|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1-562 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 1218.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 1 MIENFWKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAV 80
Cdd:PRK05677 1 MIENFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 81 QLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPL 160
Cdd:PRK05677 81 QLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 161 KRFIVNFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCK 240
Cdd:PRK05677 161 KRLLINAVVKHVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 241 ALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETF 320
Cdd:PRK05677 241 ALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVP 400
Cdd:PRK05677 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 401 LGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPG 480
Cdd:PRK05677 401 LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 481 VLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAG 560
Cdd:PRK05677 481 VLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAG 560
|
..
gi 15598495 561 QK 562
Cdd:PRK05677 561 LK 562
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-553 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 849.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 1 MIENFWKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAV 80
Cdd:PRK12492 1 MQPDFWNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 81 QLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPL 160
Cdd:PRK12492 81 QMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 161 KRFIVNFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCK 240
Cdd:PRK12492 161 KGWLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 241 ALMGAN-------LNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVA 313
Cdd:PRK12492 241 ACLSQLgpdgqplMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 314 LCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLCKVI 392
Cdd:PRK12492 321 LMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELaRLGTVGIPVPGTALKVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 393 GDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
Cdd:PRK12492 401 DDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 473 DVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGaTLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
.
gi 15598495 553 D 553
Cdd:PRK12492 560 D 560
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2-562 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 816.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 2 IENFWKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQ 81
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 82 LPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLK 161
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 162 RFIVNFVVKHIKKMVPAYSLPQATKLTDALARgaGKSFQEAAPQ--ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC 239
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHK--GRRMQYVKPElvPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 240 KALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNET 319
Cdd:PRK08974 239 KAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 320 FRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFqNIQ--VGTIGIPVPSTLCKVIGDDGQ 397
Cdd:PRK08974 319 FQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPY-DLDyySGSIGLPVPSTEIKLVDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 398 EVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT 477
Cdd:PRK08974 398 EVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVML 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 478 LPGVLQCAAIGIPDEKSGESIKVFvVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELK 557
Cdd:PRK08974 477 HPKVLEVAAVGVPSEVSGEAVKIF-VVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARA 555
|
....*
gi 15598495 558 KAGQK 562
Cdd:PRK08974 556 KVDNK 560
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
3-554 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 799.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 3 ENFWKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQL 82
Cdd:PRK07059 2 EKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 83 PNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPpLKR 162
Cdd:PRK07059 81 PNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLLG-FKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 163 FIVNFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKAL 242
Cdd:PRK07059 160 HIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 243 MGANLNEGCEI----LIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNE 318
Cdd:PRK07059 240 LQPAFEKKPRPdqlnFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 319 TFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQ-VGTIGIPVPSTLCKVIGDDGQ 397
Cdd:PRK07059 320 DFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRDDDGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 398 EVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT 477
Cdd:PRK07059 400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 478 LPGVLQCAAIGIPDEKSGESIKVFVVVKPGAtLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDG 555
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
26-552 |
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: 703.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 26 ILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNT 105
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 106 NPLYTARELEHQFNDSGAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqAT 185
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIV-------------------------------------------------------AV 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 186 KLTDALARGAGKSFqEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGaNLNEGCEILIAPLPLYHIYA 265
Cdd:cd05936 105 SFTDLLAAGAPLGE-RVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLE-DLLEGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 266 FTFHCMAMMLTGNHNILITNPRDlPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAER 345
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRP-IGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 WKEVTGCAICEGYGMTETAPVVSVNPFQNIQ-VGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEA 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 425 TDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV 504
Cdd:cd05936 342 TAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 15598495 505 KPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05936 421 KEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
6-553 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 686.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 6 WKDKYPAGIAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNV 85
Cdd:PRK08751 7 WLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALMMPNC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 86 LQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIV 165
Cdd:PRK08751 87 LQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 166 NFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGA 245
Cdd:PRK08751 167 NFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 246 N--LNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKL 323
Cdd:PRK08751 247 TgkLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 324 DFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQV-GTIGIPVPSTLCKVIGDDGQEVPLG 402
Cdd:PRK08751 327 DFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYnGSIGLPIPSTDACIKDDAGTVLAIG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 403 ERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVL 482
Cdd:PRK08751 407 EIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 483 QCAAIGIPDEKSGESIKVfVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK08751 487 EVAAVGVPDEKSGEIVKV-VIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
26-561 |
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: 544.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 26 ILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNT 105
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 106 NPLYTARELEHQFNDSGAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqat 185
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 186 kltdalargagksfqeaapqaddvAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYA 265
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALG--LTPG-DVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 266 FTFHCMAMMLTGNHNILITNpRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAER 345
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 WKEVTGCAICEGYGMTETAPVVSVNP--FQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQE 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPedPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 424 ATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVV 503
Cdd:COG0318 315 ATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 504 VKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQ 561
Cdd:COG0318 394 LRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
6-560 |
1.38e-157 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 462.16 E-value: 1.38e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 6 WKDKYPAGIAAEINPDQyPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNV 85
Cdd:PRK05605 15 WLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRA-LGVRPGDRVAIVLPNC 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 86 LQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIV 165
Cdd:PRK05605 93 PQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQRLAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 166 NFVVKHIKKMVPAYSLPqAT------KLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC 239
Cdd:PRK05605 173 RLPIPALRKARAALTGP-APgtvpweTLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 240 KALMGAnLNEGCEILIAPLPLYHIYAFTFhCMAM-MLTGNHNILITNPrDLPSMLKDLGQWKFTGFVGLNTLFVALCNNE 318
Cdd:PRK05605 252 KAWVPG-LGDGPERVLAALPMFHAYGLTL-CLTLaVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 319 TFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLCKVIG--DD 395
Cdd:PRK05605 329 EERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVGVPFPDTEVRIVDpeDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 396 GQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
Cdd:PRK05605 409 DETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 476 ATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:PRK05605 488 REHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREEL 567
|
....*
gi 15598495 556 LKKAG 560
Cdd:PRK05605 568 LEKLG 572
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
25-554 |
9.89e-140 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 414.30 E-value: 9.89e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 25 NILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVN 104
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 105 TNPLYTARELEHQFNDSGAKAVVCLAnmahlveGVLPktgvkqvIVTEVGDILPPLKRFIVnfvvkhIKKMVPAYSLPQA 184
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLG-------LFLG-------VDYSATTRLPALEHVVI------CETEEDDPHTEKM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 185 TKLTDALARGAGkSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIApLPLYHIY 264
Cdd:PRK07656 145 KTFTDFLAAGDP-AERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLG--LTEGDRYLAA-NPFFHVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 265 AFTFHCMAMMLTGNhNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAE 344
Cdd:PRK07656 221 GYKAGVNAPLMRGA-TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 345 RWKEVTGCAIC-EGYGMTETAPVVSVNPF---QNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQ 420
Cdd:PRK07656 300 RFESELGVDIVlTGYGLSEASGVTTFNRLdddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 421 RQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKV 500
Cdd:PRK07656 380 DPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKA 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15598495 501 FVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK07656 460 YVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
2-558 |
2.31e-137 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 410.19 E-value: 2.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 2 IENFWKDKYPAGIAAEINPDQYPnILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQ 81
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTISYDIQP-LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 82 LPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLK 161
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 162 RFIVNFVVKHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqckA 241
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSN-----T 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 242 LMGA----NLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILItnPR-DLPSMLKDLGQWKFTGFVGLNTLFVALCN 316
Cdd:PRK06710 236 LMGVqwlyNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 317 NETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQV-GTIGIPVPSTLCKVIG-D 394
Cdd:PRK06710 314 SPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSlE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 395 DGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
Cdd:PRK06710 394 TGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 475 LATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK06710 473 LYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
....
gi 15598495 555 ELKK 558
Cdd:PRK06710 553 EKRK 556
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
21-553 |
1.48e-134 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 401.49 E-value: 1.48e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 21 DQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGL 100
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 101 IVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPK-TGVKQVIVTEVGDILPPLKRfivnfvvkhikkmVPAY 179
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlPTVRTVIVEGDGPAAPLAPE-------------VGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 180 slpqatkltDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIApLP 259
Cdd:PRK06187 149 ---------EELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLK--LSRDDVYLVI-VP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTFhCMAMMLTGNHNILitnPRDL-PSMLKDL-GQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMA 337
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVI---PRRFdPENLLDLiETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 338 LQLATAERWKEVTGCAICEGYGMTETAPVVSVNPF------QNIQVGTIGIPVPSTLCKVIGDDGQEVP--LGERGELCV 409
Cdd:PRK06187 293 LPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPedqlpgQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 410 KGPQVMKGYWQRQEATDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGI 489
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 490 PDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK06187 452 PDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
47-547 |
4.63e-133 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 396.58 E-value: 4.63e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VClanMAHLVEGVLpktgvkqvivtEVGDILPPLKRFIV----NFVVKHIKKMVPAYSLPQATKLTDALARGAgksfqea 202
Cdd:cd05911 87 FT---DPDGLEKVK-----------EAAKELGPKDKIIVlddkPDGVLSIEDLLSPTLGEEDEDLPPPLKDGK------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 apqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGcEILIAPLPLYHIYAFTFhCMAMMLTGnHNIL 282
Cdd:cd05911 146 ----DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSN-DVILGFLPLYHIYGLFT-TLASLLNG-ATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ITNPRDLPSMLKDLGQWKFTgFVGL-NTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEV-TGCAICEGYGM 360
Cdd:cd05911 219 IMPKFDSELFLDLIEKYKIT-FLYLvPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRfPNATIKQGYGM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 361 TETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQE-VPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGD 439
Cdd:cd05911 298 TETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 440 IAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHM 519
Cdd:cd05911 378 IGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYV 457
|
490 500
....*....|....*....|....*....
