----PGFVKELKKWRFSALLGLNTLFV--ALMEHPG----FKDVDFSNLKLTNSGGTALVSATAERWKGV 356
Cdd:PRK09274 239 ------P-DMdptrPATVDPAKLFAAIERYGVTNLFGspALLERLGrygeANGIKLPSLRRVISAGAPVPIAVIERFRAM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 --TGCTVVEGYGLTECSPVVT---------TNPYGEQARlGT-VGIPVVGTALKVID---------EQGNELPVGERGEL 415
Cdd:PRK09274 312 lpPDAEILTPYGATEALPISSiesreilfaTRAATDNGA-GIcVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEE--ILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAS 491
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKR 470
|
490 500 510
....*....|....*....|....*....|....
gi 15598496 492 CAAVGIPdeKSGEAVKLFVVARDPSLSVEELKAY 525
Cdd:PRK09274 471 SALVGVG--VPGAQRPVLCVELEPGVACSKSALY 502
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
15-558 |
1.78e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.91 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 15 PDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFG 94
Cdd:PRK12467 3086 ATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLI-AIGVGPDVLVGVAVERSVEMIVALLA 3164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 95 ALRAGLVVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGwlvnsvvksVKK 174
Cdd:PRK12467 3165 VLKAGGAYVPLDPEYPRERLAYMIEDSGVKLL---------------------LTQAHLLEQLPAPAG---------DTA 3214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 175 MVPDYRLPQALPfrqalkqgqGHALQPVRVGlEDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGKDGLPLM 254
Cdd:PRK12467 3215 LTLDRLDLNGYS---------ENNPSTRVMG-ENLAYVIYTSGSTGKPKGVGVRHGAL-ANHLCWIAEAYELDANDRVLL 3283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 255 KE------AQEVMIAPLplyhiyaftANCMCMMVSGNHNvlitnpRDIPGFVKELKKWRFSALLGLNTLFVALMEhpgFK 328
Cdd:PRK12467 3284 FMsfsfdgAQERFLWTL---------ICGGCLVVRDNDL------WDPEELWQAIHAHRISIACFPPAYLQQFAE---DA 3345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 329 DV-DFSNLKLTNSGGTALVSATAERWKGVTG-CTVVEGYGLTECSPVVTTNPYGEQARLGT----VGIPVVGTALKVIDE 402
Cdd:PRK12467 3346 GGaDCASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLWKCGGDAVCEApyapIGRPVAGRSIYVLDG 3425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 403 QGNELPVGERGELCVKGPQVMKGYWQRPEATEE------ILDAEGWL-KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVY 475
Cdd:PRK12467 3426 QLNPVPVGVAGELYIGGVGLARGYHQRPSLTAErfvadpFSGSGGRLyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 476 PNEIEDVVMAHPKVASCAAVGIpDEKSGEAVKLFVVARDPSLSV-EELKAYCKENLTGYKIPRQIVLKDALPMTPVGKIL 554
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
|
....
gi 15598496 555 RREL 558
Cdd:PRK12467 3585 RKAL 3588
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-558 |
2.47e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.32 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 20 FAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAG 99
Cdd:PRK12316 507 YPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 100 LVVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGWlvnsvvksvkkmvpdy 179
Cdd:PRK12316 586 GAYVPLDPEYPAERLAYMLEDSGVQLL---------------------LSQSHLGRKLPLAAGV---------------- 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 180 rlpQALPFRQALKQGQGHALQP--VRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLG-KDG------ 250
Cdd:PRK12316 629 ---QVLDLDRPAAWLEGYSEENpgTELNPENLAYVIYTSGSTGKPKGAGNRHRALS-NRLCWMQQAYGLGvGDTvlqktp 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 251 -----------LPLMKEAQEVMIAPlplyhiyaftancmcmmvsGNHnvlitnpRDIPGFVKELKKWRFSALLGLNTLFV 319
Cdd:PRK12316 705 fsfdvsvweffWPLMSGARLVVAAP-------------------GDH-------RDPAKLVELINREGVDTLHFVPSMLQ 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 320 ALMEHPGFKDVDfsNLKLTNSGGTALVSATAERWKG-VTGCTVVEGYGLTECSPVVT-TNPYGEQARLGTVGIPVVGTAL 397
Cdd:PRK12316 759 AFLQDEDVASCT--SLRRIVCSGEALPADAQEQVFAkLPQAGLYNLYGPTEAAIDVThWTCVEEGGDSVPIGRPIANLAC 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 398 KVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSG 471
Cdd:PRK12316 837 YILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRG 916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 472 FNVYPNEIEDVVMAHPKVASCAAVGIpdekSGEAVKLFVVARDPSLS-VEELKAYCKENLTGYKIPRQIVLKDALPMTPV 550
Cdd:PRK12316 917 LRIELGEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDwREALKAHLAASLPEYMVPAQWLALERLPLTPN 992
|
....*...
gi 15598496 551 GKILRREL 558
Cdd:PRK12316 993 GKLDRKAL 1000
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
39-559 |
4.60e-34 |
|
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: 134.42 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALvylnvfgkLVEEvlPDTrIEYLIearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqgha 198
Cdd:cd17649 81 EDSGAGLL--------LTHH--PRQ-LAYVI------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvgledvavlqYTGGTTGVSKGAMLTHGNL------VANMLQVHA-----QLSQLGKDGL------PLMKEAQeVM 261
Cdd:cd17649 101 ---------------YTSGSTGTPKGVAVSHGPLaahcqaTAERYGLTPgdrelQFASFNFDGAheqllpPLICGAC-VV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 262 IAPLPLYHiyafTANCMCMMVSgnhNVLITNPRDIPGFVKELKKWrfsallglntlfvalMEHPGfkDVDFSNLKLTNSG 341
Cdd:cd17649 165 LRPDELWA----SADELAEMVR---ELGVTVLDLPPAYLQQLAEE---------------ADRTG--DGRPPSLRLYIFG 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 342 GTALVSATAERWkGVTGCTVVEGYGLTECspVVTTNPYGEQARLGT------VGIPVVGTALKVIDEQGNELPVGERGEL 415
Cdd:cd17649 221 GEALSPELLRRW-LKAPVRLFNAYGPTEA--TVTPLVWKCEAGAARagasmpIGRPLGGRSAYILDADLNPVPVGVTGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 416 CVKGPQVMKGYWQRPEATEE--ILD---AEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPK 488
Cdd:cd17649 298 YIGGEGLARGYLGRPELTAErfVPDpfgAPGsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPG 377
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 489 VASCAAVGIPDEKSGEAVKlFVVARDPS---LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd17649 378 VREAAVVALDGAGGKQLVA-YVVLRAAAaqpELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
198-560 |
2.08e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 133.97 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 ALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqVHAQLSQLGKDglplmkEAQEVMIAPLPLYHIYAFTANC 277
Cdd:PRK07768 143 PIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN---AEAMFVAAEFD------VETDVMVSWLPLFHDMGMVGFL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 MCMMVSGNHNVLITnP----RDIPGFVKELKKWRFSALLGLN---TLFVALMEH-PGFKDVDFSNLKLTNSGGTALVSAT 349
Cdd:PRK07768 214 TVPMYFGAELVKVT-PmdflRDPLLWAELISKYRGTMTAAPNfayALLARRLRRqAKPGAFDLSSLRFALNGAEPIDPAD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 350 AERWK------GVTGCTVVEGYGLTECSPVVTTNPYGEQA-------------------------RLGTVGIPVVGTALK 398
Cdd:PRK07768 293 VEDLLdagarfGLRPEAILPAYGMAEATLAVSFSPCGAGLvvdevdadllaalrravpatkgntrRLATLGPPLPGLEVR 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 399 VIDEQGNELPVGERGELCVKGPQVMKGYwQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNE 478
Cdd:PRK07768 373 VVDEDGQVLPPRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTD 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 479 IEDVVMAHPKV-ASCA-AVGIPDEKSGE--AVKLFVVARDPSLSVEELKAYCKENL---TGYKiPRQIVL--KDALPMTP 549
Cdd:PRK07768 452 IERAAARVEGVrPGNAvAVRLDAGHSREgfAVAVESNAFEDPAEVRRIRHQVAHEVvaeVGVR-PRNVVVlgPGSIPKTP 530
|
410
....*....|.
gi 15598496 550 VGKILRRELRE 560
Cdd:PRK07768 531 SGKLRRANAAE 541
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
208-562 |
2.58e-33 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 133.99 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNlvanmlqvhAQLSQLGkdglplMKEAQEVMIAP-----LPLYHIYAFTANcMCMMV 282
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRG---------AYLSTLS------AIIGWEMGTCPvylwtLPMFHCNGWTFT-WGTAA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGNHNVLITNPrDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVtGCTVV 362
Cdd:PLN03102 251 RGGTSVCMRHV-TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 363 EGYGLTECS-PVVTTN--------PYGEQARL-GTVGIPVVGTA---------LKVIDEQGNELpvgerGELCVKGPQVM 423
Cdd:PLN03102 329 HAYGLTEATgPVLFCEwqdewnrlPENQQMELkARQGVSILGLAdvdvknketQESVPRDGKTM-----GEIVIKGSSIM 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 424 KGYWQRPEATEEILDaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSG 503
Cdd:PLN03102 404 KGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWG 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 504 EAVKLFVVARDPSLSVEE-----------LKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PLN03102 483 ETPCAFVVLEKGETTKEDrvdklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDIA 552
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
51-562 |
3.13e-33 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 133.82 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 51 SYAELDRLSAAFAAYlqkqtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYLN 130
Cdd:PLN02479 51 TYQRCRRLASALAKR-----SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 131 VFGKLVEEVLpdtriEYLIEARMGDLLPALkgwLVNSVVKSVKKMVPDYRLPQ-ALPFRQALKQGQ-GHALQPVRVGLED 208
Cdd:PLN02479 126 EFFTLAEEAL-----KILAEKKKSSFKPPL---LIVIGDPTCDPKSLQYALGKgAIEYEKFLETGDpEFAWKPPADEWQS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAvLQYTGGTTGVSKGAMLTHGNlvanmlqvhAQLSQLGKdglPLMKEAQE--VMIAPLPLYHI----YAFTANCMCmmv 282
Cdd:PLN02479 198 IA-LGYTSGTTASPKGVVLHHRG---------AYLMALSN---ALIWGMNEgaVYLWTLPMFHCngwcFTWTLAALC--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 sGNHNVL--ITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHpgfKDVDFSNLKLTNSGGTA----LVSATAERwkgv 356
Cdd:PLN02479 262 -GTNICLrqVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSE---TILPLPRVVHVMTAGAApppsVLFAMSEK---- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 tGCTVVEGYGLTE-------CS--PVVTTNPYGEQARLGT-VGIPVVG-TALKVIDEQGNElPV----GERGELCVKGPQ 421
Cdd:PLN02479 334 -GFRVTHTYGLSEtygpstvCAwkPEWDSLPPEEQARLNArQGVRYIGlEGLDVVDTKTMK-PVpadgKTMGEIVMRGNM 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 422 VMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEK 501
Cdd:PLN02479 412 VMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 502 SGEAVKLFVVAR------DPSLSVEELKAYCKENLTGYKIPRQIVLkDALPMTPVGKILRRELREIA 562
Cdd:PLN02479 491 WGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAKA 556
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
28-558 |
1.29e-32 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 129.98 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 28 EVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNP 107
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 108 LYtaremrhqfkdagvralvylnvfgklveevlPDTRIEYLiearmgdllpalkgwLVNSVVKSVkkmvpdyrlpqalpf 187
Cdd:cd17645 81 DY-------------------------------PGERIAYM---------------LADSSAKIL--------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 188 rqaLKQGqghalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAQLSQLGKDGLPLmkeaqevmiaplpL 267
Cdd:cd17645 100 ---LTNP------------DDLAYVIYTSGSTGLPKGVMIEHHNLV-NLCEWHRPYFGVTPADKSL-------------V 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 268 YHIYAFTANCMCM----MVSGNHNVLitnPRDIPGFVKELKKWRFSALLGLNTLFVALMEHpgFKDVDFSNLKLTNSGGT 343
Cdd:cd17645 151 YASFSFDASAWEIfphlTAGAALHVV---PSERRLDLDALNDYFNQEGITISFLPTGAAEQ--FMQLDNQSLRVLLTGGD 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 344 ALVSATAErwkgvtGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVM 423
Cdd:cd17645 226 KLKKIERK------GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLA 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 424 KGYWQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI 497
Cdd:cd17645 300 RGYLNRPELTAEkfivhpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK 379
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 498 PDEKSGEAVKLFVVARDpSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17645 380 EDADGRKYLVAYVTAPE-EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-552 |
1.46e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 128.27 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLqYTGGTTGVSKGAMLTHGNLVANMLQV--HAQLSQLGKDGLPLMKEAQE--VMIAPLPLYH----IYAFTAncm 278
Cdd:cd05924 4 DDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGGadFGTGEFTPSEDAHKAAAAAAgtVMFPAPPLMHgtgsWTAFGG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 cmmVSGNHNVLITNPRDIPGFVkelkkWRFSALLGLNTLFVA--LMEHP------GFKDVDFSNLKLTNSGGTALVSATA 350
Cdd:cd05924 80 ---LLGGQTVVLPDDRFDPEEV-----WRTIEKHKVTSMTIVgdAMARPlidalrDAGPYDLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 351 ERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTAlkVIDEQGNELPVGE--RGELCVKGpQVMKGYW 427
Cdd:cd05924 152 QGLlELVPNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV--VLDDDGRVVPPGSggVGWIARRG-HIPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 428 QRPEATEEI---LDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:cd05924 229 GDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15598496 505 AVKLFVVARDP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGK 552
Cdd:cd05924 309 EVVAVVQLREGaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-558 |
1.54e-32 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 133.63 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 6 WNDKRPAgVPDSldfaayrSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNV 85
Cdd:PRK10252 448 VNATAVE-IPET-------TLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLL-RERGVKPGDSVAVALPRS 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 86 LQYPIAVFGALRAGLVVVntnPLYTARemrhqfkdagvralvylnvfgklveevlPDTRIEYLIEarmgDLLPALkgwLV 165
Cdd:PRK10252 519 VFLTLALHAIVEAGAAWL---PLDTGY----------------------------PDDRLKMMLE----DARPSL---LI 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 NSvvKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGleDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQ 245
Cdd:PRK10252 561 TT--ADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPH--HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 LGKDG-----------------LPLMKEAQEVMIAP------LPLYHIYAFTAncmcmmVSGNHNVlitnPRDIPGFVKE 302
Cdd:PRK10252 637 TADDVvlqktpcsfdvsvweffWPFIAGAKLVMAEPeahrdpLAMQQFFAEYG------VTTTHFV----PSMLAAFVAS 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 303 LKKWR-FSALLGLNTLFVAlmehpgfkdvdfsnlkltnsgGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGE 381
Cdd:PRK10252 707 LTPEGaRQSCASLRQVFCS---------------------GEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFG 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 382 QARLGT------VGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE------ILDAEGWLKTGDIA 449
Cdd:PRK10252 766 EELAAVrgssvpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASrfiadpFAPGERMYRTGDVA 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 450 VIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI----PDEKSGEAVKL--FVVAR-DPSLSVEEL 522
Cdd:PRK10252 846 RWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqAAATGGDARQLvgYLVSQsGLPLDTSAL 925
|
570 580 590
....*....|....*....|....*....|....*.
gi 15598496 523 KAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK10252 926 QAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
39-560 |
2.26e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 130.57 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVYLNVFGKLVEEVLPDTRIeyliearmgdllpalkgwlVNSvvksvkkmvpdyrlpQALPFRQALKQGQGHA 198
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRV-------------------INV---------------DSPAWADELAAHRDAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLV--ANMLqvhAQLSQLGKDglplmkeaqEVMIAPLPLYHIYAFTAn 276
Cdd:PRK07867 144 PPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsaGVML---AQRFGLGPD---------DVCYVSMPLFHSNAVMA- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 277 CMCMMVSGNHNVLITNPRDIPGFVKELKkwRFSAllglnTLF----------VALMEHPGfkDVDfSNLKLT--NSGGTA 344
Cdd:PRK07867 211 GWAVALAAGASIALRRKFSASGFLPDVR--RYGA-----TYAnyvgkplsyvLATPERPD--DAD-NPLRIVygNEGAPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 LVSATAERWkgvtGCTVVEGYGLTECSPVVTTNPygeQARLGTVGIPVVGTAlkVID-EQGNELPVGER----------- 412
Cdd:PRK07867 281 DIARFARRF----GCVVVDGFGSTEGGVAITRTP---DTPPGALGPLPPGVA--IVDpDTGTECPPAEDadgrllnadea 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 413 -GELC-VKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVA 490
Cdd:PRK07867 352 iGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 491 SCAAVGIPDEKSGEAVKLFVV-ARDPSLSVEELKAY--CKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAALVlAPGAKFDPDAFAEFlaAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
207-560 |
5.33e-32 |
|
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: 129.15 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDGLplmkeaqevmIAPLPLYHIYAFTA-NCMCMMVSGN 285
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRI----------LSWMPLTHDMGLIAfHLAPLIAGMN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 286 HNVLITNP--RDIPGFVKELKKWRFSALLGLN---TLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWK------ 354
Cdd:cd05908 176 QYLMPTRLfiRRPILWLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLdhmsky 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 355 GVTGCTVVEGYGLTECSPVVTTNPYGEQ---------------------------ARLGTVGIPVVGTALKVIDEQGNEL 407
Cdd:cd05908 256 GLKRNAILPVYGLAEASVGASLPKAQSPfktitlgrrhvthgepepevdkkdsecLTFVEVGKPIDETDIRICDEDNKIL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 408 PVGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIdEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHP 487
Cdd:cd05908 336 PDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 488 KVAS--CAAVGIPDEKS-GEAVKLFVVARDpslSVEELKAYCKE------NLTGYKIpRQIVLKDALPMTPVGKILRREL 558
Cdd:cd05908 415 GVELgrVVACGVNNSNTrNEEIFCFIEHRK---SEDDFYPLGKKikkhlnKRGGWQI-NEVLPIRRIPKTTSGKVKRYEL 490
|
..
gi 15598496 559 RE 560
Cdd:cd05908 491 AQ 492
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
39-560 |
8.30e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 129.38 E-value: 8.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDlqPGDR--IAVQMPNVLQYPIAVFGALRAGLVVVNTNPL----YTAR 112
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALAD--PDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTrrgaALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 113 EMRHqfkdAGVRALVylnvfgklveevlpdTRIEYLieARMGDL-LPALKGWLVNSvvksvkkmvPDYRlpqalpfrQAL 191
Cdd:PRK13388 94 DIRR----ADCQLLV---------------TDAEHR--PLLDGLdLPGVRVLDVDT---------PAYA--------ELV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 192 kqGQGHALQPVR-VGLEDVAVLQYTGGTTGVSKGAMLTHGnlvanMLQVHAQlSQLGKDGLplmkEAQEVMIAPLPLYHI 270
Cdd:PRK13388 136 --AAAGALTPHReVDAMDPFMLIFTSGTTGAPKAVRCSHG-----RLAFAGR-ALTERFGL----TRDDVCYVSMPLFHS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 271 YAFTANCMCMMVSGnhnVLITNPRDIP--GFVKELKkwRFSAllglnTLF----------VALMEHPgfkdvDFSNLKLT 338
Cdd:PRK13388 204 NAVMAGWAPAVASG---AAVALPAKFSasGFLDDVR--RYGA-----TYFnyvgkplayiLATPERP-----DDADNPLR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 339 NSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLG--TVGIPVVGT------ALKVIDEQGNELPVG 410
Cdd:PRK13388 269 VAFGNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPPGSIGrgAPGVAIYNPetltecAVARFDAHGALLNAD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 411 ER-GELCVK-GPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPK 488
Cdd:PRK13388 349 EAiGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA 427
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 489 VASCAAVGIPDEKSGEAVKLFVVARDP-SLSVEELKAY--CKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK13388 428 INRVAVYAVPDERVGDQVMAALVLRDGaTFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
14-560 |
8.35e-32 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 129.74 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 14 VPDSLDFAAyrsvvevfeRSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKqTDLQPGDRIAVQMPNVLQYPIAVF 93
Cdd:PRK09192 23 LVEALDYAA---------LGEAGMNFYDRRGQLEEALPYQTLRARAEAGARRLLA-LGLKPGDRVALIAETDGDFVEAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 94 GALRAGLVVVNTnPLYTA---RE-----MRHQFKDAGVRALVYLNVFGKLVEEVLPDTRIEYLIEARMGDLLPAlkgwlv 165
Cdd:PRK09192 93 ACQYAGLVPVPL-PLPMGfggREsyiaqLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPE------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 166 nsvvksvkkmvPDYRLPQALPfrqalkqgqghalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANmLQVHAQlsq 245
Cdd:PRK09192 166 -----------ADVALPRPTP--------------------DDIAYLQYSSGSTRFPRGVIITHRALMAN-LRAISH--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 246 lgkDGLPLmkEAQEVMIAPLPLYHIYAFTAnCMCMMVSGNHNVLITNPRDipgFVKELKKW-----------RFSALLGL 314
Cdd:PRK09192 211 ---DGLKV--RPGDRCVSWLPFYHDMGLVG-FLLTPVATQLSVDYLPTRD---FARRPLQWldlisrnrgtiSYSPPFGY 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 315 NtLFVALMEHPGFKDVDFSNLKLTNSGG----TALVSATAERWK--GVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTV 388
Cdd:PRK09192 282 E-LCARRVNSKDLAELDLSCWRVAGIGAdmirPDVLHQFAEAFApaGFDDKAFMPSYGLAEATLAVSFSPLGSGIVVEEV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 389 ---------------------------GIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEiLDAEG 441
Cdd:PRK09192 361 drdrleyqgkavapgaetrrvrtfvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDV-LAADG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 442 WLKTGDIAVIdEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAS--CAAVGIPDEkSGEAVKLFVVAR--DP-- 515
Cdd:PRK09192 440 WLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAAFSIAQE-NGEKIVLLVQCRisDEer 517
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 15598496 516 --SLsVEELKAYCKeNLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK09192 518 rgQL-IHALAALVR-SEFGVEAAVELVPPHSLPRTSSGKLSRAKAKK 562
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
49-471 |
1.64e-31 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 128.84 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYtaremrhqfkdagvrALVY 128
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDR-GLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY---------------SLVS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNvFGKL---VEEVLPDtrieyLIEARMGDLL-PALKGWLVNSV-VKSVKKMVPDyrlPQALPFRQALKQGQGHALQPV- 202
Cdd:PRK08180 133 QD-FGKLrhvLELLTPG-----LVFADDGAAFaRALAAVVPADVeVVAVRGAVPG---RAATPFAALLATPPTAAVDAAh 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 203 -RVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqvHAQLSQLgkdgLPLMKEAQEVMIAPLPLYHIYAftancmcmm 281
Cdd:PRK08180 204 aAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCAN----QQMLAQT----FPFLAEEPPVLVDWLPWNHTFG--------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 282 vsGNHN---VL-------ITNPRDIPG-FVKELKKWR-------FSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGT 343
Cdd:PRK08180 267 --GNHNlgiVLynggtlyIDDGKPTPGgFDETLRNLReisptvyFNVPKGWEMLVPALERDAALRRRFFSRLKLLFYAGA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 344 ALVSATAERWKGVTGCTVVE------GYGLTECSPVVTtNPYGEQARLGTVGIPVVGTALKVIdeqgnelPVGERGELCV 417
Cdd:PRK08180 345 ALSQDVWDRLDRVAEATCGErirmmtGLGMTETAPSAT-FTTGPLSRAGNIGLPAPGCEVKLV-------PVGGKLEVRV 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598496 418 KGPQVMKGYWQRPEATEEILDAEGWLKTGD-IAVIDED----GFV---RIVDrkkDLILVSG 471
Cdd:PRK08180 417 KGPNVTPGYWRAPELTAEAFDEEGYYRSGDaVRFVDPAdperGLMfdgRIAE---DFKLSSG 475
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-558 |
1.91e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 130.67 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 4 EFWNdkrpagvPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMP 83
Cdd:PRK12467 1561 EGWN-------ATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVE 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 84 NVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGw 163
Cdd:PRK12467 1633 RSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELL---------------------LTQSHLQARLPLPDG- 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 164 lVNSVVksvkkmvpdyrLPQAlpfrQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlQVHAql 243
Cdd:PRK12467 1691 -LRSLV-----------LDQE----DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVN---RLCA-- 1749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 244 sqlgkdglplMKEAQEVMIAPLPL-YHIYAFTANC---MCMMVSGNhNVLITNP---RDIPGFVKELKKWRFSALLGLNT 316
Cdd:PRK12467 1750 ----------TQEAYQLSAADVVLqFTSFAFDVSVwelFWPLINGA-RLVIAPPgahRDPEQLIQLIERQQVTTLHFVPS 1818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 LFVALMEHPGfKDVDFSNLKLTNSGGTALVSATAERWKGVTGCT-VVEGYGLTECSPVVT----TNPYGEQARLGTVGIP 391
Cdd:PRK12467 1819 MLQQLLQMDE-QVEHPLSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTETAVDVThwtcRRKDLEGRDSVPIGQP 1897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 392 VVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE--ILDAEGWL-----KTGDIAVIDEDGFVRIVDRKK 464
Cdd:PRK12467 1898 IANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAErfVADPFGTVgsrlyRTGDLARYRADGVIEYLGRID 1977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 465 DLILVSGFNVYPNEIEDVVMAHPKVAScAAVGIPDEKSGEAVKLFVVARDPSL---------SVEELKAYCKENLTGYKI 535
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVRE-AVVIAQDGANGKQLVAYVVPTDPGLvdddeaqvaLRAILKNHLKASLPEYMV 2056
|
570 580
....*....|....*....|...