gi 15598495 520 HDNLTGYKRPKA-VEFRDSLPTTNVGKIL 547
Cdd:cd05911 458 AKKVASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-462 |
1.24e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 385.13 E-value: 1.24e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 30 LKESCQRFATKPAFTN-LGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPL 108
Cdd:pfam00501 1 LERQAARTPDKTALEVgEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 109 YTARELEHQFNDSGAKAVVCLANmaHLVEGVLPKTG-VKQVIVTEVGDILPPLKRFIVNFVVKHIKKMVPayslpqatkl 187
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDA--LKLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 188 tdalargagksfQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEG-CEILIAPLPLYHIYAF 266
Cdd:pfam00501 148 ------------PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpDDRVLSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 267 TFHCMAMMLTGNHNILI--TNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAE 344
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 345 RWKEVTGCAICEGYGMTETAPVVSVNPFQNIQ---VGTIGIPVPSTLCKVIGDD-GQEVPLGERGELCVKGPQVMKGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15598495 421 RQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS 462
Cdd:pfam00501 376 DPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
30-561 |
8.72e-129 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 387.39 E-value: 8.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 30 LKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLY 109
Cdd:PRK08314 16 LEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 110 TARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIV-NFVVKHIKkmVPAYSLPQATKLT 188
Cdd:PRK08314 96 REEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAEPEIAVpAWLRAEPP--LQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqckalmGANL--NEGCE-ILIAPLPLYHIYA 265
Cdd:PRK08314 174 EALAAGLAPPPHTAGP--DDLAVLPYTSGTTGVPKGCMHTHRTVMANAV------GSVLwsNSTPEsVVLAVLPLFHVTG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 266 FTfHCM-AMMLTGNHNILITN-PRDLPSMLkdLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATA 343
Cdd:PRK08314 246 MV-HSMnAPIYAGATVVLMPRwDREAAARL--IERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 344 ERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQ 422
Cdd:PRK08314 323 ERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 423 EATDEI---LDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIK 499
Cdd:PRK08314 403 EATAEAfieIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 500 VFVVVKPGA--TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQ 561
Cdd:PRK08314 483 AVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKARAAK 546
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
30-548 |
1.06e-124 |
|
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: 373.10 E-value: 1.06e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 30 LKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLY 109
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 110 TARELEHQFNDSGAKAVVclanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltd 189
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 190 alargagksfqeaapqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqcKALMGANLNEGCeILIAPLPLYHIYAFTFH 269
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV--NALAALDLGPDD-VLLVVAPLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 270 CMAMMLTGNHNILITNPrDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEv 349
Cdd:cd17631 158 TLPTLLRGGTVVILRKF-DPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TGCAICEGYGMTETAPVVSVNPFQNIQ--VGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE 427
Cdd:cd17631 236 RGVKFVQGYGMTETSPGVTFLSPEDHRrkLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAA 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 428 ILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPG 507
Cdd:cd17631 316 AF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPG 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15598495 508 ATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILR 548
Cdd:cd17631 395 AELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
22-551 |
2.78e-122 |
|
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: 369.26 E-value: 2.78e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 22 QYPNILSVLKESCQRFATKPAFTN--LGKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAG 99
Cdd:cd05904 3 TDLPLDSVSFLFASAHPSRPALIDaaTGRALTYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 100 LIVVNTNPLYTARELEHQFNDSGAKavvclanmahlvegvlpktgvkqVIVTeVGDILPPLKRFIVNFVVkhikkmVPAY 179
Cdd:cd05904 82 AVVTTANPLSTPAEIAKQVKDSGAK-----------------------LAFT-TAELAEKLASLALPVVL------LDSA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 180 SLPQATKLTDALARGAGKSFQEAAPQaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLnEGCEILIAPLP 259
Cdd:cd05904 132 EFDSLSFSDLLFEADEAEPPVVVIKQ-DDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNS-DSEDVFLCVLP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTFHCMAMMLTGNhNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQ 339
Cdd:cd05904 210 MFHIYGLSSFALGLLRLGA-TVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LATAERWKEV-TGCAICEGYGMTETAPVVSVNPFQ---NIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQV 414
Cdd:cd05904 289 KELIEAFRAKfPNVDLGQGYGMTESTGVVAMCFAPekdRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKS 494
Cdd:cd05904 369 MKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEA 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 495 GESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
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 ... |
208-547 |
2.93e-112 |
|
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: 337.72 E-value: 2.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIyAFTFHCMAMMLTGnHNILITNPR 287
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG--LTEG-DVFLSTLPLFHI-GGLFGLLGALLAG-GTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVV 367
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 368 SVNPF--QNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEIlDADGWLKTGDIAIIQE 445
Cdd:cd04433 156 ATGPPddDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 446 DGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTG 525
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 15598495 526 YKRPKAVEFRDSLPTTNVGKIL 547
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2-551 |
2.72e-108 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 335.47 E-value: 2.72e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 2 IENFWKDKYPAGIAAEInpdQYPN----ILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDR 77
Cdd:PRK06178 10 LRALQQAAWPAGIPREP---EYPHgerpLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQR-GVGAGDR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 78 IAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDIL 157
Cdd:PRK06178 86 VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 158 PPLKRFIVNFVVKhikkmVPAYSLPQATKLTDALaRGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANml 237
Cdd:PRK06178 166 PAEPTLPLPDSLR-----APRLAAAGAIDLLPAL-RACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYT-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 238 qCKALMGANLNEGC-EILIAPLPLYHIYAFTFHCMAMMLTGNHNILITnpR-DLPSMLKDLGQWKFTGFVGLNTLFVALC 315
Cdd:PRK06178 238 -AAAAYAVAVVGGEdSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVDNAVELM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 316 NNETFRKLDFSALKLT--LSGGMALQLATAERWKEVTGCAICEG-YGMTETApvvSVNPF-QNIQVGT---------IGI 382
Cdd:PRK06178 315 DHPRFAEYDLSSLRQVrvVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETH---TCDTFtAGFQDDDfdllsqpvfVGL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 383 PVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILV 461
Cdd:PRK06178 392 PVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 462 SGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKaVEFRDSLPTT 541
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMT 549
|
570
....*....|
gi 15598495 542 NVGKILRREL 551
Cdd:PRK06178 550 ATGKVRKQDL 559
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
50-551 |
6.81e-104 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 319.42 E-value: 6.81e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCL 129
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 130 ANMahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapqaDDV 209
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 210 AVLQYTGGTTGVAKGAMLTHRNLVANMLQckALMGANLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNpRDL 289
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQ--SAVWTGLTPS-DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR-WDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 290 PSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSV 369
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 370 NPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADG---WLKTGDIAIIQE 445
Cdd:cd05935 243 NPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDE 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 446 DGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPG--ATLTKEQVMQHMHDNL 523
Cdd:cd05935 323 EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQM 402
|
490 500
....*....|....*....|....*...