gi 15598496 536 PRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
29-558 |
2.62e-31 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 127.82 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 29 VFERSCKKFADRPAFSNL----GVT-LSYAELDRLSAAFAAYLQKQTDLQpGDRIAVQMPNVLQYPIAVFGALRAGLVVV 103
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALrrcdGTSaLRYRELVAEVGGLAADLRAQSVSR-GSRVLVISDNGPETYLSVLACAKLGAIAV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 104 ----NTNPLYTARemrhqFKDAGVRALVYLNVFGKLVEEVLPDTRIEyliearmgdlLPALKGWLVNSVVKSVKKMVPDY 179
Cdd:PRK05857 95 madgNLPIAAIER-----FCQITDPAAALVAPGSKMASSAVPEALHS----------IPVIAVDIAAVTRESEHSLDAAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 180 rlPQALPfrqalkqgqghalqpvRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVA--NMLQvhaqlsqlgKDGLPLMK-E 256
Cdd:PRK05857 160 --LAGNA----------------DQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpDILQ---------KEGLNWVTwV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 257 AQEVMIAPLPLYHIYAFTANCMCMMVSGnhnVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLK 336
Cdd:PRK05857 213 VGETTYSPLPATHIGGLWWILTCLMHGG---LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 337 LTNSGGTALVSATAeRWKGVTGCTVVEGYGLTE--CSPVVTTNPYGEQARL--GTVGIPVVGTALKVIDEQG------NE 406
Cdd:PRK05857 290 LVGYGGSRAIAADV-RFIEATGVRTAQVYGLSEtgCTALCLPTDDGSIVKIeaGAVGRPYPGVDVYLAATDGigptapGA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 407 LPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAH 486
Cdd:PRK05857 369 GPSASFGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGV 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 487 PKVASCAAVGIPDEKSGEAVKLFVVAR---DPSLSVE---ELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK05857 448 SGVREAACYEIPDEEFGALVGLAVVASaelDESAARAlkhTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-559 |
5.23e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.13 E-value: 5.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 15 PDSLDFAAYRSVVEVFERSCKKF-ADRPafsNLGVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVF 93
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFlADDP---GEGVVLSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSGPDYVAAFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 94 GALRAGLVVVNTNPLYTAREmRHQ------FKDAGVRALvylnvfgkLVEEVLPDTRIEylIEARMGDLLPalkGWLvns 167
Cdd:PRK05691 83 GCLYAGVIAVPAYPPESARR-HHQerllsiIADAEPRLL--------LTVADLRDSLLQ--MEELAAANAP---ELL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 168 vvkSVKKMVPdyrlpqalpfrqALKQG-QGHALQPvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqvhaqlSQL 246
Cdd:PRK05691 146 ---CVDTLDP------------ALAEAwQEPALQP-----DDIAFLQYTSGSTALPKGVQVSHGNLVAN--------EQL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 247 GKDGLPLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITnprdiPG-FVKELKKW--RFSALLGLNT------- 316
Cdd:PRK05691 198 IRHGFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMS-----PAyFLERPLRWleAISEYGGTISggpdfay 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 -LFVALMEHPGFKDVDFSNLKLTNSGGTAL----VSATAERWK--GVTGCTVVEGYGLTECSPVVTTNPYGE-------- 381
Cdd:PRK05691 273 rLCSERVSESALERLDLSRWRVAYSGSEPIrqdsLERFAEKFAacGFDPDSFFASYGLAEATLFVSGGRRGQgipaleld 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 382 -------QARLGT------VGIPVVGTALKVIDEQ-GNELPVGERGELCVKGPQVMKGYWQRPEATEEI---LDAEGWLK 444
Cdd:PRK05691 353 aealarnRAEPGTgsvlmsCGRSQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfveHDGRTWLR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 445 TGDIAVIdEDGFVRIVDRKKDLILVSGFNVYPNEIEDV------VMAHPKVASCA-------AVGIPDEKSgEAVKLFVV 511
Cdd:PRK05691 433 TGDLGFL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTvereveVVRKGRVAAFAvnhqgeeGIGIAAEIS-RSVQKILP 510
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 15598496 512 ARDPSLSVEELKA-YCKEnltgykIPRQIVLKD--ALPMTPVGKILRRELR 559
Cdd:PRK05691 511 PQALIKSIRQAVAeACQE------APSVVLLLNpgALPKTSSGKLQRSACR 555
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
194-560 |
5.40e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 123.62 E-value: 5.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 194 GQGHALQPV---------------RVGL---EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLsqlGKDGLPLMK 255
Cdd:PRK07824 4 GRAPALLPVpaqderraallrdalRVGEpidDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRL---GGPGQWLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 256 eaqevmiapLPLYHIYAFTAnCMCMMVSGNHNVLIT-----NPRDIPGFVKELKKWRFSALLGLNTLFVAlMEHPGFKDV 330
Cdd:PRK07824 81 ---------LPAHHIAGLQV-LVRSVIAGSEPVELDvsagfDPTALPRAVAELGGGRRYTSLVPMQLAKA-LDDPAATAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 331 dfsnLKLTNS---GGTALVSATAERWKGVtGCTVVEGYGLTECSPvvttnpygeqarlGTV--GIPVVGTALKVIDEqgn 405
Cdd:PRK07824 150 ----LAELDAvlvGGGPAPAPVLDAAAAA-GINVVRTYGMSETSG-------------GCVydGVPLDGVRVRVEDG--- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 406 elpvgeRGELcvKGPQVMKGYwqRPEATEEILDAEGWLKTGDIAVIDeDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMA 485
Cdd:PRK07824 209 ------RIAL--GGPTLAKGY--RNPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 486 HPKVASCAAVGIPDEKSGEAVKLFVVAR-DPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK07824 278 HPAVADCAVFGLPDDRLGQRVVAAVVGDgGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
335-558 |
1.01e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 125.88 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 335 LKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNelPVGER-- 412
Cdd:PRK13383 294 LRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNR--PVGPRvt 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 413 GELCVKGPQVMKGYwqRPEATEEILDaeGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASC 492
Cdd:PRK13383 372 GRIFVGGELAGTRY--TDGGGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADN 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 493 AAVGIPDEKSGEAVKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK13383 448 AVIGVPDERFGHRLAAFVVLHPGSgVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-558 |
1.69e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.77 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 1 MQPEFWNDKRPAGVPDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAV 80
Cdd:PRK12316 3034 LDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL-IERGVGPDVLVGV 3112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 81 QMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALvylnvfgkLVEEVLPdtrieyliearmgdlLPAL 160
Cdd:PRK12316 3113 AVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL--------LSQSHLR---------------LPLA 3169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 161 KGWLVNSVvksvkkmvpdyrlpqalpfrQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVH 240
Cdd:PRK12316 3170 QGVQVLDL--------------------DRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL-SNHLCWM 3228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 241 AQLSQLGKDGLPLMKEAQEVMIAPLPLYHIYAFTANcmcMMVSGnhnvlITNPRDIPGFVKELKKWRFSALLGLNTLFVA 320
Cdd:PRK12316 3229 QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGAR---VVLAG-----PEDWRDPALLVELINSEGVDVLHAYPSMLQA 3300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 321 LMEHPGFKDvdFSNLKLTNSGGTALVSATAERWkgVTGCTVVEGYGLTECSPVVTTNPYGEQARLGT-VGIPVVGTALKV 399
Cdd:PRK12316 3301 FLEEEDAHR--CTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAVpIGRPIANRACYI 3376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 400 IDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE------ILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFN 473
Cdd:PRK12316 3377 LDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAErfvpdpFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFR 3456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 474 VYPNEIEDVVMAHPKVAScaAVGIPDEksGEAVKLFVVARDPSLSV-EELKAYCKENLTGYKIPRQIVLKDALPMTPVGK 552
Cdd:PRK12316 3457 IELGEIEARLLEHPWVRE--AVVLAVD--GRQLVAYVVPEDEAGDLrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGK 3532
|
....*.
gi 15598496 553 ILRREL 558
Cdd:PRK12316 3533 LDRKAL 3538
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
49-560 |
2.81e-30 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 124.89 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVY 128
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVFGKLVEEVLPDTrieyliearmgdllPALKGWLVNSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVrVGLED 208
Cdd:PRK05620 118 DPRLAEQLGEILKEC--------------PCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLDGRSTVYDWPE-LDETT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLvanMLQvhaQLSQLGKDGLPLmkEAQEVMIAPLPLYHIYAFTANCMCMMvSGNHNV 288
Cdd:PRK05620 183 AAAICYSTGTTGAPKGVVYSHRSL---YLQ---SLSLRTTDSLAV--THGESFLCCVPIYHVLSWGVPLAAFM-SGTPLV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 289 LITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLT 368
Cdd:PRK05620 254 FPGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 369 ECSPV--VTTNPYGE--QARLG---TVGIPVVGTALKVIDEqGNELPVGER--GELCVKGPQVMKGYWQRPEATE----- 434
Cdd:PRK05620 334 ETSPVgtVARPPSGVsgEARWAyrvSQGRFPASLEYRIVND-GQVMESTDRneGEIQVRGNWVTASYYHSPTEEGggaas 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 435 -----------EILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSG 503
Cdd:PRK05620 413 tfrgedvedanDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 504 E---AVKLFVVARDPSL-SVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK05620 493 ErplAVTVLAPGIEPTReTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
25-480 |
3.63e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 125.23 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 25 SVVEVFERSCKKFADRPAFSNL-------GVT--LSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGA 95
Cdd:PRK07769 22 NLVRHVERWAKVRGDKLAYRFLdfsterdGVArdLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 96 LRAGLVVVntnPLYTAREMRHQfkdagvralvylnvfGKLveevlpdtrieyliEARMGDLLPA--LKgwlVNSVVKSVK 173
Cdd:PRK07769 100 LYAGRIAV---PLFDPAEPGHV---------------GRL--------------HAVLDDCTPSaiLT---TTDSAEGVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 174 KMV---PDYRLPQALPFrQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHaqlsqlgkDG 250
Cdd:PRK07769 145 KFFrarPAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVI--------DA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 251 LPLMKEAQEVmiAPLPLYHIYAFTancMCMMVS-GNHNVLITNPRdipGFVKELKKW-RFSALLGLNTL--FVAL----M 322
Cdd:PRK07769 216 LEGQEGDRGV--SWLPFFHDMGLI---TVLLPAlLGHYITFMSPA---AFVRRPGRWiRELARKPGGTGgtFSAApnfaF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 323 EH--------PGFKDVDFSNLK-LTNsgGTALVSATAERwK--------GVTGCTVVEGYGLTECSPVVTTNPYGEQARL 385
Cdd:PRK07769 288 EHaaarglpkDGEPPLDLSNVKgLLN--GSEPVSPASMR-KfneafapyGLPPTAIKPSYGMAEATLFVSTTPMDEEPTV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 386 GTV-------------------GIPVVGT--------ALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE--- 435
Cdd:PRK07769 365 IYVdrdelnagrfvevpadapnAVAQVSAgkvgvsewAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAAtfq 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 436 -ILD-------AEG------WLKTGDIAVIdEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:PRK07769 445 nILKsrlseshAEGapddalWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
24-562 |
5.06e-30 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 123.77 E-value: 5.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAF--SNLGVtLSYAELDRLSAAFAAYLQKQtdlqPGDRIAVQMPNVLQYPIAVFGALRAGLV 101
Cdd:PRK06334 19 KTVLESFLKLCSEMTTATVCwdEQLGK-LSYNQVRKAVIALATKVSKY----PDQHIGIMMPASAGAYIAYFATLLSGKI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 102 VVNTNPLYTAREMRHQFKDAGVRALVYLNVFGKLVEEVLPDTrIEY---LIeaRMGDLLPALKGWlvnsvvksvKKMVPD 178
Cdd:PRK06334 94 PVMINWSQGLREVTACANLVGVTHVLTSKQLMQHLAQTHGED-AEYpfsLI--YMEEVRKELSFW---------EKCRIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 179 YRLpqALPFRQALK----QGQGHalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSqlgkdglplm 254
Cdd:PRK06334 162 IYM--SIPFEWLMRwfgvSDKDP---------EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFS---------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 255 KEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNP---RDIPGFVKELKkwrfSALLGLNTLFVALMEHPGFK-DV 330
Cdd:PRK06334 221 PKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNPlypKKIVEMIDEAK----VTFLGSTPVFFDYILKTAKKqES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 331 DFSNLKLTNSGGTALV-SATAERWKGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQgNELPV 409
Cdd:PRK06334 297 CLPSLRFVVIGGDAFKdSLYQEALKTFPHIQLRQGYGTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEE-TKVPV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 410 --GERGELCVKGPQVMKGYWQRPEATEEI-LDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAH 486
Cdd:PRK06334 376 ssGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 487 ------PKVASCAAVGIPdeksGEAVKLFVVARDPSlSVEELKAYCKENLTG--YKIPRQIVLkDALPMTPVGKILRREL 558
Cdd:PRK06334 456 fgqnaaDHAGPLVVCGLP----GEKVRLCLFTTFPT-SISEVNDILKNSKTSsiLKISYHHQV-ESIPMLGTGKPDYCSL 529
|
....
gi 15598496 559 REIA 562
Cdd:PRK06334 530 NALA 533
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
204-559 |
5.35e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 125.14 E-value: 5.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 204 VGLEDVAVLQYTGGTTGVSKGAMLTHGNlvanmlqVHAQLSQLGKDGLPLMkeAQEVMIAPLPLYHIYAFTANCMCMMVS 283
Cdd:PRK06060 142 MGGDALAYATYTSGTTGPPKAAIHRHAD-------PLTFVDAMCRKALRLT--PEDTGLCSARMYFAYGLGNSVWFPLAT 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 284 GNHNVLitNPRDIPGFVKELKKWRF--SALLGLNTLFVALMEhpGFKDVDFSNLKLTNSGGTALVSATAERW-KGVTGCT 360
Cdd:PRK06060 213 GGSAVI--NSAPVTPEAAAILSARFgpSVLYGVPNFFARVID--SCSPDSFRSLRCVVSAGEALELGLAERLmEFFGGIP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 361 VVEGYGLTECSPVVTTNPYGEQaRLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEAteeILDAE 440
Cdd:PRK06060 289 ILDGIGSTEVGQTFVSNRVDEW-RLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 441 GWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR-----DP 515
Cdd:PRK06060 365 GWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATsgatiDG 444
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15598496 516 SLsVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:PRK06060 445 SV-MRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
10-466 |
1.28e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 123.93 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 10 RPAGVPD------SLDFAAYRSVVEVFERSCKKFADRPAFS---------------------------NLGVTLSYAELD 56
Cdd:PTZ00216 49 RIAGVTDeeherlRNEWYYGPNFLQRLERICKERGDRRALAyrpvervekevvkdadgkertmevthfNETRYITYAELW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 57 RLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALV-----YLNV 131
Cdd:PTZ00216 129 ERIVNFGRGLA-ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVcngknVPNL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 132 FGKLVEEVLPDTRIEYLiearmgDLLPAlkgwlvnsvvkSVKKMvpDYRLpqaLPFRQALKQGQGHALQ-PVRVGL--ED 208
Cdd:PTZ00216 208 LRLMKSGGMPNTTIIYL------DSLPA-----------SVDTE--GCRL---VAWTDVVAKGHSAGSHhPLNIPEnnDD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQL-GKdglplmKEAQEVMIAPLPLYHIYAFTANCMcMMVSGNHn 287
Cdd:PTZ00216 266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLiGP------PEEDETYCSYLPLAHIMEFGVTNI-FLARGAL- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLITNPRDIPG-FVK---ELKKWRFSALLGLNTLF------------------------------VAL---MEHPGFKDV 330
Cdd:PTZ00216 338 IGFGSPRTLTDtFARphgDLTEFRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdhayqsrlRALkegKDTPYWNEK 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 331 DFS--------NLKLTNSGGTALVSATAERWKGVTGCtVVEGYGLTEcspvvtTNPYGEQARLGTVGIPVVGTALKVidE 402
Cdd:PTZ00216 418 VFSapravlggRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE------TVCCGGIQRTGDLEPNAVGQLLKG--V 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 403 QGNELPVGE---------RGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDL 466
Cdd:PTZ00216 489 EMKLLDTEEykhtdtpepRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKAL 561
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
25-558 |
4.27e-29 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 120.77 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 25 SVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQkqtDLQPGDRiavqmpnvlqYPIAVFGalraglvvvn 104
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFID---SLKLPDK----------SPIIVFG---------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 105 tnplytaremrHQFKD--AGVRALV-----YLNVfgklvEEVLPDTRIEYLIEARMGDLLPALKGWLVNSV---VKSVKK 174
Cdd:PRK04813 60 -----------HMSPEmlATFLGAVkaghaYIPV-----DVSSPAERIEMIIEVAKPSLIIATEELPLEILgipVITLDE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 175 MVPDYRLPQALPFRQALKQgqghalqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLV--AN-MLQVHAqlsqlgkdgl 251
Cdd:PRK04813 124 LKDIFATGNPYDFDHAVKG-------------DDNYYIIFTSGTTGKPKGVQISHDNLVsfTNwMLEDFA---------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 252 plmKEAQEVMIAPLPlyhiYAFTANCM----CMMVSGNHNVLitnPRDIPGFVKELkkwrFSAL--LGLNTL-----FV- 319
Cdd:PRK04813 181 ---LPEGPQFLNQAP----YSFDLSVMdlypTLASGGTLVAL---PKDMTANFKQL----FETLpqLPINVWvstpsFAd 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 320 -ALMEhPGFKDVDFSNLK--------LTNSGGTALVSA--TAerwkgvtgcTVVEGYGLTECSPVVT----TNPYGEQ-A 383
Cdd:PRK04813 247 mCLLD-PSFNEEHLPNLThflfcgeeLPHKTAKKLLERfpSA---------TIYNTYGPTEATVAVTsieiTDEMLDQyK 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 384 RLgTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEI---LDAEGWLKTGDIAVIDEdgfvriv 460
Cdd:PRK04813 317 RL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAfftFDGQPAYHTGDAGYLED------- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 461 drkkDLILVSG-------FNVYPNEIEDV---VMAHPKVASCAAVgiPDEKSGEAVKL--FVVARDPSLSVE-----ELK 523
Cdd:PRK04813 389 ----GLLFYQGridfqikLNGYRIELEEIeqnLRQSSYVESAVVV--PYNKDHKVQYLiaYVVPKEEDFEREfeltkAIK 462
|
570 580 590
....*....|....*....|....*....|....*
gi 15598496 524 AYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK04813 463 KELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-558 |
6.91e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 119.49 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVAnmlQVHAQLSQLGKdglplmkEAQEVMIAPLPLYHIYAFTANCMCMMVSGNH 286
Cdd:cd05910 85 DEPAAILFTSGSTGTPKGVVYRHGTFAA---QIDALRQLYGI-------RPGEVDLATFPLFALFGPALGLTSVIPDMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLI-TNPRDIPGFvkeLKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERWKGVT--GCTVVE 363
Cdd:cd05910 155 TRPArADPQKLVGA---IRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 364 GYGLTECSPV---------VTTNPYGEQARLGTVGIPVVGTALKVID---------EQGNELPVGERGELCVKGPQVMKG 425
Cdd:cd05910 232 PYGATEALPVssigsrellATTTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 426 YWQRPEAT--EEILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIpdEK 501
Cdd:cd05910 312 YVNRPVATalAKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GK 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 502 SGEAVKLFVVARDPSLSV------EELKAYCKENLTGYKIpRQIVLKDALPMTPV--GKILRREL 558
Cdd:cd05910 390 PGCQLPVLCVEPLPGTITprarleQELRALAKDYPHTQRI-GRFLIHPSFPVDIRhnAKIFREKL 453
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
207-558 |
1.46e-28 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 118.69 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglplmKEAQEVMIA-PLPLYHIYAftancmcMMVSGN 285
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSD-----RVLQFASIAfDVAAEEIYV-------TLLSGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 286 HNVLITNP--RDIPGFVKELKKWRFSaLLGLNTLFVALMEHPGFKDVD--FSNLKLTNSGGTALVSATAERWKGVTG--C 359
Cdd:cd17644 174 TLVLRPEEmrSSLEDFVQYIQQWQLT-VLSLPPAYWHLLVLELLLSTIdlPSSLRLVIVGGEAVQPELVRQWQKNVGnfI 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 360 TVVEGYGLTECSPVVT----TNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE 435
Cdd:cd17644 253 QLINVYGPTEATIAATvcrlTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 436 --ILDA------EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVK 507
Cdd:cd17644 333 kfISHPfnssesERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLV 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15598496 508 LFVVARDP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17644 413 AYIVPHYEeSPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
49-502 |
1.63e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 119.66 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQTDlqPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLYTARemrhqfkdAGVRalvy 128
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAGLIAV---PLSVPQ--------GGAH---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 lnvfgklveevlpDTRIEylieARMGDLLPALKgwLVNS-VVKSVKKMVPDYRLPQALPFRQ--ALKQGQGHALQPVRVG 205
Cdd:PRK05850 98 -------------DERVS----AVLRDTSPSVV--LTTSaVVDDVTEYVAPQPGQSAPPVIEvdLLDLDSPRGSDARPRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 206 LEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAqlSQLG-KDGLPlmkEAQEVMIAPLPLYHIYAFTANCMCMMVSG 284
Cdd:PRK05850 159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMS--DYFGdTGGVP---PPDTTVVSWLPFYHDMGLVLGVCAPILGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 285 NHNVLiTNPRdipGFVKelKKWRFSALLGLNTL-FVALmehPGF---------KDVDFSNLKLtnsGGTALVSATAERWK 354
Cdd:PRK05850 234 CPAVL-TSPV---AFLQ--RPARWMQLLASNPHaFSAA---PNFafelavrktSDDDMAGLDL---GGVLGIISGSERVH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 355 GVTGCTVVE--------------GYGLTECSPVVTTNPYGE---------------QARLGTVGipvVGTAL-------- 397
Cdd:PRK05850 302 PATLKRFADrfapfnlretairpSYGLAEATVYVATREPGQppesvrfdyeklsagHAKRCETG---GGTPLvsygsprs 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 398 ---KVIDEQGN-ELPVGERGELCVKGPQVMKGYWQRPEATEEILDA----------EG-WLKTGDIAVIDEDGFVrIVDR 462
Cdd:PRK05850 379 ptvRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgtpEGpWLRTGDLGFISEGELF-IVGR 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15598496 463 KKDLILVSGFNVYPNEIEDVVMAHPKvASCAAVGIPDEKS 502
Cdd:PRK05850 458 IKDLLIVDGRNHYPDDIEATIQEITG-GRVAAISVPDDGT 496
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
25-559 |
3.09e-28 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 119.08 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 25 SVVEVFERSCKKFADRPAFSNL---------GVTLSYAELDRLSAAFAAYLQKQTdlQPGDRIAVQMPNVLQYPIAVFGA 95
Cdd:PRK12476 35 TLISLIERNIANVGDTVAYRYLdhshsaagcAVELTWTQLGVRLRAVGARLQQVA--GPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 96 LRAGLVVVntnPLYT------AREMRHQFKDAGVRALVYLNVFGKLVEEVLpdtrieyliearmgDLLPALKGWLVNSVv 169
Cdd:PRK12476 113 IKAGTIAV---PLFApelpghAERLDTALRDAEPTVVLTTTAAAEAVEGFL--------------RNLPRLRRPRVIAI- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 170 ksvkKMVPDyrlpqalpfrqalkqGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKD 249
Cdd:PRK12476 175 ----DAIPD---------------SAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 250 glplmkeAQEVmiAPLPLYHIYAFTancMCMM--VSGNHNVLITnprdiP-GFVKELKKWrFSALLGLNTLFVALMEHPG 326
Cdd:PRK12476 236 -------THGV--SWLPLYHDMGLS---MIGFpaVYGGHSTLMS-----PtAFVRRPQRW-IKALSEGSRTGRVVTAAPN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 327 F--------------KDVDFSNLKLTNsgGTALVSATAERW-------KGVTGCTVVEGYGLTECSPVVTTNP------- 378
Cdd:PRK12476 298 FayewaaqrglpaegDDIDLSNVVLII--GSEPVSIDAVTTfnkafapYGLPRTAFKPSYGIAEATLFVATIApdaepsv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 379 -YGEQARLGT-VGIPVVGT------------------ALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPEATEEILD 438
Cdd:PRK12476 376 vYLDREQLGAgRAVRVAADapnavahvscgqvarsqwAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 439 A-------EG-----------WLKTGDIAVIdEDGFVRIVDRKKDLILVSGFNVYPNEIE-DVVMAHPKVAS--CAAVGI 497
Cdd:PRK12476 456 AklqsrlaEGshadgaaddgtWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEaTVAEASPMVRRgyVTAFTV 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 498 PDEKSGEAVklfVVAR--------DPSLSVEELKAYCKENltgYKIPR---QIVLKDALPMTPVGKILRRELR 559
Cdd:PRK12476 535 PAEDNERLV---IVAEraagtsraDPAPAIDAIRAAVSRR---HGLAVadvRLVPAGAIPRTTSGKLARRACR 601
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
210-483 |
7.53e-28 |
|
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: 117.84 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVanmLQVHAqLSQLGKDGLPLMKeaQEVMIAPLPLYHIYAFTANC-MCMMVSGNhnV 288
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNIT---WTAKA-ASQHMDLRPATVG--QESVVSYLPLSHIAAQILDIwLPIKVGGQ--V 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 289 LITNPRDIPG-FVKELKKWRFSALLGLNTLFVALMEH--------PGFKDVDFS---------NLKLTNSG-------GT 343
Cdd:cd05933 225 YFAQPDALKGtLVKTLREVRPTAFMGVPRVWEKIQEKmkavgaksGTLKRKIASwakgvgletNLKLMGGEspsplfyRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 344 A--LVSATAERWKGVTGCT-----------------------VVEGYGLTECS-PVVTTNPYGeqARLGTVGIPVVGTAL 397
Cdd:cd05933 305 AkkLVFKKVRKALGLDRCQkfftgaapisretlefflslnipIMELYGMSETSgPHTISNPQA--YRLLSCGKALPGCKT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 398 KVIDEQGNELpvgerGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYP 476
Cdd:cd05933 383 KIHNPDADGI-----GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPP 457
|
....*..