gi 15598495 524 TGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd05935 403 AAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
48-559 |
2.17e-100 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 314.74 E-value: 2.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:COG0365 38 RTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 ClanmahlVEGVLPKTGVKQV--IVTEVGDILPPLKRFIVnfvvkhIKKMVPAYSLPQATKLTDALARgAGKSFQEAAPQ 205
Cdd:COG0365 117 T-------ADGGLRGGKVIDLkeKVDEALEELPSLEHVIV------VGRTGADVPMEGDLDWDELLAA-ASAEFEPEPTD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLvanMLQCKALMGA--NLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNIL- 282
Cdd:COG0365 183 ADDPLFILYTSGTTGKPKGVVHTHGGY---LVHAATTAKYvlDLKPG-DVFWCTADIGWATGHSYIVYGPLLNGATVVLy 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 --ITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCN--NETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGY 358
Cdd:COG0365 259 egRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGW 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTET-APVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQ--VMKGYWQRQEATDEIL--DADG 433
Cdd:COG0365 339 GQTETgGIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT-- 511
Cdd:COG0365 419 WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSde 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598495 512 -KEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKA 559
Cdd:COG0365 499 lAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRP 547
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
29-554 |
5.94e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 307.24 E-value: 5.94e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 29 VLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPL 108
Cdd:PRK08316 16 ILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLD-LGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 109 YTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIvNFvvkhikkmvpayslpqatklt 188
Cdd:PRK08316 95 LTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWL-DF--------------------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCkaLMGANLNEGcEILIAPLPLYHIYAFtf 268
Cdd:PRK08316 153 ADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSC--IVAGDMSAD-DIPLHALPLYHCAQL-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 269 HCMAM--MLTGNHNILITNPrDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERW 346
Cdd:PRK08316 228 DVFLGpyLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKEL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 KE-VTGCAICEGYGMTETAPVVSV-NPF-QNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQE 423
Cdd:PRK08316 307 RErLPGLRFYNCYGQTEIAPLATVlGPEeHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 424 ATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVV 503
Cdd:PRK08316 387 KTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15598495 504 VKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK08316 466 PKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
38-553 |
6.69e-97 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 303.46 E-value: 6.69e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 38 ATKPAF--TNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELE 115
Cdd:cd05926 1 PDAPALvvPGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 116 HQFNDSGAKAVVclanmahlvegvLPKTGVkqvivTEVGDILPPLKRFIVNFVVKHIKKMVPayslPQATKLTDALARGA 195
Cdd:cd05926 80 FYLADLGSKLVL------------TPKGEL-----GPASRAASKLGLAILELALDVGVLIRA----PSAESLSNLLADKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 196 GKSFqEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKAlmGANLNEGcEILIAPLPLYHIYAFTFHCMAMML 275
Cdd:cd05926 139 NAKS-EGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITN--TYKLTPD-DRTLVVMPLFHVHGLVASLLSTLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 276 TGNhNILITnPRDLPSML-KDLGQWKFTGFVGLNTLFVALCNNETFRKLD-FSALKLTLSGGMALQLATAERWKEVTGCA 353
Cdd:cd05926 215 AGG-SVVLP-PRFSASTFwPDVRDYNATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ICEGYGMTETAPVVSVNPFQNIQV--GTIGIPVPSTLCkVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDA 431
Cdd:cd05926 293 VLEAYGMTEAAHQMTSNPLPPGPRkpGSVGKPVGVEVR-ILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 432 DGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT 511
Cdd:cd05926 372 DGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVT 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15598495 512 KEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05926 452 EEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
30-562 |
8.93e-97 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 305.20 E-value: 8.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 30 LKESCQRFATKPA--FTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNP 107
Cdd:PRK08315 22 LDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 108 LYTARELEHQFNDSGAKAVVCL-----ANMAHLVEGVLP--KTGVKQVIVTEVgdiLPPLKRFIVNFVVKHikkmvpays 180
Cdd:PRK08315 101 AYRLSELEYALNQSGCKALIAAdgfkdSDYVAMLYELAPelATCEPGQLQSAR---LPELRRVIFLGDEKH--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 181 lPQATKLTDALARGAGKSFQE-----AAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGCEILI 255
Cdd:PRK08315 169 -PGMLNFDELLALGRAVDDAElaarqATLDPDDPINIQYTSGTTGFPKGATLTHRNILNNGYFIGEAM--KLTEEDRLCI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 256 aPLPLYHiyaftfhCMAMMLtGN-----H--NILITNPR-DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSA 327
Cdd:PRK08315 246 -PVPLYH-------CFGMVL-GNlacvtHgaTMVYPGEGfDPLATLAAVEEERCTALYGVPTMFIAELDHPDFARFDLSS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 328 LKltlSGGMALQLATAERWKEV------TGCAICegYGMTETAPVV---SVN-PFQNiQVGTIGIPVPSTLCKVIG-DDG 396
Cdd:PRK08315 317 LR---TGIMAGSPCPIEVMKRVidkmhmSEVTIA--YGMTETSPVStqtRTDdPLEK-RVTTVGRALPHLEVKIVDpETG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 397 QEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA 476
Cdd:PRK08315 391 ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLY 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 477 TLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD--- 553
Cdd:PRK08315 471 THPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREmmi 550
|
....*....
gi 15598495 554 EELKKAGQK 562
Cdd:PRK08315 551 EELGLQAAK 559
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
26-557 |
1.09e-95 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 302.46 E-value: 1.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 26 ILSVLKESCQRFATKPA--FTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVV 103
Cdd:PRK12583 20 IGDAFDATVARFPDREAlvVRHQALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 104 NTNPLYTARELEHQFNDSGAKAVVCLA-----NMAHLVEGVLPKTGVKQVIVTEVGDiLPPLKRFIVnfvvkhikkMVPA 178
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADafktsDYHAMLQELLPGLAEGQPGALACER-LPELRGVVS---------LAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 179 YSlPQATKLTDALARGAGKSFQ-----EAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEI 253
Cdd:PRK12583 169 PP-PGFLAWHELQARGETVSREalaerQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG--LTEH-DR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 254 LIAPLPLYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLS 333
Cdd:PRK12583 245 LCVPVPLYHCFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 334 GGMALQLATAERWKEVTGCA-ICEGYGMTETAPVV---SVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCV 409
Cdd:PRK12583 325 AGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSPVSlqtTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 410 KGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGI 489
Cdd:PRK12583 405 RGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGV 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 490 PDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD---EELK 557
Cdd:PRK12583 485 PDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREisiEELA 555
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
38-554 |
2.28e-94 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 297.17 E-value: 2.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 38 ATKPAF-TNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQL---PNVLqypIVVFGAMRAGLIVVNTNPLYTARE 113
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVeksPEAL---ALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 114 LEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVivtevgdilpplkrfivnfvvkhikkmvpaYSLPQATK--LTDAl 191
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHV------------------------------ETLDADGTgsLLEA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 192 ARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYAFTFHCM 271
Cdd:PRK07514 141 AAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWR--FTPD-DVLIHALPIFHTHGLFVATN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 AMMLTGNHNILItnPR-DLPSMLKDLGQwkFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVT 350
Cdd:PRK07514 218 VALLAGASMIFL--PKfDPDAVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 351 GCAICEGYGMTETAPVVSvNPFQNIQV-GTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEI 428
Cdd:PRK07514 294 GHAILERYGMTETNMNTS-NPYDGERRaGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 429 LDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGA 508
Cdd:PRK07514 373 FRADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGA 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15598495 509 TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK07514 453 ALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
20-488 |
7.52e-93 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 296.24 E-value: 7.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 20 PDQYPNILSVLKESCQRFATKPAFTNLG----KTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGA 95
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 96 MRAGLIVVntnPLY---TARELEHQFNDSGAKAVVclanmahlVEG--VLPKtgvkqviVTEVGDILPPLKRfIVNFvvk 170
Cdd:COG1022 86 LAAGAVTV---PIYptsSAEEVAYILNDSGAKVLF--------VEDqeQLDK-------LLEVRDELPSLRH-IVVL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 171 hikKMVPAYSLPQATKLTDALARGAGKSFQE------AAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMG 244
Cdd:COG1022 144 ---DPRGLRDDPRLLSLDELLALGREVADPAelearrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 245 anLNEGCEILiAPLPLYHIYAFTFHCMAMML--TGNHnilitnPRDLPSMLKDLGQWKFTGFVG--------LNTLFVAL 314
Cdd:COG1022 221 --LGPGDRTL-SFLPLAHVFERTVSYYALAAgaTVAF------AESPDTLAEDLREVKPTFMLAvprvwekvYAGIQAKA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 315 cNNETF--RKLDFSALKL------------TLSGGMALQLATAER-----WKEVTG-------CA--------------- 353