gi 15598496 477 NEIEDVV 483
Cdd:cd05933 458 VPIEDAV 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-558 |
1.23e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.91 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLqKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF 118
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRL-RARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYML 2096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 KDAGVRALVYLNvfgKLVEEVLPDTRIEYLIEARMGDLlpalkgwlvnsvvksvkkmvPDYrlPQALPfrqalkqgqgha 198
Cdd:PRK12316 2097 EDSGAALLLTQR---HLLERLPLPAGVARLPLDRDAEW--------------------ADY--PDTAP------------ 2139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmLQVHAQLSQLGkdglPLMKEAQEVMIAplplyhIYAFTANCM 278
Cdd:PRK12316 2140 --AVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH-CQAAGERYELS----PADCELQFMSFS------FDGAHEQWF 2206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNhNVLITNP--RDIPGFVKELKKWRFSALLGLNTLFVALMEHPGfKDVDFSNLKLTNSGGTALVSATAER-WKG 355
Cdd:PRK12316 2207 HPLLNGA-RVLIRDDelWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE-RDGRPPAVRVYCFGGEAVPAASLRLaWEA 2284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 356 VTGCTVVEGYGLTECSPVVTTNPYGEQARLGTVGIPVvGTALK-----VIDEQGNELPVGERGELCVKGPQVMKGYWQRP 430
Cdd:PRK12316 2285 LRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPI-GRALGnrrayILDADLNLLAPGMAGELYLGGEGLARGYLNRP 2363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 431 EATEE-----ILDAEGWL--KTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIpDEKSG 503
Cdd:PRK12316 2364 GLTAErfvpdPFSASGERlyRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASG 2442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 504 EAVKLFVVARDP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:PRK12316 2443 KQLVAYVVPDDAaEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
208-470 |
1.42e-27 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 117.22 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLgKDGLplmkEAQEVMIAPLPLYHI-------YAFTANCMCM 280
Cdd:PLN02430 221 DICTIMYTSGTSGDPKGVVLTHEAVATFVRGVDLFMEQF-EDKM----THDDVYLSFLPLAHIldrmieeYFFRKGASVG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 281 MVSGNHNVLitnpRD------------IPGFVKELKKWRFSALLGLNTL----FVALMEHP------GFKD------VDF 332
Cdd:PLN02430 296 YYHGDLNAL----RDdlmelkptllagVPRVFERIHEGIQKALQELNPRrrliFNALYKYKlawmnrGYSHkkaspmADF 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 333 -----------SNLKLTNSGGTALvSATAERWKGVTGCT-VVEGYGLTE-CSPVVTTNPyGEQARLGTVGIPVVGTALKV 399
Cdd:PLN02430 372 lafrkvkaklgGRLRLLISGGAPL-STEIEEFLRVTSCAfVVQGYGLTEtLGPTTLGFP-DEMCMLGTVGAPAVYNELRL 449
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 400 --IDEQGNElPVGE--RGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS 470
Cdd:PLN02430 450 eeVPEMGYD-PLGEppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLS 522
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
199-560 |
1.53e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 116.38 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 LQPVR-VGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhAQLSQLGKDGLPlmkeaqeVMIAPLPLYH-------- 269
Cdd:cd05915 144 EADPVrVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAA-SLVDGTALSEKD-------VVLPVVPMFHvnawclpy 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 270 -IYAFTANCMCMMVSGNHNV---------------------LITNPRDIpgfVKELKKWRFSALLGLNTLFVALmehpgf 327
Cdd:cd05915 216 aATLVGAKQVLPGPRLDPASlvelfdgegvtftagvptvwlALADYLES---TGHRLKTLRRLVVGGSAAPRSL------ 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 328 kdvdfsnLKLTNSGGTALVSATaerwkgvtGCTVVEGYGlTEC--SPVVTTNPYGEQARLGTV-GIPVVGTALKVIDEQG 404
Cdd:cd05915 287 -------IARFERMGVEVRQGY--------GLTETSPVV-VQNfvKSHLESLSEEEKLTLKAKtGLPIPLVRLRVADEEG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGERG--ELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDV 482
Cdd:cd05915 351 RPVPKDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENA 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 483 VMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYK-IPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05915 431 LMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
50-524 |
2.94e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 116.30 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQ------------ 117
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDL-GLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAklkhlfdlvkpr 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 118 --FKDAGV---RALVYLNVFGklVEEVLPDTRIEYLIEARMGDLLpalkgwlvnsvvksvkkmvpdyrlpqALPFRQALK 192
Cdd:PRK12582 160 vvFAQSGApfaRALAALDLLD--VTVVHVTGPGEGIASIAFADLA--------------------------ATPPTAAVA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 193 QGqgHAlqpvRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANmLQVHAQLSQLGKDGLPlmkeaqEVMIAPLPLYHIYA 272
Cdd:PRK12582 212 AA--IA----AITPDTVAKYLFTSGSTGMPKAVINTQRMMCAN-IAMQEQLRPREPDPPP------PVSLDWMPWNHTMG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 273 FTANCMCMMVSGNhNVLITNPRDIPG-FVKELKKWR-------FSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTA 344
Cdd:PRK12582 279 GNANFNGLLWGGG-TLYIDDGKPLPGmFEETIRNLReisptvyGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 LVSATAERWKGV----TGCTVV--EGYGLTECSPVvTTNPYGEQARLGTVGIPVVGTALKVIdeqgnelPVGERGELCVK 418
Cdd:PRK12582 358 LSDDLYERMQALavrtTGHRIPfyTGYGATETAPT-TTGTHWDTERVGLIGLPLPGVELKLA-------PVGDKYEVRVK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 419 GPQVMKGYWQRPEATEEILDAEGWLKTGDIAV-IDED----GFV---RIVDrkkDLILVSGFNVYPNE------------ 478
Cdd:PRK12582 430 GPNVTPGYHKDPELTAAAFDEEGFYRLGDAARfVDPDdpekGLIfdgRVAE---DFKLSTGTWVSVGTlrpdavaacspv 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15598496 479 IEDVVMAHPKVASCAAVGIPDEKSGEAvklfvVARDPSLSVEELKA 524
Cdd:PRK12582 507 IHDAVVAGQDRAFIGLLAWPNPAACRQ-----LAGDPDAAPEDVVK 547
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
365-562 |
1.23e-26 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 112.78 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 YGLTE-CSPVVTTNPygEQARLGTVGipvVGTAL---KVideqgnELPVGERGELCVKGPQVMKGYWQrpeateEILDAE 440
Cdd:PRK07445 261 YGMTEtASQIATLKP--DDFLAGNNS---SGQVLphaQI------TIPANQTGNITIQAQSLALGYYP------QILDSQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 441 GWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVE 520
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE 403
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598496 521 ELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK07445 404 ELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
49-496 |
1.76e-26 |
|
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: 113.67 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQkQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLYtaremrhqfKDAGVRALVY 128
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSL---GIY---------QDSMAEEVAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 LNVFGKLVEEVLPDT-RIEYLIEarMGDLLPalkgwLVNSVVKSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGL- 206
Cdd:cd17641 78 LLNYTGARVVIAEDEeQVDKLLE--IADRIP-----SVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLYEr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 -------EDVAVLQYTGGTTGVSKGAMLTHGNLVANmlqvhaqlsqlGKDGL---PLMKEAQEVMIAPLP--LYHIYA-- 272
Cdd:cd17641 151 evaagkgEDVAVLCTTSGTTGKPKLAMLSHGNFLGH-----------CAAYLaadPLGPGDEYVSVLPLPwiGEQMYSvg 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 273 ------FTANCM----CMMVS----GNHNVLITnPR--------------DIPGFVKELKKWRFSALL-GLNT------- 316
Cdd:cd17641 220 qalvcgFIVNFPeepeTMMEDlreiGPTFVLLP-PRvwegiaadvrarmmDATPFKRFMFELGMKLGLrALDRgkrgrpv 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 --------------LFVALMEHPGFkdvdfSNLKLTNSGGTALVSATAERWKGVtGCTVVEGYGLTECSPVVTTNPYGeQ 382
Cdd:cd17641 299 slwlrlaswladalLFRPLRDRLGF-----SRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDG-D 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 383 ARLGTVGIPVVGTALKVIdeqgnelpvgERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDR 462
Cdd:cd17641 372 VDPDTVGVPFPGTEVRID----------EVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDR 441
|
490 500 510
....*....|....*....|....*....|....*
gi 15598496 463 KKDLILVS-GFNVYPNEIEDVVMAHPKVASCAAVG 496
Cdd:cd17641 442 AKDVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
24-560 |
2.34e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 113.43 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 24 RSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVV- 102
Cdd:PRK08279 37 RSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVVa 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 103 -VNTN----PLytaremRHQFKDAGVRALVylnvfgkLVEEVLPdtrieyLIEARMGDLLPALKGWLVNSVVKsvkkmvp 177
Cdd:PRK08279 116 lLNTQqrgaVL------AHSLNLVDAKHLI-------VGEELVE------AFEEARADLARPPRLWVAGGDTL------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 178 dyrlpQALPFRQALKQ---GQGHALQPVR--VGLEDVAVLQYTGGTTGVSKGAMLTHGNlVANMLQVHAQLSQLGKDglp 252
Cdd:PRK08279 170 -----DDPEGYEDLAAaaaGAPTTNPASRsgVTAKDTAFYIYTSGTTGLPKAAVMSHMR-WLKAMGGFGGLLRLTPD--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 253 lmkeaqEVMIAPLPLYHIYAFTAnCMCMMVSGNHNVLITNPRDIPGFVKELKKWRFsallglnTLFVA-------LMEHP 325
Cdd:PRK08279 241 ------DVLYCCLPLYHNTGGTV-AWSSVLAAGATLALRRKFSASRFWDDVRRYRA-------TAFQYigelcryLLNQP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 326 GfKDVDFSNlKLTNSGGTALvsaTAERWK------GVTGctVVEGYGLTECSpVVTTNPYGeqaRLGTVGI-------PV 392
Cdd:PRK08279 307 P-KPTDRDH-RLRLMIGNGL---RPDIWDefqqrfGIPR--ILEFYAASEGN-VGFINVFN---FDGTVGRvplwlahPY 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 393 ------VGTALKVIDEQGNELPV--GERGELC--VKGPQVMKGYWQrPEATEE-IL-------DAegWLKTGDIAVIDED 454
Cdd:PRK08279 376 aivkydVDTGEPVRDADGRCIKVkpGEVGLLIgrITDRGPFDGYTD-PEASEKkILrdvfkkgDA--WFNTGDLMRDDGF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 455 GFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVG--IP--DEKSGEAVklFVVARDPSLSVEELKAYCKENL 530
Cdd:PRK08279 453 GHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGveVPgtDGRAGMAA--IVLADGAEFDLAALAAHLYERL 530
|
570 580 590
....*....|....*....|....*....|
gi 15598496 531 TGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK08279 531 PAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
49-471 |
5.08e-26 |
|
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: 112.14 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAR-----EMRHQFkDAGV 123
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMsqdlaKLKHLF-ELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 124 RALVYLN---VFGKLVEEVLPDTrieyliearmgdlLPALkgwlvnsvvkSVKKMVPDYRlpqALPFRQALKQGQGHALQ 200
Cdd:cd05921 103 PGLVFAQdaaPFARALAAIFPLG-------------TPLV----------VSRNAVAGRG---AISFAELAATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 201 PV--RVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMlqvhAQLSQLgkdgLPLMKEAQEVMIAPLPLYHIYAFTANCM 278
Cdd:cd05921 157 AAfaAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQ----AMLEQT----YPFFGEEPPVLVDWLPWNHTFGGNHNFN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNhNVLITNPRDIPGF----VKELKK----WRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATA 350
Cdd:cd05921 229 LVLYNGG-TLYIDDGKPMPGGfeetLRNLREisptVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVW 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 351 ERWKGVTGCTVVE------GYGLTECSPVvTTNPYGEQARLGTVGIPVVGTALKVIdeqgnelPVGERGELCVKGPQVMK 424
Cdd:cd05921 308 DRLQALAVATVGEripmmaGLGATETAPT-ATFTHWPTERSGLIGLPAPGTELKLV-------PSGGKYEVRVKGPNVTP 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 425 GYWQRPEATEEILDAEGWLKTGDIA--VIDED---GFV---RIVDrkkDLILVSG 471
Cdd:cd05921 380 GYWRQPELTAQAFDEEGFYCLGDAAklADPDDpakGLVfdgRVAE---DFKLASG 431
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
386-562 |
5.99e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 112.16 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 386 GTVGIPVVGTALKVIDEQGNELPVGERGELCVKG--PQVMKGYWQRPEATEEIL--DAEGWLKTGDIAVIDEDGFVRIVD 461
Cdd:PRK00174 424 GSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYGDHERFVKTYfsTFKGMYFTGDGARRDEDGYYWITG 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 462 RKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD---PSLS-VEELKAYCKENLTGYKIPR 537
Cdd:PRK00174 504 RVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGgeePSDElRKELRNWVRKEIGPIAKPD 583
|
170 180
....*....|....*....|....*
gi 15598496 538 QIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK00174 584 VIQFAPGLPKTRSGKIMRRILRKIA 608
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
15-558 |
1.01e-25 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 112.95 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 15 PDSLDFAAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFG 94
Cdd:PRK05691 2179 GEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLA 2257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 95 ALRAGLVVVNTNPLYTAREMRHQFKDAGVRALV-YLNVFGKLVEevLPDTRIEYLIEarmgDLLPALKGWlvnsvvksvk 173
Cdd:PRK05691 2258 ILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLsDRALFEALGE--LPAGVARWCLE----DDAAALAAY---------- 2321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 174 kmvPDYRLPqalpfRQALKQGQghalqpvrvgledvAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglpl 253
Cdd:PRK05691 2322 ---SDAPLP-----FLSLPQHQ--------------AYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADD---- 2375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 254 mkeaqevmiAPLPLYHIY--AFTANCMCMMVSGNHNVLIT----NPRDIPGFVKELKkwrfSALLGLNTLFVALMEHPGF 327
Cdd:PRK05691 2376 ---------CELHFYSINfdAASERLLVPLLCGARVVLRAqgqwGAEEICQLIREQQ----VSILGFTPSYGSQLAQWLA 2442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 328 KDVDFSNLKLTNSGGTALvsaTAERWKGVTGCTVVE----GYGLTECSPVVTTNPYGEQARLGTVGIP---VVGTALKVI 400
Cdd:PRK05691 2443 GQGEQLPVRMCITGGEAL---TGEHLQRIRQAFAPQlffnAYGPTETVVMPLACLAPEQLEEGAASVPigrVVGARVAYI 2519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 401 -DEQGNELPVGERGELCVKGPQVMKGYWQRPEATEE-----ILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGF 472
Cdd:PRK05691 2520 lDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAErfvadPFAADGgrLYRTGDLVRLRADGLVEYVGRIDHQVKIRGF 2599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 473 NVYPNEIEDVVMAHPKVAScAAVGIPDEKSGEAVKLFVVARDPSLSVEE-------LKAYCKENLTGYKIPRQIVLKDAL 545
Cdd:PRK05691 2600 RIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDSL 2678
|
570
....*....|...
gi 15598496 546 PMTPVGKILRREL 558
Cdd:PRK05691 2679 PLTANGKLDRRAL 2691
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
186-489 |
6.73e-25 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 109.05 E-value: 6.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 186 PFRQALKQGQGHALQPVRVGLEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKdglplmkeaQEVMIAPL 265
Cdd:PLN02387 229 SFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGK---------NDVYLAYL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 266 PLYHIYAFTANCMcMMVSG-----------------------------NHNVLITNP------RD--------IPGFVKE 302
Cdd:PLN02387 300 PLAHILELAAESV-MAAVGaaigygspltltdtsnkikkgtkgdasalKPTLMTAVPaildrvRDgvrkkvdaKGGLAKK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 303 L----KKWRFSAL-------LGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALvSATAERWKGVT-GCTVVEGYGLTE- 369
Cdd:PLN02387 379 LfdiaYKRRLAAIegswfgaWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPL-SGDTQRFINIClGAPIGQGYGLTEt 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 370 CSPVVTTNPygEQARLGTVGIPVVGTALKVID-EQGNEL----PVgERGELCVKGPQVMKGYWQRPEATEEI--LDAEG- 441
Cdd:PLN02387 458 CAGATFSEW--DDTSVGRVGPPLPCCYVKLVSwEEGGYLisdkPM-PRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGm 534
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15598496 442 -WLKTGDIAVIDEDGFVRIVDRKKDLI-LVSGFNVYPNEIEDVVMAHPKV 489
Cdd:PLN02387 535 rWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAALSVSPYV 584
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
39-558 |
2.62e-24 |
|
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: 105.95 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 39 DRPAFSNLGVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYtaremrhqf 118
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 119 kdagvralvylnvfgklveevlPDTRIEYLIEArmgdllPALKGWLVNSvvksvkkmvpdyrlpqalpfrqalkqgqgha 198
Cdd:cd17648 73 ----------------------PDERIQFILED------TGARVVITNS------------------------------- 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 199 lqpvrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVanmlQVHAQLSQLgkdgLPLMKEAQEVmIAPLPLYhIYAFTANCM 278
Cdd:cd17648 94 --------TDLAYAIYTSGTTGKPKGVLVEHGSVV----NLRTSLSER----YFGRDNGDEA-VLFFSNY-VFDFFVEQM 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 279 CMMVSGNHNVLITNPR---DIPGFVKELKKWRFSALLGLNTLFvalmehpgfKDVDFS---NLKLTNSGGTALVSATAER 352
Cdd:cd17648 156 TLALLNGQKLVVPPDEmrfDPDRFYAYINREKVTYLSGTPSVL---------QQYDLArlpHLKRVDAAGEEFTAPVFEK 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 353 WKGVTGCTVVEGYGLTECSPVVTTNPYGEQARL-GTVGIPVVGTALKVIDEQGNELPVGERGELCVKGPQVMKGYWQRPE 431
Cdd:cd17648 227 LRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPE 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 432 AT------------EEILDAEG--WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGI 497
Cdd:cd17648 307 LTaerflpnpfqteQERARGRNarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 498 PDEKSGEAVKL-----FVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17648 387 EDASQAQSRIQkylvgYYLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-562 |
3.65e-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: 105.34 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQF-KDAGVRALVy 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSI-GVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVdRGGAVYAAV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 129 lnvfgklvEEVLpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqgHALQPVrvgled 208
Cdd:cd05974 79 --------DENT--------------------------------------------------------HADDPM------ 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 vaVLQYTGGTTGVSKGAMLTHGNLVANMLQ-----------VHAQLSQLGkdglpLMKEAQEVMIAPLPlyhiyaftanc 277
Cdd:cd05974 89 --LLYFTSGTTSKPKLVEHTHRSYPVGHLStmywiglkpgdVHWNISSPG-----WAKHAWSCFFAPWN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 mcmmvSGNHNVLITNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHP--GFKdvdfSNLKLTNSGGTALVSATAERWK 354
Cdd:cd05974 151 -----AGATVFLFNYARfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDlaSFD----VKLREVVGAGEPLNPEVIEQVR 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 355 GVTGCTVVEGYGLTECSPVVTTNPyGEQARLGTVGIPVVGTALKVIDEQGNelPVGErGELCV-----KGPQVMKGYWQR 429
Cdd:cd05974 222 RAWGLTIRDGYGQTETTALVGNSP-GQPVKAGSMGRPLPGYRVALLDPDGA--PATE-GEVALdlgdtRPVGLMKGYAGD 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 430 PEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLF 509
Cdd:cd05974 298 PDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAF 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 510 VV-----ARDPSLSVEELKaYCKENLTGYKIPRQIVLKDaLPMTPVGKILRRELREIA 562
Cdd:cd05974 377 IVlragyEPSPETALEIFR-FSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
38-562 |
1.22e-23 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 105.03 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAF------SNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLV--VV------ 103
Cdd:PRK10524 67 PEQLALiavsteTDEERTYTFRQLHDEVNRMAAMLRSL-GVQRGDRVLIYMPMIAEAAFAMLACARIGAIhsVVfggfas 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 104 --------NTNP--LYTAremrhqfkDAGVRAlvylnvfGKLVE-EVLPDTRIEyLIEARMGDLLpalkgwLVNsvvksv 172
Cdd:PRK10524 146 hslaaridDAKPvlIVSA--------DAGSRG-------GKVVPyKPLLDEAIA-LAQHKPRHVL------LVD------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 173 KKMVPDYRLPQALPFRQALKQGQGHALQPVrVGLE--DVAVLQYTGGTTGVSKGAMLTHGN----LVANMLQVHAqlsql 246
Cdd:PRK10524 198 RGLAPMARVAGRDVDYATLRAQHLGARVPV-EWLEsnEPSYILYTSGTTGKPKGVQRDTGGyavaLATSMDTIFG----- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 247 GKDGlplmkeaqEVMIAPLPL-------YHIYA-FTANCMCMMVSGnhnvLITNPRdiPGFVkelkkWRFSALLGLNTLF 318
Cdd:PRK10524 272 GKAG--------ETFFCASDIgwvvghsYIVYApLLAGMATIMYEG----LPTRPD--AGIW-----WRIVEKYKVNRMF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 319 VA------LMEHPG--FKDVDFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTECS-PVVTTNPYGEQA--RLGT 387
Cdd:PRK10524 333 SAptairvLKKQDPalLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGwPILAIARGVEDRptRLGS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 388 VGIPVVGTALKVIDEQ-GNELPVGERGELCVKGP--------------QVMKGYWqrpEATEEILDAegwlkTGDIAVID 452
Cdd:PRK10524 413 PGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIEGPlppgcmqtvwgdddRFVKTYW---SLFGRQVYS-----TFDWGIRD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 453 EDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPS--------LSVE-ELK 523
Cdd:PRK10524 485 ADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDsladrearLALEkEIM 564
|
570 580 590
....*....|....*....|....*....|....*....
gi 15598496 524 AYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PRK10524 565 ALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQAIA 603
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
21-560 |
1.21e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 103.32 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 21 AAYRSVVEVFERSCKKFADRPAFSNLGVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGL 100
Cdd:PRK05691 1128 PAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDK-GVGPDVCVAIAAERSPQLLVGLLAILKAGG 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 101 VVVNTNPLYTAREMRHQFKDAGVRALvylnvfgklveevlpdtrieyLIEARMGDLLPALKGwlVNSVVKSVKKMvpdyr 180
Cdd:PRK05691 1207 AYVPLDPDYPAERLAYMLADSGVELL---------------------LTQSHLLERLPQAEG--VSAIALDSLHL----- 1258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 181 lpqalpfrqalkqgQGHALQPVRVGL--EDVAVLQYTGGTTGVSKGAMLTHGNLvANMLQVHAQLSQLGKDGLPLMKeaq 258
Cdd:PRK05691 1259 --------------DSWPSQAPGLHLhgDNLAYVIYTSGSTGQPKGVGNTHAAL-AERLQWMQATYALDDSDVLMQK--- 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 259 evmiAPLplyhiyAFTAN---CMCMMVSGNHNVLIT-----NPRDIPGFVKELKKWRFSALLGLNTLFValmEHPGFKDV 330
Cdd:PRK05691 1321 ----API------SFDVSvweCFWPLITGCRLVLAGpgehrDPQRIAELVQQYGVTTLHFVPPLLQLFI---DEPLAAAC 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 331 dfSNLKLTNSGGTALVSATAER-WKGVTGCTVVEGYGLTECSPVVTT-NPYGEQARLGTVGIPVVGTALKVIDEQGNELP 408
Cdd:PRK05691 1388 --TSLRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVTHwQCQAEDGERSPIGRPLGNVLCRVLDAELNLLP 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 409 VGERGELCVKGPQVMKGYWQRPEATEE--ILDAEG-----WLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIED 481
Cdd:PRK05691 1466 PGVAGELCIGGAGLARGYLGRPALTAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQA 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 482 VVMAHPKVAScAAVGIPDEKSG-EAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:PRK05691 1546 RLLAQPGVAQ-AAVLVREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
430-562 |
5.49e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 98.57 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 430 PEATEEIL--DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVK 507
Cdd:PRK08308 278 ENAPEEIVvkMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVK 357
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598496 508 LFVVARDPsLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRR--ELREIA 562
Cdd:PRK08308 358 AKVISHEE-IDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKllELGEVT 413
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
208-504 |
9.62e-22 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 99.15 E-value: 9.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 208 DVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKdglplMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHN 287
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDR-----VATEEDSYFSYLPLAHVYDQVIETYCISKGASIG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 288 VLITNPRDIPGFVKELKK-------------------------------WRFSALLGLNTLFVALMEH---PGFKDVDFS 333
Cdd:PLN02861 296 FWQGDIRYLMEDVQALKPtifcgvprvydriytgimqkissggmlrkklFDFAYNYKLGNLRKGLKQEeasPRLDRLVFD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 334 NLKLTNSG-------GTALVSATAERWKGVTGC-TVVEGYGLTECSPVVTTNPYGEQARLGTVGIPV--VGTALKVIDEQ 403
Cdd:PLN02861 376 KIKEGLGGrvrlllsGAAPLPRHVEEFLRVTSCsVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMttIEARLESVPEM 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 404 G-NELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS-GFNVYPNEIED 481
Cdd:PLN02861 456 GyDALSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYVAVENLEN 534
|
330 340 350
....*....|....*....|....*....|....