Cdd:COG1022 292 -EEAGGlkRKLFRWALAVgrryararlagkSPSLLLRLKHALADKlvfskLREALGgrlrfavSGgaalgpelarffral 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ---ICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTlckvigddgqEVPLGERGELCVKGPQVMKGYWQRQEATDEILD 430
Cdd:COG1022 371 gipVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGV----------EVKIAEDGEILVRGPNVMKGYYKNPEATAEAFD 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 431 ADGWLKTGDIAIIQEDGYMRIVDRKKDMI-LVSGFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:COG1022 441 ADGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
30-552 |
3.47e-90 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 290.32 E-value: 3.47e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 30 LKESCQRFATKPAFTNL--------GKTLTYGELYklsGDF--AAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAG 99
Cdd:PRK07529 31 LSRAAARHPDAPALSFLldadpldrPETWTYAELL---ADVtrTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 100 lIVVNTNPLYTARELEHQFNDSGAKAVVCLA-----NMAHLVEGVLPK-TGVKQVIVTEVGDILPPLKRFIVNFVVKHIK 173
Cdd:PRK07529 108 -IANPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtDIWQKVAEVLAAlPELRTVVEVDLARYLPGPKRLAVPLIRRKAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 174 KMVPAYslpqatklTDALARGAG-KSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgce 252
Cdd:PRK07529 187 ARILDF--------DAELARQPGdRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD--- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 253 ILIAPLPLYHIYAFTFHCMAMMLTGNHNILIT-----NPRDLPSMLKDLGQWKFTGFVGLNTLFVAL----CNNEtfrkl 323
Cdd:PRK07529 256 TVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrGPGVIANFWKIVERYRINFLSGVPTVYAALlqvpVDGH----- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 324 DFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNP-FQNIQVGTIGIPVPSTLCKVI-----GDDGQ 397
Cdd:PRK07529 331 DISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPpDGERRIGSVGLRLPYQRVRVVilddaGRYLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 398 EVPLGERGELCVKGPQVMKGYWQRQEATDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT 477
Cdd:PRK07529 411 DCAVDEVGVLCIAGPNVFSGYLEAAHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLR 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 478 LPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTgyKR---PKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK07529 490 HPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIA--ERaavPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
48-551 |
6.98e-88 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 280.21 E-value: 6.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 CLANMAHLVEGVLPKTGVKQVIVTEvgDILPPLKRFIVNFVvkhikkmvpayslpqatkltdalargagksfqeaAPQAD 207
Cdd:PRK06839 106 VEKTFQNMALSMQKVSYVQRVISIT--SLKEIEDRKIDNFV----------------------------------EKNES 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILiapLPLYHIYAFTFHCMAMMLTGNHnILITNPR 287
Cdd:PRK06839 150 ASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVL---LPLFHIGGIGLFAFPTLFAGGV-IIVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGG----MALQLATAERwkevtGCAICEGYGMTET 363
Cdd:PRK06839 226 EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GFLFGQGFGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVNPFQNI--QVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDaDGWLKTGDIA 441
Cdd:PRK06839 301 SPTVFMLSEEDArrKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQ-DGWLCTGDLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 442 IIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHD 521
Cdd:PRK06839 380 RVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRL 459
|
490 500 510
....*....|....*....|....*....|
gi 15598495 522 NLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK06839 460 FLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
20-552 |
7.29e-87 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 278.79 E-value: 7.29e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 20 PDQY-PNILSvLKESC----QRFATKPAFTN--LGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVV 92
Cdd:PLN02246 15 PDIYiPNHLP-LHDYCferlSEFSDRPCLIDgaTGRVYTYADVELLSRRVAAGLHKL-GIRQGDVVMLLLPNCPEFVLAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 93 FGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILpplkrfiVNFvvkhi 172
Cdd:PLN02246 93 LGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGC-------LHF----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 173 kkmvpayslpqaTKLTDAlargAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQckALMGANLN---E 249
Cdd:PLN02246 161 ------------SELTQA----DENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQ--QVDGENPNlyfH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 250 GCEILIAPLPLYHIYAFTFHCMAMMLTGNhNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALK 329
Cdd:PLN02246 223 SDDVILCVLPMFHIYSLNSVLLCGLRVGA-AILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 330 LTLSGG--MALQLATAERWKeVTGCAICEGYGMTETAPVVSV------NPFQnIQVGTIGIPVPSTLCKVIG-DDGQEVP 400
Cdd:PLN02246 302 MVLSGAapLGKELEDAFRAK-LPNAVLGQGYGMTEAGPVLAMclafakEPFP-VKSGSCGTVVRNAELKIVDpETGASLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 401 LGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPG 480
Cdd:PLN02246 380 RNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPS 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598495 481 VLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PLN02246 460 IADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
40-553 |
1.05e-86 |
|
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: 275.32 E-value: 1.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVclanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksf 199
Cdd:cd05941 82 DSEPSLVL------------------------------------------------------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeaapqadDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNH 279
Cdd:cd05941 90 --------DPALILYTSGTTGRPKGVVLTHANLAA---NVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGAS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILITNPrDLPSMLKDLGQWKFTGFVGLNTLFVAL--------CNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTG 351
Cdd:cd05941 159 VEFLPKF-DPKEVAISRLMPSITVFMGVPTIYTRLlqyyeahfTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 352 CAICEGYGMTETAPVVSvNPFQNIQV-GTIGIPVPSTLCKVIGDD-GQEVPLGERGELCVKGPQVMKGYWQRQEATDEIL 429
Cdd:cd05941 238 HTLLERYGMTEIGMALS-NPLDGERRpGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 430 DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGA 508
Cdd:cd05941 317 TDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGA 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15598495 509 -TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05941 397 aALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
26-552 |
4.26e-85 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 273.79 E-value: 4.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 26 ILSVLKescqRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNT 105
Cdd:PRK06188 18 LVSALK----RYPDRPALVLGDTRLTYGQLADRISRYIQAFEA-LGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 106 NPLYTARELEHQFNDSGAKAVVCLANM-----AHLVEGVlpkTGVKQVIvtevgdilpplkrfivnfvvkhikkmvPAYS 180
Cdd:PRK06188 93 HPLGSLDDHAYVLEDAGISTLIVDPAPfveraLALLARV---PSLKHVL---------------------------TLGP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 181 LPQATKLTDALARGAGKSFqEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQckALMGA-NLNEGCEILiAPLP 259
Cdd:PRK06188 143 VPDGVDLLAAAAKFGPAPL-VAAALPPDIAGLAYTGGTTGKPKGVMGTHRSIAT-MAQ--IQLAEwEWPADPRFL-MCTP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTFhcMAMMLTGNHNILIT--NPRDLPSMLKDlGQWKFTGFVglNTLFVALCNNETFRKLDFSALKLTLSGGMA 337
Cdd:PRK06188 218 LSHAGGAFF--LPTLLRGGTVIVLAkfDPAEVLRAIEE-QRITATFLV--PTMIYALLDHPDLRTRDLSSLETVYYGASP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 338 L---QLATAerwKEVTGCAICEGYGMTETAPVVSV------NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELC 408
Cdd:PRK06188 293 MspvRLAEA---IERFGPIFAQYYGQTEAPMVITYlrkrdhDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEIC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 409 VKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:PRK06188 370 VRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIG 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 489 IPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK06188 449 VPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
40-552 |
3.01e-84 |
|
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: 271.16 E-value: 3.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd05959 20 KTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVclanmahlVEGVLpktgvKQVIVTEVGDILPPLKRFIVnfvvkhikkMVPAYSLPQATKLTDALARGAGkSF 199
Cdd:cd05959 99 DSRARVVV--------VSGEL-----APVLAAALTKSEHTLVVLIV---------SGGAGPEAGALLLAELVAAEAE-QL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNL-VANMLQCKALMGANLNEGCeiLIAPlPLYHIYAFTFHCMAMMLTGN 278
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIyWTAELYARNVLGIREDDVC--FSAA-KLFFAYGLGNSLTFPLSVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNpRDLP-SMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEG 357
Cdd:cd05959 233 TTVLMPE-RPTPaAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 358 YGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAdGWLKT 437
Cdd:cd05959 312 IGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 438 GDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT---KEQ 514
Cdd:cd05959 391 GDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSealEEE 470
|
490 500 510
....*....|....*....|....*....|....*...
gi 15598495 515 VMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05959 471 LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-552 |
7.50e-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.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 264.91 E-value: 7.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNP 286
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLG--LTEQ-DRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKltlSGGMALQLATAERWKEV------TGCAICegYGM 360
Cdd:cd05917 79 FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLR---TGIMAGAPCPPELMKRVievmnmKDVTIA--YGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 361 TETAPVV---SVNPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLK 436
Cdd:cd05917 154 TETSPVStqtRTDDSIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 437 TGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVM 516
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIK 313
|
330 340 350
....*....|....*....|....*....|....*.
gi 15598495 517 QHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05917 314 AYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
28-554 |
2.93e-82 |
|
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: 266.63 E-value: 2.93e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 28 SVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNP 107
Cdd:COG1021 29 DLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 108 LYTARELEHQFNDSGAKAVVCLA--------NMAHLVEGVLPktGVKQVIVteVGDilPPlkrfivnfvvkhikkmvPAY 179
Cdd:COG1021 108 AHRRAEISHFAEQSEAVAYIIPDrhrgfdyrALARELQAEVP--SLRHVLV--VGD--AG-----------------EFT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 180 SLpqatkltDALARGAGkSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIApLP 259
Cdd:COG1021 165 SL-------DALLAAPA-DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICG--LDADTVYLAA-LP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTfhC---MAMMLTGNHNILITNPrDLPSMLKDLGQWKFTgFVGL-NTLFVALCNNETFRKLDFSALKLTLSGG 335
Cdd:COG1021 234 AAHNFPLS--SpgvLGVLYAGGTVVLAPDP-SPDTAFPLIERERVT-VTALvPPLALLWLDAAERSRYDLSSLRVLQVGG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 MALQLATAERWKEVTGCAICEGYGMTE-----TAPVVSVNpfqnIQVGTIGIPvpstLC-----KVIGDDGQEVPLGERG 405
Cdd:COG1021 310 AKLSPELARRVRPALGCTLQQVFGMAEglvnyTRLDDPEE----VILTTQGRP----ISpddevRIVDEDGNPVPPGEVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 406 ELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCA 485
Cdd:COG1021 382 ELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAA 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 486 AIGIPDEKSGESIKVFVVVKpGATLTKEQVMQHMHD-NLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:COG1021 462 VVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
3-558 |
1.03e-81 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 265.69 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 3 ENFWKDKYPAGIAaeinPDQYPNILSVLKEScQRFATKPAFTN--LGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAV 80
Cdd:PLN02330 12 EHIFRSRYPSVPV----PDKLTLPDFVLQDA-ELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 81 QLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVlpktGVKQVIVTEVGDilppl 160
Cdd:PLN02330 86 VLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL----GLPVIVLGEEKI----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 161 kRFIVNFvvkhikkmvpayslpqaTKLTDALARGAGKSFQEAAPQADDVAvLQYTGGTTGVAKGAMLTHRNLVANMlqCK 240
Cdd:PLN02330 157 -EGAVNW-----------------KELLEAADRAGDTSDNEEILQTDLCA-LPFSSGTTGISKGVMLTHRNLVANL--CS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 241 ALMGAnlneGCEIL-----IAPLPLYHIYAFTFHCMAMMlTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALC 315
Cdd:PLN02330 216 SLFSV----GPEMIgqvvtLGLIPFFHIYGITGICCATL-RNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 316 NNETFRKLDFSALKL----TLSGGMALQLATAERwKEVTGCAICEGYGMTETAPVVSV--NPFQNIQVG---TIGIPVPS 386
Cdd:PLN02330 291 KNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFE-AKFPGVQVQEAYGLTEHSCITLThgDPEKGHGIAkknSVGFILPN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 387 TLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFN 465
Cdd:PLN02330 370 LEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 466 VYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGK 545
Cdd:PLN02330 450 VAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
|
570
....*....|...
gi 15598495 546 ILRRELRDEELKK 558
Cdd:PLN02330 530 IMRRLLKEKMLSI 542
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
28-553 |
3.35e-81 |
|
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: 264.00 E-value: 3.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 28 SVLKESCQRFATKP---AFTN--LGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIV 102
Cdd:cd17642 18 EQLHKAMKRYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 103 VNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVteVGDILPPLKRF--IVNFVVKHIKKMVPAYS 180
Cdd:cd17642 97 APTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTII--ILDSKEDYKGYqcLYTFITQNLPPGFNEYD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 181 LPQatkltdalargagksfqEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCK-ALMGANLNEGCEILIApLP 259
Cdd:cd17642 175 FKP-----------------PSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARdPIFGNQIIPDTAILTV-IP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHiyAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQ 339
Cdd:cd17642 237 FHH--GFGMFTTLGYLICGFRVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LATAERWKEVTGC-AICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKG 417
Cdd:cd17642 315 KEVGEAVAKRFKLpGIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 418 YWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGES 497
Cdd:cd17642 395 YVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGEL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 498 IKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPK-AVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd17642 475 PAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
45-561 |
3.44e-81 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 264.30 E-value: 3.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 45 NLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAK 124
Cdd:PRK06087 45 NHGASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVClanmahlvegvlpKTGVKQV----IVTEVGDILPPLKRFIVnfvvkhIKKMVPAYSLPQATKLtdaLARGagKSFQ 200
Cdd:PRK06087 124 MFFA-------------PTLFKQTrpvdLILPLQNQLPQLQQIVG------VDKLAPATSSLSLSQI---IADY--EPLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 EAAP-QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ-CKALmgaNLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGN 278
Cdd:PRK06087 180 TAITtHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAyCARL---NLTWQ-DVFMMPAPLGHATGFLHGVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNIL--ITNPRdlpSMLKDLGQWKFTGFVGLnTLFV--ALCNNETfRKLDFSALKLTLSGGMALQLATAERWKEvTGCAI 354
Cdd:PRK06087 256 RSVLldIFTPD---ACLALLEQQRCTCMLGA-TPFIydLLNLLEK-QPADLSALRFFLCGGTTIPKKVARECQQ-RGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 355 CEGYGMTETAPVVSVNPFQNIQ--VGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAD 432
Cdd:PRK06087 330 LSVYGSTESSPHAVVNLDDPLSrfMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 433 GWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVK-PGATLT 511
Cdd:PRK06087 410 GWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKaPHHSLT 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15598495 512 KEQVMQHM-HDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQ 561
Cdd:PRK06087 490 LEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQ 540
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-552 |
1.53e-79 |
|
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: 256.06 E-value: 1.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQHTDlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCla 130
Cdd:cd05934 5 TYAELLRESARIAAALAALGI-RPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 131 nmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapqadDVA 210
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 211 VLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILItnPRDLP 290
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTFAGYYSARRFG--LGED-DVYLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFSA 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 291 S-MLKDLGQWKFTGFVGLNTLFVALCNNEtfRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSV 369
Cdd:cd05934 160 SrFWSDVRRYGATVTNYLGAMLSYLLAQP--PSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 370 NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVK---GPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQED 446
Cdd:cd05934 238 PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDAD 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGY 526
Cdd:cd05934 317 GFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYF 396
|
490 500
....*....|....*....|....*.
gi 15598495 527 KRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05934 397 KVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-553 |
5.64e-77 |
|
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: 249.56 E-value: 5.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCl 129
Cdd:cd05972 1 WSFRELKRESAKAANVLAKL-GLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 130 anmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapQADDV 209
Cdd:cd05972 79 ---------------------------------------------------------------------------DAEDP 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 210 AVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEI---LIAPLPLYHIYaFTFhcMAMMLTGNHNILITNP 286
Cdd:cd05972 84 ALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLG--LRPD-DIhwnIADPGWAKGAW-SSF--FGPWLLGATVFVYEGP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RDLPS-MLKDLGQWKFTGFVGLNTLFVALCNNETFRkLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAP 365
Cdd:cd05972 158 RFDAErILELLERYGVTSFCGPPTAYRMLIKQDLSS-YKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 366 VVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVK--GPQVMKGYWQRQEATDEILdADGWLKTGDIAII 443
Cdd:cd05972 237 TVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDYYLTGDRAYR 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 444 QEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT---KEQVMQHMH 520
Cdd:cd05972 316 DEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelAEELQGHVK 395
|
490 500 510
....*....|....*....|....*....|...
gi 15598495 521 DNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05972 396 KVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
51-553 |
6.58e-76 |
|
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: 249.47 E-value: 6.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLiVVNT-NPLYTARELEHQFNDSGAKAVVCL 129
Cdd:cd12119 27 TYAEVAERARRLANALRR-LGVKPGDRVATLAWNTHRHLELYYAVPGMGA-VLHTiNPRLFPEQIAYIINHAEDRVVFVD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 130 ANMAHLVEGVLPKtgvkqvivtevgdiLPPLKRFIVNFVVKHIkkmvPAYSLPQATKLTDALARGAGKsfqEAAPQAD-- 207
Cdd:cd12119 105 RDFLPLLEAIAPR--------------LPTVEHVVVMTDDAAM----PEPAGVGVLAYEELLAAESPE---YDWPDFDen 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILIApLPLYHIYAFTFHCMAMMLTGNHniLITNPR 287
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHAMAALLTDGLGLSESDVVLPV-VPMFHVNAWGLPYAAAMVGAKL--VLPGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLP-SMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTETAPV 366
Cdd:cd12119 241 LDPaSLAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETSPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 367 VSVNPFQNIQVG-----------TIGIPVPSTLCKVIGDDGQEVPL--GERGELCVKGPQVMKGYWQRQEATDEiLDADG 433
Cdd:cd12119 320 GTVARPPSEHSNlsedeqlalraKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEA-LTEDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE 513
Cdd:cd12119 399 WLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15598495 514 QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd12119 479 ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
48-488 |
1.69e-75 |
|
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: 246.35 E-value: 1.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLY---TARELEHQFNDSGAK 124
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVclanmahlvegvlpktgvkqvivteVGDilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaap 204
Cdd:cd05907 80 ALF-------------------------VED------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 qADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGAnlnEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHNILIT 284
Cdd:cd05907 86 -PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA---TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 NPRDLPSMLKDLgqwKFTGFVGLNTLFVALCNN-------ETFRKLDFSA----LKLTLSGGMALQLATAERWKEVtGCA 353
Cdd:cd05907 162 SAETLLDDLSEV---RPTVFLAVPRVWEKVYAAikvkavpGLKRKLFDLAvggrLRFAASGGAPLPAELLHFFRAL-GIP 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKvIGDDGqevplgergELCVKGPQVMKGYWQRQEATDEILDADG 433
Cdd:cd05907 238 VYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVR-IADDG---------EILVRGPNVMLGYYKNPEATAEALDADG 307
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:cd05907 308 WLHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
46-553 |
2.41e-73 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 242.02 E-value: 2.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 46 LGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKA 125
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRR-GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 126 VVCLANMAHLvegvlpktgvkqvivtevGDILPPLKRFIvnfvvkhikkmvpayslpqatkltdALARGAGKSFQEAAPq 205
Cdd:PRK09088 98 LLGDDAVAAG------------------RTDVEDLAAFI-------------------------ASADALEPADTPSIP- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCkALMGANLNEgcEILIAPLPLYHIYAFTFHCMAMMLTGNhNILITN 285
Cdd:PRK09088 134 PERVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRVDAH--SSFLCDAPMFHIIGLITSVRPVLAVGG-SILVSN 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLPSMLKDLGQWKF--TGFVGLNTLFVALCNNETFrklDFSALK-LT--LSGGmALQLATAERWKEVTGCAICEGYGM 360
Cdd:PRK09088 210 GFEPKRTLGRLGDPALgiTHYFCVPQMAQAFRAQPGF---DAAALRhLTalFTGG-APHAAEDILGWLDDGIPMVDGFGM 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 361 TETAPV--VSVNP-FQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKT 437
Cdd:PRK09088 286 SEAGTVfgMSVDCdVIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 438 GDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQ 517
Cdd:PRK09088 366 GDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRS 445
|
490 500 510
....*....|....*....|....*....|....*.