gi 15598496 482 VVMAHPKVASC-----------AAVGIPDEKSGE 504
Cdd:PLN02861 535 TYSRCPLIASIwvygnsfesflVAVVVPDRQALE 568
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
191-482 |
2.18e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 98.17 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 191 LKQGQGHALQ-PVRVGlEDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVhaqLSQLGKDGLPLmkEAQEVMIAPLPLYH 269
Cdd:PLN02614 207 LKLGEGKQYDlPIKKK-SDICTIMYTSGTTGDPKGVMISNESIVTLIAGV---IRLLKSANAAL--TVKDVYLSYLPLAH 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 270 IY-AFTANCMCMMVS------GNHNVLITN------------PRDI----PGFVKEL------KKWRFSALLGLNTLFVA 320
Cdd:PLN02614 281 IFdRVIEECFIQHGAaigfwrGDVKLLIEDlgelkptifcavPRVLdrvySGLQKKLsdggflKKFVFDSAFSYKFGNMK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 321 -----LMEHPGFKDVDFS--------NLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTE-CSPVVTTNPyGEQARLG 386
Cdd:PLN02614 361 kgqshVEASPLCDKLVFNkvkqglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEsCAGTFVSLP-DELDMLG 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 387 TVGIPV--VGTALKVIDEQG-NELPVGERGELCVKGPQVMKGYWQRPEATEEILdAEGWLKTGDIAVIDEDGFVRIVDRK 463
Cdd:PLN02614 440 TVGPPVpnVDIRLESVPEMEyDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRK 518
|
330 340
....*....|....*....|
gi 15598496 464 KDLI-LVSGFNVYPNEIEDV 482
Cdd:PLN02614 519 KNIFkLSQGEYVAVENIENI 538
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
478-552 |
3.20e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 84.90 E-value: 3.20e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598496 478 EIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARD-PSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGK 552
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
47-559 |
4.34e-18 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 87.40 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVntnPLytarEMRHQFKDAG---- 122
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPI---PI----EPPDISQQLGfllg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 123 -VRALVYLNVFGKLVEevlPDTRIEYLIEArmgDLLPALKGWLVNSVVKSVKKMVPDYRLPQALPFRQALkqgqghalqp 201
Cdd:cd05905 85 tCKVRVALTVEACLKG---LPKKLLKSKTA---AEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRD---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 202 vrvglEDVAVLQYTGGTTGVSKGAMLTHGNLVANMlQVHAQLSQLGKDglplmkeaqEVMIAPLPLYHIYAFTANCMCMM 281
Cdd:cd05905 149 -----GDTAYIEYSFSSDGSLSGVAVSHSSLLAHC-RALKEACELYES---------RPLVTVLDFKSGLGLWHGCLLSV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 282 VSGNHNVLI------TNPrdiPGFVKELKKWR-FSALLGLNTLFVALMEHPGF------KDVDFSNLKLtnsggtaLVSA 348
Cdd:cd05905 214 YSGHHTILIppelmkTNP---LLWLQTLSQYKvRDAYVKLRTLHWCLKDLSSTlaslknRDVNLSSLRM-------CMVP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 349 TAERW----------------------KGVTGCTV--------------VEGY----GLTECSPVVTTNPYGEQARLGTV 388
Cdd:cd05905 284 CENRPrisscdsflklfqtlglspravSTEFGTRVnpficwqgtsgpepSRVYldmrALRHGVVRLDERDKPNSLPLQDS 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 389 GIPVVGTALKVIDEQGNEL-PVGERGELCVKGPQVMKGYWQRPEATEEILDAE------------GWLKTGDIAVI---- 451
Cdd:cd05905 364 GKVLPGAQVAIVNPETKGLcKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFpstrlstgitnnSYARTGLLGFLrptk 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 452 ------DEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMA-HPKVASCAAVGIpdeksgeAVKLFVVARDPSLSVEELKA 524
Cdd:cd05905 444 ctdlnvEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRvHPYRGRCAVFSI-------TGLVVVVAEQPPGSEEEALD 516
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15598496 525 Y----CKENLTGYKIPRQIVL---KDALPMTPVGKILRRELR 559
Cdd:cd05905 517 LvplvLNAILEEHQVIVDCVAlvpPGSLPKNPLGEKQRMEIR 558
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
49-560 |
4.35e-18 |
|
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: 87.02 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 49 TLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVV--VNTNplYTAREMRHQFKDAGVRAL 126
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAalINYN--LRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 VYlnvfgklveevlpdtrieyliearmgdllpalkgwlvnsvvksvkkmvpdyrlpqalpfrqalkqgqghalqpvrvgl 206
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 eDVAVLQYTGGTTGVSKGAMLTHGNLVaNMLQVHAqlsqlgkdGLPLMKeAQEVMIAPLPLYH----IYAFTAncmcMMV 282
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFA--------GSGGAL-PSDVLYTCLPLYHstalIVGWSA----CLA 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGNhNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGfKDVDFSNlKLTNSGGTALVSATAERWK---GVTgc 359
Cdd:cd05940 147 SGA-TLVIRKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPP-KPTERKH-KVRMIFGNGLRPDIWEEFKerfGVP-- 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 360 TVVEGYGLTECSpVVTTNPYGeqaRLGTVG----IPVVGTALKVI-----------DEQG--NELPVGERGELC--VKGP 420
Cdd:cd05940 222 RIAEFYAATEGN-SGFINFFG---KPGAIGrnpsLLRKVAPLALVkydlesgepirDAEGrcIKVPRGEPGLLIsrINPL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMKGYWQRPEATEEIL-----DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:cd05940 298 EPFDGYTDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVY 377
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598496 496 GIP----DEKSGEAVklFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05940 378 GVQvpgtDGRAGMAA--IVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRN 444
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
47-548 |
2.05e-17 |
|
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: 85.42 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRAL 126
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 127 VYLNVFGKLVEEVLP-----DTRIEYLIE----ARMGDLLPALKGwlvnsvvksvkkmVPDYRLPQALPFRQALKqgqgh 197
Cdd:cd05938 83 VVAPELQEAVEEVLPalradGVSVWYLSHtsntEGVISLLDKVDA-------------ASDEPVPASLRAHVTIK----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 198 alqpvrvgleDVAVLQYTGGTTGVSKGAMLTHGNLvanmLQVHAQLSQLGkdglplmKEAQEVMIAPLPLYHIYAFTANC 277
Cdd:cd05938 145 ----------SPALYIYTSGTTGLPKAARISHLRV----LQCSGFLSLCG-------VTADDVIYITLPLYHSSGFLLGI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 278 MCMMVSGNHNVLitNPR-DIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLtnSGGTALVSATAERWKGV 356
Cdd:cd05938 204 GGCIELGATCVL--KPKfSASQFWDDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRL--AIGNGLRADVWREFLRR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 357 TG-CTVVEGYGLTECSpVVTTNPYGEQARLGTVG------IPV------VGTALKVIDEQGNELPV--GERGELCVKGPQ 421
Cdd:cd05938 280 FGpIRIREFYGSTEGN-IGFFNYTGKIGAVGRVSylykllFPFelikfdVEKEEPVRDAQGFCIPVakGEPGLLVAKITQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 422 V--MKGYWQRPEATEEIL--------DAegWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKV-- 489
Cdd:cd05938 359 QspFLGYAGDKEQTEKKLlrdvfkkgDV--YFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLqe 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 490 ASCAAVGIPDE--KSG-EAVKLfvvaRDP-SLSVEELKAYCKENLTGYKIPRQIVLKDALPMT 548
Cdd:cd05938 437 VNVYGVTVPGHegRIGmAAVKL----KPGhEFDGKKLYQHVREYLPAYARPRFLRIQDSLEIT 495
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
346-562 |
3.18e-17 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 84.95 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 346 VSATAERW----KGVTGCTVVEGYGLTECSP-VVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNELPVGERGELCVKGP 420
Cdd:PLN02654 409 INPSAWRWffnvVGDSRCPISDTWWQTETGGfMITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 -----QVMKGYWQRPEATEeILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAV 495
Cdd:PLN02654 489 wpgafRTLYGDHERYETTY-FKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598496 496 GIPDEKSGEAVKLFVVARDPSLSVEELKA----YCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREIA 562
Cdd:PLN02654 568 GIEHEVKGQGIYAFVTLVEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
207-559 |
5.53e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 84.05 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSqlgkdglplMKEAQEVMIAPLPLYHIYAFTancmcmmvsgnh 286
Cdd:PRK05851 152 GGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVG---------LDAATDVGCSWLPLYHDMGLA------------ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 nVLITnprdipGFVKELKKWR-----FSA-----LLGLNTLFVALMEHPGF------------KDVDFSNLKLTNSGGTA 344
Cdd:PRK05851 211 -FLLT------AALAGAPLWLapttaFSAspfrwLSWLSDSRATLTAAPNFaynligkyarrvSDVDLGALRVALNGGEP 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 345 LVSATAERWK------GVTGCTVVEGYGLTECSPVVTTNPYGEQA--------------RLGTVGIPVVGTALKvIDEQG 404
Cdd:PRK05851 284 VDCDGFERFAtamapfGFDAGAAAPSYGLAESTCAVTVPVPGIGLrvdevttddgsgarRHAVLGNPIPGMEVR-ISPGD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGER--GELCVKGPQVMKGYwqrpeATEEILDAEGWLKTGDIAVIDEDGFVrIVDRKKDLILVSGFNVYPNEIEDV 482
Cdd:PRK05851 363 GAAGVAGReiGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 483 VMAHPKVASCAAVGIPDEKSGEAVKLFVVA--RDPSLS------VEELKAYCKenltgyKIPRQIVL--KDALPMTPVGK 552
Cdd:PRK05851 437 AAQVRGVREGAVVAVGTGEGSARPGLVIAAefRGPDEAgarsevVQRVASECG------VVPSDVVFvaPGSLPRTSSGK 510
|
....*..
gi 15598496 553 ILRRELR 559
Cdd:PRK05851 511 LRRLAVK 517
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
331-555 |
2.35e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 82.48 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 331 DFSNLKLTNSGGTALVSATAERWKGVTGCTVVEGYGLTE--CSPVVT----TNPYGeqarlgTVGIPVVGTALKVIDEQG 404
Cdd:PTZ00237 378 DLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEigITYLYCyghiNIPYN------ATGVPSIFIKPSILSEDG 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 405 NELPVGERGELCVK---GPQVMKGYWQRPEATEEILDA-EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIE 480
Cdd:PTZ00237 452 KELNVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 481 DVVMAHPKVASCAAVGI--PDEKSgEAVKLFVVARD---PSLSVEELKA----YCKENLTGYKIPRQIVLKDALPMTPVG 551
Cdd:PTZ00237 532 TSILKHPLVLECCSIGIydPDCYN-VPIGLLVLKQDqsnQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTG 610
|
....
gi 15598496 552 KILR 555
Cdd:PTZ00237 611 KIPR 614
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
37-541 |
7.78e-16 |
|
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: 80.58 E-value: 7.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 37 FADRPAF---------------SNLG-----VTLSYAELDRLSAAFAAYLQKQTDLQPGDRIAVQMPNVLQYPIAVFGAL 96
Cdd:cd17632 35 YADRPALgqratelvtdpatgrTTLRllprfETITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 97 RAGLVVVntnPLYT---AREMRHQFKDAGVRALV----YLNVFGKLVEEVLPDTRIEYLIEARMGDLLPAlkgwlvnsVV 169
Cdd:cd17632 115 RLGAVSV---PLQAgasAAQLAPILAETEPRLLAvsaeHLDLAVEAVLEGGTPPRLVVFDHRPEVDAHRA--------AL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 170 KSVKKMVPDYRLPQALPFRQALKQGQGHALQPVRVGLED--VAVLQYTGGTTGVSKGAMLTHgNLVANMLQVhaqlSQLG 247
Cdd:cd17632 184 ESARERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDDdpLALLIYTSGSTGTPKGAMYTE-RLVATFWLK----VSSI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 248 KDGLPLmkeaQEVMIAPLPLYHIYA---------------FTANCMcmMVSGNHNVLITNPRDIpGFVK---ELKKWRFS 309
Cdd:cd17632 259 QDIRPP----ASITLNFMPMSHIAGrislygtlarggtayFAAASD--MSTLFDDLALVRPTEL-FLVPrvcDMLFQRYQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 310 ALL------GLNTLFVALMEHPGFKDVDFSNLKLTNSGGTALVSATAERW-KGVTGCTVVEGYGLTECSPVVttnpygeq 382
Cdd:cd17632 332 AELdrrsvaGADAETLAERVKAELRERVLGGRLLAAVCGSAPLSAEMKAFmESLLDLDLHDGYGSTEAGAVI-------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 383 aRLGTVGIPVVgTALKVID--EQG---NELPvGERGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDI-AVIDEDGF 456
Cdd:cd17632 404 -LDGVIVRPPV-LDYKLVDvpELGyfrTDRP-HPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVmAELGPDRL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 457 VrIVDRKKDLI-LVSGFNVYPNEIEDVVMAHPKV-----------ASCAAVGIPDEKSGEAVKlfvVARDPSLSVEELKA 524
Cdd:cd17632 481 V-YVDRRNNVLkLSQGEFVTVARLEAVFAASPLVrqifvygnserAYLLAVVVPTQDALAGED---TARLRAALAESLQR 556
|
570
....*....|....*...
gi 15598496 525 YCKEN-LTGYKIPRQIVL 541
Cdd:cd17632 557 IAREAgLQSYEIPRDFLI 574
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-561 |
2.41e-15 |
|
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: 79.24 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDAGVRALVYL 129
Cdd:cd05943 99 VTWAELRRRVARLAAALRAL-GVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 N--VFGKLVEEVLPDTRIeylIEARMGDLLPALkgwLVNSVVKSVKkmvPDYR-LPQALPFRQALKQGQGHALQPVRVGL 206
Cdd:cd05943 178 DayTYNGKRHDVREKVAE---LVKGLPSLLAVV---VVPYTVAAGQ---PDLSkIAKALTLEDFLATGAAGELEFEPLPF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 ED-VAVLqYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKdglplmkeaQEVMIaplplyhiyaFTANCMCMM---- 281
Cdd:cd05943 249 DHpLYIL-YSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRP---------GDRLF----------YYTTCGWMMwnwl 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 282 ----VSGNHNVLITNPrdiPGFVKELKKWRFSALLGLNTL-----FVALMEHPGFK---DVDFSNLKLTNSGGTALVSAT 349
Cdd:cd05943 309 vsglAVGATIVLYDGS---PFYPDTNALWDLADEEGITVFgtsakYLDALEKAGLKpaeTHDLSSLRTILSTGSPLKPES 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 350 AE----RWKG------VTGCTVVegyglteCSPVVTTNPY-----GE-QARlgtvgipVVGTALKVIDEQGNELpVGERG 413
Cdd:cd05943 386 FDyvydHIKPdvllasISGGTDI-------ISCFVGGNPLlpvyrGEiQCR-------GLGMAVEAFDEEGKPV-WGEKG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 414 EL-CVKG-PQVMKGYWQRPEATE------EILdaEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMA 485
Cdd:cd05943 451 ELvCTKPfPSMPVGFWNDPDGSRyraayfAKY--PGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEK 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 486 HPKVASCAAVGIPDEKSGEAVKLFVVAR-----DPSLsVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05943 529 IPEVEDSLVVGQEWKDGDERVILFVKLRegvelDDEL-RKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKK 607
|
.