gi 15598495 518 HMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
47-553 |
4.55e-73 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 243.21 E-value: 4.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGakav 126
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCS---- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHLVEGVLPKTGVKQVIVTEVG---DILPPLKRFivNFVVKHIKKMVPAYSLPQatkltdalargagksfqeaa 203
Cdd:PLN02574 140 VGLAFTSPENVEKLSPLGVPVIGVPENYdfdSKRIEFPKF--YELIKEDFDFVPKPVIKQ-------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 204 pqaDDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQCKALMGANLNE--GCE-ILIAPLPLYHIYAFTFHCMAMMLTGNhN 280
Cdd:PLN02574 198 ---DDVAAIMYSSGTTGASKGVVLTHRNLIA-MVELFVRFEASQYEypGSDnVYLAALPMFHIYGLSLFVVGLLSLGS-T 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNN-ETFRKLDFSALKLTLSGGMALQLATAERWKEV-TGCAICEGY 358
Cdd:PLN02574 273 IVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTlPHVDFIQGY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVS--VNPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWL 435
Cdd:PLN02574 353 GMTESTAVGTrgFNTEKLSKYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 436 KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQV 515
Cdd:PLN02574 433 RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAV 512
|
490 500 510
....*....|....*....|....*....|....*...
gi 15598495 516 MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PLN02574 513 INYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
40-552 |
5.58e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 240.06 E-value: 5.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:PRK07786 33 APALRFLGNTTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVclanmahlVEGVLpktgvkQVIVTEVGDILPPLKRFIVnfvvkhikkmvpAYSLPQATKLT-DALARGAGKS 198
Cdd:PRK07786 112 DCGAHVVV--------TEAAL------APVATAVRDIVPLLSTVVV------------AGGSSDDSVLGyEDLLAEAGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 199 FQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgcEILIAPLPLYHIYAFTFHCMAMMLTGN 278
Cdd:PRK07786 166 HAPVDIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINS--DVGFVGVPLFHIAGIGSMLPGLLLGAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDfsaLKL-TLSGGMALQLATAERWKEVT--GCAIC 355
Cdd:PRK07786 244 TVIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRD---LALrVLSWGAAPASDTLLRQMAATfpEAQIL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 356 EGYGMTETAPVVSVNPFQNI--QVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAdG 433
Cdd:PRK07786 321 AAFGQTEMSPVTCMLLGEDAirKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-G 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGE-SIKVFVVVKPGATLTK 512
Cdd:PRK07786 400 WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEvPVAVAAVRNDDAALTL 479
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 15598495 513 EQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK07786 480 EDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
40-552 |
2.82e-71 |
|
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: 235.06 E-value: 2.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqATKLTdalargagksf 199
Cdd:cd05958 81 KARITVALC-------------------------------------------------------AHALT----------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQCKALMGANLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNH 279
Cdd:cd05958 95 -----ASDDICILAFTSGTTGAPKATMHFHRDPLA-SADRYAVNVLRLRED-DRFVGSPPLAFTFGLGGVLLFPFGVGAS 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILItnPRDLPS-MLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGY 358
Cdd:cd05958 168 GVLL--EEATPDlLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGI 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQvmkGYWQRQEATDEILDADGWLKTG 438
Cdd:cd05958 246 GSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGAT---LTKEQV 515
Cdd:cd05958 323 DTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIpgpVLAREL 402
|
490 500 510
....*....|....*....|....*....|....*..
gi 15598495 516 MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05958 403 QDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
11-556 |
3.08e-71 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 238.03 E-value: 3.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 11 PAGIAAEINPDQYPN--ILSVLKESCQRFATKPAFTNLGK------TLTYGELYKLSGDFAAYLqqhTDL--KPGDRIAV 80
Cdd:PRK13295 9 PPRRAASIAAGHWHDrtINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGL---ARLgvGRGDVVSC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 81 QLPNVLQYPIVVFGAMRAGLIvvnTNPL---YTARELEHQFNDSGAKAVVC--------LANMAHLVEGVLPKtgVKQVI 149
Cdd:PRK13295 86 QLPNWWEFTVLYLACSRIGAV---LNPLmpiFRERELSFMLKHAESKVLVVpktfrgfdHAAMARRLRPELPA--LRHVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 150 VTEvGDILPPLKRFIvnfvvkhikkMVPAYSLpqatkltdalARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTH 229
Cdd:PRK13295 161 VVG-GDGADSFEALL----------ITPAWEQ----------EPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 230 RNLVANMLQCKALMGanLNEGCEILIAPlPLYHIYAFTFHCMAMMLTGNHNIL--ITNPRDLPSMLKDLGqwkfTGFVGL 307
Cdd:PRK13295 220 NTLMANIVPYAERLG--LGADDVILMAS-PMAHQTGFMYGLMMPVMLGATAVLqdIWDPARAAELIRTEG----VTFTMA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 308 NTLFVA-LCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQV--GTIGIPV 384
Cdd:PRK13295 293 STPFLTdLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERasTTDGCPL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 385 PSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEilDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGF 464
Cdd:PRK13295 373 PGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 465 NVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVM-----QHMHDNLTgykrPKAVEFRDSLP 539
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVeflkaQKVAKQYI----PERLVVRDALP 526
|
570 580
....*....|....*....|.
gi 15598495 540 TTNVGKI----LRRELRDEEL 556
Cdd:PRK13295 527 RTPSGKIqkfrLREMLRGEDA 547
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
40-553 |
5.35e-71 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 236.27 E-value: 5.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:TIGR02262 21 KTAFIDDISSLSYGELEAQVRRLAAALRR-LGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVCLANMAHLVEGVLPKT-GVKQVIVteVGDILPPLKRFiVNFVVKHikkmvpayslpqatkltdalargaGKS 198
Cdd:TIGR02262 100 DSRARVVFVSGALLPVIKAALGKSpHLEHRVV--VGRPEAGEVQL-AELLATE------------------------SEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 199 FQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQCKALMGANLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGN 278
Cdd:TIGR02262 153 FKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYW-TAELYARNTLGIRED-DVCFSAAKLFFAYGLGNALTFPMSVGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGY 358
Cdd:TIGR02262 231 TTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAAMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAdGWLKTG 438
Cdd:TIGR02262 311 GSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQG-EWTRSG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQH 518
Cdd:TIGR02262 390 DKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEH 469
|
490 500 510
....*....|....*....|....*....|....*
gi 15598495 519 MHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:TIGR02262 470 VKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
208-548 |
1.18e-70 |
|
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: 230.08 E-value: 1.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALmgANLNEGCEILIAPlPLYHIYAFTFHCMAMMLTGNhNILITNPR 287
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADC--ADLTEDDRYLIIN-PFFHTFGYKAGIVACLLTGA-TVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGC-AICEGYGMTETAPV 366
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 367 VSVNPFQNIQVgtigipVPSTLCKVIgdDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQED 446
Cdd:cd17638 157 TMCRPGDDAET------VATTCGRAC--PGFEVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDER 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 447 GYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGY 526
Cdd:cd17638 229 GYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLANY 308
|
330 340
....*....|....*....|..
gi 15598495 527 KRPKAVEFRDSLPTTNVGKILR 548
Cdd:cd17638 309 KVPRFVRFLDELPRNASGKVMK 330
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
49-552 |
2.49e-69 |
|
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: 229.96 E-value: 2.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKavvc 128
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAA-LGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 lanmahlvegvlpktgvkqvivtevgdilpplkrfiVNFVVKHIKKMVPAyslpqatkltdalargagksfqeaaPQADD 208
Cdd:cd05903 76 ------------------------------------VFVVPERFRQFDPA-------------------------AMPDA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 209 VAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIaPLPLYHIYAFTFHCMAMMLTGNHNIL--ITNP 286
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDVFLV-ASPMAHQTGFVYGFTLPLLLGAPVVLqdIWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RDLPSMLKDLGqwkfTGFVGLNTLFVA-LCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAP 365
Cdd:cd05903 172 DKALALMREHG----VTFMMGATPFLTdLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 366 VVSV--NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDaDGWLKTGDIAII 443
Cdd:cd05903 248 AVTSitPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 444 QEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHM-HDN 522
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQG 406
|
490 500 510
....*....|....*....|....*....|
gi 15598495 523 LTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
47-562 |
5.46e-69 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 230.95 E-value: 5.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHLVEGvlpktgvkqvIVTEVGDILPPLkrfivnfvvkhikkMVPAYSLPQATKLTDALARgagksfQEAAPQA 206
Cdd:PRK08276 88 IVSAALADTAAE----------LAAELPAGVPLL--------------LVVAGPVPGFRSYEEALAA------QPDTPIA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVA--VLQYTGGTTGVAKGAM--LTHRNL--VANMLQCKALMGANLNEGCeILIAPLPLYHIYAFTFHCMAMMLTGNhn 280
Cdd:PRK08276 138 DETAgaDMLYSSGTTGRPKGIKrpLPGLDPdeAPGMMLALLGFGMYGGPDS-VYLSPAPLYHTAPLRFGMSALALGGT-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 iLITNPR-DLPSMLK-------DLGQWKFTGFVGLNTLfvalcnNETFR-KLDFSALKLTLSGG----MALQLATAERWk 347
Cdd:PRK08276 215 -VVVMEKfDAEEALAlieryrvTHSQLVPTMFVRMLKL------PEEVRaRYDVSSLRVAIHAAapcpVEVKRAMIDWW- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 348 evtGCAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLcKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATD 426
Cdd:PRK08276 287 ---GPIIHEYYASSEGGGVTVITSEDWLaHPGSVGKAVLGEV-RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 427 EILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKP 506
Cdd:PRK08276 363 AARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAD 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 507 GATLTKE---QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQK 562
Cdd:PRK08276 443 GADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQRA 501
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
40-552 |
6.78e-69 |
|
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: 228.89 E-value: 6.78e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksf 199
Cdd:cd05919 80 DCEARLVVT----------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANM-LQCKALMGanLNEGCEILIAPlPLYHIYAFTFHCMAMMLTGN 278
Cdd:cd05919 89 -----SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALG--LTPGDRVFSSA-KMFFGYGLGNSLWFPLAVGA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGY 358
Cdd:cd05919 161 SAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTG 438
Cdd:cd05919 241 GATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYRTG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGAT---LTKEQV 515
Cdd:cd05919 320 DKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAApqeSLARDI 399
|
490 500 510
....*....|....*....|....*....|....*..
gi 15598495 516 MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05919 400 HRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
72-562 |
9.41e-69 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 230.36 E-value: 9.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 72 LKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKtGVKQVIVT 151
Cdd:PRK12406 33 VRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADLLHGLASALPA-GVTVLSVP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 152 EvgdilPPlkrfivnfvvkhikKMVPAYSLPQATKLTDALARGAGKSFQE----AAPQADDVAVLQYTGGTTGVAKG--- 224
Cdd:PRK12406 112 T-----PP--------------EIAAAYRISPALLTPPAGAIDWEGWLAQqepyDGPPVPQPQSMIYTSGTTGHPKGvrr 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 225 AMLTHRNLVANMLQCKALMGanLNEGCEILIaPLPLYHIYAFTFHCMAMMLTGNhniLITNPR-DLPSMLKDLGQWKFTG 303
Cdd:PRK12406 173 AAPTPEQAAAAEQMRALIYG--LKPGIRALL-TGPLYHSAPNAYGLRAGRLGGV---LVLQPRfDPEELLQLIERHRITH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 304 FVGLNTLFVALCN--NETFRKLDFSALKLTLSGGMA----LQLATAERWkevtGCAICEGYGMTETAPVVSVNPFQNI-Q 376
Cdd:PRK12406 247 MHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPcpadVKRAMIEWW----GPVIYEYYGSTESGAVTFATSEDALsH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 377 VGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMK-GYWQRQEATDEIlDADGWLKTGDIAIIQEDGYMRIVDRK 455
Cdd:PRK12406 323 PGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-DRGGFITSGDVGYLDADGYLFLCDRK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 456 KDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFR 535
Cdd:PRK12406 402 RDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIM 481
|
490 500
....*....|....*....|....*..
gi 15598495 536 DSLPTTNVGKILRRELRDEELKKAGQK 562
Cdd:PRK12406 482 AELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
25-561 |
4.98e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 226.46 E-value: 4.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 25 NILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVN 104
Cdd:PRK07470 8 NLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 105 TNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGvkqvivtevgdilpplkrfivnfvvkHIKKMVPAYSLPQA 184
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASP--------------------------DLTHVVAIGGARAG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 185 TKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNL---VANMLqCKaLMGANLNEGCEILIAPLPly 261
Cdd:PRK07470 141 LDYEALVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMafvITNHL-AD-LMPGTTEQDASLVVAPLS-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 262 hiYAFTFHCMAMMLTGNHNILITNPR-DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQL 340
Cdd:PRK07470 217 --HGAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 341 ATAERWKEVTGCAICEGYGMTE--------TAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGP 412
Cdd:PRK07470 295 ADQKRALAKLGKVLVQYFGLGEvtgnitvlPPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 413 QVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDE 492
Cdd:PRK07470 375 AVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDP 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 493 KSGEsIKVFVVV-KPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRdEELKKAGQ 561
Cdd:PRK07470 454 VWGE-VGVAVCVaRDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR-EELEERGL 521
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
40-555 |
3.89e-65 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 220.22 E-value: 3.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:PRK03640 18 RTAIEFEEKKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVCLANMAHLVegvlpkTGVKQVIVTEVGDilpplkrfivnfVVKHIKKMVPAYSLpqatkltdalargagksf 199
Cdd:PRK03640 97 DAEVKCLITDDDFEAKL------IPGISVKFAELMN------------GPKEEAEIQEEFDL------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeaapqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqckalMGANLNEGC---EILIAPLPLYHIYAFT------FHC 270
Cdd:PRK03640 141 -------DEVATIMYTSGTTGKPKGVIQTYGNHWWSA------VGSALNLGLtedDCWLAAVPIFHISGLSilmrsvIYG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 271 MAMMLTGN------HNIL----ITNPRDLPSMLKDLgqwkftgfvgLNTLFVALCNNeTFRKLdfsalkltLSGGMALQL 340
Cdd:PRK03640 208 MRVVLVEKfdaekiNKLLqtggVTIISVVSTMLQRL----------LERLGEGTYPS-SFRCM--------LLGGGPAPK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 341 ATAERWKEvTGCAICEGYGMTETAP-VVSVNP-FQNIQVGTIGIPV-PSTLCkvIGDDGQEVPLGERGELCVKGPQVMKG 417
Cdd:PRK03640 269 PLLEQCKE-KGIPVYQSYGMTETASqIVTLSPeDALTKLGSAGKPLfPCELK--IEKDGVVVPPFEEGEIVVKGPNVTKG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 418 YWQRQEATDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGES 497
Cdd:PRK03640 346 YLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQV 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 498 IKVFVVVkpGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:PRK03640 425 PVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-555 |
9.38e-65 |
|
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: 220.44 E-value: 9.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:cd05970 46 RIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 CLA--NMAHLVEGVLPKTGVKQVIVtEVGDILPplKRFIvNFVvKHIKKMVPAYSLPQAtkltdalargagksfqEAAPQ 205
Cdd:cd05970 125 AIAedNIPEEIEKAAPECPSKPKLV-WVGDPVP--EGWI-DFR-KLIKNASPDFERPTA----------------NSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKgaMLTHRNLVANMLQCKALMGANLNEGceiliaplPLYHIYAFTFHCMAMM-------LTGN 278
Cdd:cd05970 184 GEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREG--------GLHLTVADTGWGKAVWgkiygqwIAGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLP-SMLKDLGQWKFTGFVGLNTLFVALCNnETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEG 357
Cdd:cd05970 254 AVFVYDYDKFDPkALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 358 YGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCV---KGPQV--MKGYWQRQEATDEILDaD 432
Cdd:cd05970 333 FGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEVWH-D 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 433 GWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV----KPGA 508
Cdd:cd05970 412 GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLakgyEPSE 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598495 509 TLTKEqVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:cd05970 492 ELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
181-553 |
1.62e-64 |
|
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: 216.44 E-value: 1.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 181 LPQATKLTDA-LArgagksFQ--EAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGceiLIAP 257
Cdd:cd05912 54 VLLNTRLTPNeLA------FQlkDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDN---WLCA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 258 LPLYH-----------IYAFTFHCM---------AMMLTGNHNILITNPRDLPSMLKDLGQWKftgfvglntlfvalcnN 317
Cdd:cd05912 125 LPLFHisglsilmrsvIYGMTVYLVdkfdaeqvlHLINSGKVTIISVVPTMLQRLLEILGEGY----------------P 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 318 ETFRKLdfsalkltLSGGMALQLATAERWKEvTGCAICEGYGMTETAP-VVSVNP-FQNIQVGTIGIPVPSTLCKvIGDD 395
Cdd:cd05912 189 NNLRCI--------LLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETCSqIVTLSPeDALNKIGSAGKPLFPVELK-IEDD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 396 GQevPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
Cdd:cd05912 259 GQ--PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 476 ATLPGVLQCAAIGIPDEKSGESIKVFVVVKpgATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05912 336 LSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
208-548 |
5.94e-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: 212.52 E-value: 5.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYAFTFhCMAMMLTGNHNILItnPR 287
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTEA-DVYLNMLPLFHIAGLNL-ALATFHAGGANVVM--EK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPSMLKDLGQWKFTGFVG-----LNTLFVALCNNEtfrkLDFSALKLTLsgGMALQlATAERWKEVTGCAICEGYGMTE 362
Cdd:cd17637 75 FDPAEALELIEEEKVTLMGsfppiLSNLLDAAEKSG----VDLSSLRHVL--GLDAP-ETIQRFEETTGATFWSLYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 363 TAPVVSVNPFQNiQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDaDGWLKTGDIAI 442
Cdd:cd17637 148 TSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFR-NGWHHTGDLGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 443 IQEDGYMRIVDRK--KDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMH 520
Cdd:cd17637 226 FDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVG 305
|
330 340
....*....|....*....|....*...