gi 15598496 561 I 561
Cdd:cd05943 608 I 608
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
207-560 |
3.16e-15 |
|
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: 78.24 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 207 EDVAVLQYTGGTTGVSKGAMLTHGnlvanMLQVHAQLsqLGKDglpLMKEAQEVMIAPLPLYHIYAFTAnCMCMMVSGNH 286
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWR-----RTLVTSNL--LSHD---LNLKNGDRTYTCMPLYHGTAAFL-GACNCLMSGG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 NVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNsgGTALVSATAERWKGVTGCTVV-EGY 365
Cdd:cd05937 156 TLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAW--GNGLRPDIWERFRERFNVPEIgEFY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 366 GLTEcSPVVTTNPYGEQARLGTVG--------------IPVvgtalKVIDEQGN-----------ELPVGERGELCVKGP 420
Cdd:cd05937 234 AATE-GVFALTNHNVGDFGAGAIGhhglirrwkfenqvVLV-----KMDPETDDpirdpktgfcvRAPVGEPGEMLGRVP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 421 QVMK----GYWQRPEATEEIL--------DAegWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPK 488
Cdd:cd05937 308 FKNReafqGYLHNEDATESKLvrdvfrkgDI--YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598496 489 VASCAAVGIP----DEKSGEA-VKLFVVARDPS-LSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELRE 560
Cdd:cd05937 386 IAEANVYGVKvpghDGRAGCAaITLEESSAVPTeFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
342-561 |
4.71e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.06 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 342 GTALVSATAERW-KGVTGCTVVEGYGLTECSPVVTTNPYGEQARLGT---VGIPVVGTALKVIDEQGNELPVGERGELCV 417
Cdd:PRK05691 3992 GEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCV 4071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 418 KGPQVMKGYWQRPEATEEIL-------DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVA 490
Cdd:PRK05691 4072 AGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVR 4151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 491 ScAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKENLTG----YKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:PRK05691 4152 E-AAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKALPAL 4225
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
209-470 |
8.26e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 74.37 E-value: 8.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 209 VAVLQYTGGTTGVSKGAMLTHGNLvanmlqvHAQLSQLGKDGLpLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNHNV 288
Cdd:PTZ00342 306 ITSIVYTSGTSGKPKGVMLSNKNL-------YNTVVPLCKHSI-FKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 289 LitnPRDIPGFVKELKKWRFSALLGL----NTLFVALMEH----PGFK---------------DVDFSNL--KLTN---- 339
Cdd:PTZ00342 378 W---SKDINYFSKDIYNSKGNILAGVpkvfNRIYTNIMTEinnlPPLKrflvkkilslrksnnNGGFSKFleGITHissk 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 340 -------------SGGTALVSATAERWKGVTGCTVVEGYGLTEcspvvTTNPYGEQARLGT----VGIPVV-GTALKVID 401
Cdd:PTZ00342 455 ikdkvnpnlevilNGGGKLSPKIAEELSVLLNVNYYQGYGLTE-----TTGPIFVQHADDNntesIGGPISpNTKYKVRT 529
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598496 402 ----EQGNELPvgeRGELCVKGPQVMKGYWQRPEATEEILDAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVS 470
Cdd:PTZ00342 530 wetyKATDTLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
50-561 |
2.82e-13 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 72.61 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 50 LSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPLYTAREMRHQFKDagVRALVYL 129
Cdd:TIGR01217 115 VTWAELRRQVASLAAALRAL-GVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQ--IEPKLLF 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 130 NVFGKLVEEVLPDtRIEYLIEARMGdlLPALKGWLVNSVVKSVKKMVPdyRLPQALPFRQALKQGQGHALQPVRVGLEDV 209
Cdd:TIGR01217 192 TVDGYRYNGKEHD-RRDKVAEVRKE--LPTLRAVVHIPYLGPRETEAP--KIDGALDLEDFTAAAQAAELVFEQLPFDHP 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 210 AVLQYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGkdglplmkeaqevmiaplPLYHIYAFTANCMCM---MVSGnh 286
Cdd:TIGR01217 267 LWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLG------------------PGDRLFYYTTTGWMMwnwLVSG-- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 287 nvLITNPRDI-----PGFVKELKKWRFS-----ALLGLNTLFVALMEHPGFK---DVDFSNLKLTNSGGTALvSATAERW 353
Cdd:TIGR01217 327 --LATGATLVlydgsPGFPATNVLWDIAertgaTLFGTSAKYVMACRKAGVHparTHDLSALQCVASTGSPL-PPDGFRW 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 354 -----KGVTGCTVVEGyGLTECSPVVTTNPYGEQARlGTVGIPVVGTALKVIDEQGNELpVGERGEL-CVKG-PQVMKGY 426
Cdd:TIGR01217 404 vydeiKADVWLASISG-GTDICSCFAGANPTLPVHI-GEIQAPGLGTAVQSWDPEGKPV-TGEVGELvCTNPmPSMPIRF 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 427 WQRPEAT---EEILDA-EGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKS 502
Cdd:TIGR01217 481 WNDPDGSkyrDAYFDTyPGVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDG 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598496 503 GEAVKLFV-----VARDPSLsVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELREI 561
Cdd:TIGR01217 561 GYRVVLFVhlapgATLDDAL-LDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKRV 623
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-558 |
5.04e-13 |
|
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: 71.35 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 215 TGGTTGVSKGAMLTHGNLVANMlqVHAQLsqlgkdglpLMKEAQEVMIAPLPLYHIYAFTANCMCMMVSGNhnVLITNPR 294
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNI--QHFRS---------LFNITSEDILFLTSPLTFDPSVVEIFLSLSSGA--TLLIVPT 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 295 DIPGFVKELKKWRFSaLLGLNTLFV--ALMEHPGFKDVDFSNLKLTNS------GGTALVSATA-ERWKGVTGCT-VVEG 364
Cdd:cd17654 193 SVKVLPSKLADILFK-RHRITVLQAtpTLFRRFGSQSIKSTVLSATSSlrvlalGGEPFPSLVIlSSWRGKGNRTrIFNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 365 YGLTECSPVVTTNPYGEQARLGTVGIPVVGTALKVIDEQGNElpvgERGELCVKGPQ---VMKGYWQRPEATeeildaeg 441
Cdd:cd17654 272 YGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTGQVFLGGLNrvcILDDEVTVPKGT-------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 442 WLKTGDIaVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKsgeavkLFVVARDPSLSVEE 521
Cdd:cd17654 340 MRATGDF-VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR------LIAFIVGESSSSRI 412
|
330 340 350
....*....|....*....|....*....|....*..
gi 15598496 522 LKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRREL 558
Cdd:cd17654 413 HKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
38-554 |
3.22e-11 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 65.97 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 38 ADRPAFSNLG-----VTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLVVVNTNPlytar 112
Cdd:PRK03584 98 DDRPAIIFRGedgprRELSWAELRRQVAALAAALRAL-GVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSP----- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 113 emrhqfkDAGVRALvyLNVFGKLVEEVL------------PDTR--IEYLIEArmgdlLPALKGwLVnsVVKSVKKMVPD 178
Cdd:PRK03584 172 -------DFGVQGV--LDRFGQIEPKVLiavdgyryggkaFDRRakVAELRAA-----LPSLEH-VV--VVPYLGPAAAA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 179 YRLPQALPFRQALKQGQGHALQPVRVGLED-VAVLqYTGGTTGVSKGAMLTHGNLVANMLQVHAQLSQLGKDglplmkea 257
Cdd:PRK03584 235 AALPGALLWEDFLAPAEAAELEFEPVPFDHpLWIL-YSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPG-------- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 258 qEVMiaplpLYhiyaFTaNCMCMM----VSG-----------------NHNVLitnprdipgfvkelkkWRFSALLGLNT 316
Cdd:PRK03584 306 -DRF-----FW----YT-TCGWMMwnwlVSGllvgatlvlydgspfypDPNVL----------------WDLAAEEGVTV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 317 L-----FVALMEHPGF---KDVDFSNLKLTNSGGTALvSATAERW------KGV-----TGCTVVegyglteCSPVVTTN 377
Cdd:PRK03584 359 FgtsakYLDACEKAGLvpgETHDLSALRTIGSTGSPL-PPEGFDWvyehvkADVwlasiSGGTDI-------CSCFVGGN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 378 PY-----GE-QARLgtvgipvVGTALKVIDEQGNELpVGERGELCVKGPqvMK----GYWQrpeateeilDAEG------ 441
Cdd:PRK03584 431 PLlpvyrGEiQCRG-------LGMAVEAWDEDGRPV-VGEVGELVCTKP--FPsmplGFWN---------DPDGsryrda 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 442 --------WlKTGDIAVIDEDGFVRIVDRkKDLILvsgfnvypN---------EIEDVVMAHPKVASCAAVGIPDEKSGE 504
Cdd:PRK03584 492 yfdtfpgvW-RHGDWIEITEHGGVVIYGR-SDATL--------NrggvrigtaEIYRQVEALPEVLDSLVIGQEWPDGDV 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 15598496 505 AVKLFVVAR-----DPSLsVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKIL 554
Cdd:PRK03584 562 RMPLFVVLAegvtlDDAL-RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
364-560 |
2.22e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 62.97 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 364 GYGLTECSPVVTTNPYGEqarLGTVGIPVVGTALKVIDeqgnelpvgerGELCVKGPQVMKGYWQRPEATEeILDAEGWL 443
Cdd:PRK09029 270 GYGLTEMASTVCAKRADG---LAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLVP-LVNDEGWF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 444 KTGDIAVIDeDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGE---AvklfVVARDPSLSVE 520
Cdd:PRK09029 335 ATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQrpvA----VVESDSEAAVV 409
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598496 521 ELKAYCKENLTGYKIP-RQIVLKDALPMTPVgKILRRELRE 560
Cdd:PRK09029 410 NLAEWLQDKLARFQQPvAYYLLPPELKNGGI-KISRQALKE 449
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
47-559 |
3.62e-09 |
|
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: 58.98 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 47 GVTLSYAELDRLSAAFAAYLQKQtDLQPGDRIAVQMPNVLQYPIAVFGALRAGLV--VVNTNplYTAREMRHQFKDAGVR 124
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVEtaLINSN--LRLESLLHCITVSKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 125 ALVYlnvfgKLVEEVLPDTRIEyliearmgdllpalkgwlvnsvvksvkkmvpdyrLPQALPfrqalkqgqghalqpvrV 204
Cdd:cd05939 78 ALIF-----NLLDPLLTQSSTE----------------------------------PPSQDD-----------------V 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 205 GLEDVAVLQYTGGTTGVSKGAMLTHGNlvanmlqvHAQLSQLGKDGLPLMKEaqEVMIAPLPLYHIyafTANCMCM--MV 282
Cdd:cd05939 102 NFRDKLFYIYTSGTTGLPKAAVIVHSR--------YYRIAAGAYYAFGMRPE--DVVYDCLPLYHS---AGGIMGVgqAL 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 283 SGNHNVLITNPRDIPGFVKELKKWRFSALLGLNTLFVALMEHPGFKDVDFSNLKLTNSGGTalvsaTAERWKGVTG---- 358
Cdd:cd05939 169 LHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGL-----RPQIWEQFVRrfgi 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 359 CTVVEGYGLTECspvvTTNPYGEQARLGTVG-IPVVGTALKVI-----DEQGNELPVGERG--ELCVKG-PQVM------ 423
Cdd:cd05939 244 PQIGEFYGATEG----NSSLVNIDNHVGACGfNSRILPSVYPIrlikvDEDTGELIRDSDGlcIPCQPGePGLLvgkiiq 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 424 -------KGYWQRPEATEEIL-----DAEGWLKTGDIAVIDEDGFVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAS 491
Cdd:cd05939 320 ndplrrfDGYVNEGATNKKIArdvfkKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLED 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 492 CAAVG--IPdEKSGEAVKLFVVARDPSLSVEELKAYCKENLTGYKIPRQIVLKDALPMTPVGKILRRELR 559
Cdd:cd05939 400 VVVYGveVP-GVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
350-530 |
1.03e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.47 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 350 AERWkgvtGCTVVEGYGLTECSPVVTtnpyGE-QARLGtvgiPVVGTAL---KVID-EQGNELPVGERGELCVkgpqvmk 424
Cdd:COG1541 224 EERW----GIKAYDIYGLTEVGPGVA----YEcEAQDG----LHIWEDHflvEIIDpETGEPVPEGEEGELVV------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 425 gywqrpeaTeeILDAEGW----LKTGDIAVIDEDG---------FVRIVDRKKDLILVSGFNVYPNEIEDVVMAHPKVAS 491
Cdd:COG1541 285 --------T--TLTKEAMplirYRTGDLTRLLPEPcpcgrthprIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598496 492 CAAVGIPDEKSGEAVKLfVVARDPSLSVEELKAYCKENL 530
Cdd:COG1541 355 EYQIVVDREGGLDELTV-RVELAPGASLEALAEAIAAAL 392
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
399-545 |
1.88e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.15 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 399 VID-EQGNELPVGERGE-----LCVKGPQVMKgYWqrpeateeildaegwlkTGDIA-VIDEDGFV--------RIVDRK 463
Cdd:cd05913 261 IIDpETGEPVPPGEVGElvfttLTKEAMPLIR-YR-----------------TRDITrLLPGPCPCgrthrridRITGRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 464 KDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVARDPSLSVEELKAYCKEnltgykIPRQIVLKD 543
Cdd:cd05913 323 DDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEADDDEKLEALKQR------LERHIKSVL 396
|
..
gi 15598496 544 AL 545
Cdd:cd05913 397 GV 398
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
409-553 |
2.76e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 43.66 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 409 VGERGELCVKGPQVMKGYWQRPEATEE------ILDAEGWL----------------------KTGDIAVIDEDGFVRIV 460
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYRGLPELNKEkfvnnwFVEPDHWNyldkdnnepwrqfwlgprdrlyRTGDLGRYLPNGDCECC 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598496 461 DRKKDLILVSGFNVYPNEIEDVVMAHPKVASCAAVGIPDEKSGEAVKLFVVAR------------DPSLSVEE------- 521
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRfdkpddesfaqeDVPKEVSTdpivkgl 471
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598496 522 ---------LKAYCKENLTGYKIPRQIVLKDALPMTPVGKI 553
Cdd:cd17647 472 igyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKV 512
|
|
| |