gi 15598495 521 DNLTGYKRPKAVEFRDSLPTTNVGKILR 548
Cdd:cd17637 306 SRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
207-552 |
6.38e-64 |
|
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: 213.11 E-value: 6.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVAN--MLQCKALMGANlnegcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILIT 284
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDPD-----DVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 -----NPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRklDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYG 359
Cdd:cd05944 77 pagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 360 MTETAPVVSVNPFQN-IQVGTIGIPVPSTLCKVIGDDG-----QEVPLGERGELCVKGPQVMKGYWQrQEATDEILDADG 433
Cdd:cd05944 155 LTEATCLVAVNPPDGpKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICVAGPGVFGGYLY-TEGNKNAFVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE 513
Cdd:cd05944 234 WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE 313
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15598495 514 QVMQHMHDNLTgyKR---PKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05944 314 ELLAWARDHVP--ERaavPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-553 |
7.05e-64 |
|
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: 216.81 E-value: 7.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 46 LGKTLTYGELYKLSGDFAAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNplYTA--RELEHQFNDSGA 123
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAKMT--KEGENVGVMLPPSAGGALANFALALSGKVPVMLN--YTAglRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 124 KAVVC---LANMAHLVEGVLPKTGVKQVIVTEV-GDILPPLKRFIvnfvvKHIKKMVPAYSLPQATKLTDalargagksf 199
Cdd:cd05909 80 KTVLTskqFIEKLKLHHLFDVEYDARIVYLEDLrAKISKADKCKA-----FLAGKFPPKWLLRIFGVAPV---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHIYAFTFHCMAMMLTGNH 279
Cdd:cd05909 145 -----QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPED---VVFGALPFFHSFGLTGCLWLPLLSGIK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILITNP---RDLPSMLKDLgqwKFTGFVGLNTLFVALCNNETfrKLDFSALKLTLSGGMALQLATAERWKEVTGCAICE 356
Cdd:cd05909 217 VVFHPNPldyKKIPELIYDK---KATILLGTPTFLRGYARAAH--PEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 357 GYGMTETAPVVSVN-PFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGW 434
Cdd:cd05909 292 GYGTTECSPVISVNtPQSPNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGW 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 435 LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT-LPGVLQCAAIGIPDEKSGESIKVFVVvkpGATLTKE 513
Cdd:cd05909 371 YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDGRKGEKIVLLTT---TTDTDPS 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15598495 514 QVMQHMHD----NLTgykRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05909 448 SLNDILKNagisNLA---KPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
47-555 |
8.36e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 213.70 E-value: 8.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAylqqhtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:PRK07787 23 GRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VclanmahlveGVLPktgvkqvivtEVGDILPplkrfivnfvvkhikkMVPayslpqatklTDALARGAgksFQEAAPQA 206
Cdd:PRK07787 97 L----------GPAP----------DDPAGLP----------------HVP----------VRLHARSW---HRYPEPDP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcKALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNHniLITNP 286
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADL---DALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNR--FVHTG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLdFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPV 366
Cdd:PRK07787 203 RPTPEAYAQALSEGGTLYFGVPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 367 VSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPL-GER-GELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQ 444
Cdd:PRK07787 282 LSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVD 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 445 EDGYMRIVDRKK-DMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVvkPGATLTKEQVMQHMHDNL 523
Cdd:PRK07787 362 PDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQL 439
|
490 500 510
....*....|....*....|....*....|..
gi 15598495 524 TGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:PRK07787 440 SVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
48-553 |
3.17e-62 |
|
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: 211.14 E-value: 3.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKE-IGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 clanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatklTDAlargagksfqeaapqAD 207
Cdd:cd05971 84 ------------------------------------------------------------TDG---------------SD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRnlvanmlqckalmganlnegceILIAPLPLYHiyaFTFHCmammLTGNHNILITnPR 287
Cdd:cd05971 89 DPALIIYTSGTTGPPKGALHAHR----------------------VLLGHLPGVQ---FPFNL----FPRDGDLYWT-PA 138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 D-----------LPSMLKDLG--QWKFTGFVGLNTLFVALCNNETFRKLDFSALKLtlsggMALQLATAERW-------- 346
Cdd:cd05971 139 DwawigglldvlLPSLYFGVPvlAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKM-----MRQQGEQLKHAqvklraia 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 --------------KEVTGCAICEGYGMTETAPVVSVNP-FQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKG 411
Cdd:cd05971 214 tggeslgeellgwaREQFGVEVNEFYGQTECNLVIGNCSaLFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVEL 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 412 PQ--VMKGYWQRQEATdEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGI 489
Cdd:cd05971 294 PDpvAFLGYWNNPSAT-EKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGI 372
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 490 PDEKSGESIKVFVVVKPGATLT---KEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05971 373 PDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
72-552 |
4.05e-62 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 213.01 E-value: 4.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 72 LKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTG--VKQVI 149
Cdd:PRK08008 59 IRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtpLRHIC 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 150 VTEVGDilpPLKRFIVNFvvkhikkmvpayslpqatklTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTH 229
Cdd:PRK08008 139 LTRVAL---PADDGVSSF--------------------TQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 230 RNL-------------------VANM------LQCKALMGANLNEGCEILIAPlplYHIYAF----------TFHCMAMM 274
Cdd:PRK08008 196 YNLrfagyysawqcalrdddvyLTVMpafhidCQCTAAMAAFSAGATFVLLEK---YSARAFwgqvckyratITECIPMM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 275 LtgnhnilitnpRDLpsMLKDLGQWKftgfvglntlfvalcNNETFRKLDFSalkltlsggmaLQLATAER--WKEVTGC 352
Cdd:PRK08008 273 I-----------RTL--MVQPPSAND---------------RQHCLREVMFY-----------LNLSDQEKdaFEERFGV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTETapVVSV---NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKG---PQVMKGYWQRQEATD 426
Cdd:PRK08008 314 RLLTSYGMTET--IVGIigdRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 427 EILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKP 506
Cdd:PRK08008 392 KVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 15598495 507 GATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK08008 472 GETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
27-553 |
1.13e-61 |
|
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: 211.00 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 27 LSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTN 106
Cdd:cd12118 7 LSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAA-LGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 107 PLYTARELEHQFNDSGAKAVvcLANMAHLVEgvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatk 186
Cdd:cd12118 86 TRLDAEEIAFILRHSEAKVL--FVDREFEYE------------------------------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 187 ltDALARGagKSFQEAAPQAD--DVAVLQYTGGTTGVAKGAMLTHRnlvanmlqckalmGANLNEGCEILIAPLPLYHIY 264
Cdd:cd12118 115 --DLLAEG--DPDFEWIPPADewDPIALNYTSGTTGRPKGVVYHHR-------------GAYLNALANILEWEMKQHPVY 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 265 AFT---FHC------MAMMLTGNHNILITNPrDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGG 335
Cdd:cd12118 178 LWTlpmFHCngwcfpWTVAAVGGTNVCLRKV-DAKAIYDLIEKHKVTHFCGAPTVLNMLANAPPSDARPLPHRVHVMTAG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 MALQLATAERWKEVtGCAICEGYGMTETAPVVSVNPFQNIQ----------------VGTIG------------IPVPSt 387
Cdd:cd12118 257 APPPAAVLAKMEEL-GFDVTHVYGLTETYGPATVCAWKPEWdelpteerarlkarqgVRYVGleevdvldpetmKPVPR- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 388 lckvigdDGQEVplgerGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVY 467
Cdd:cd12118 335 -------DGKTI-----GEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENIS 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 468 PNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDsLPTTNVGKIL 547
Cdd:cd12118 402 SVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQ 480
|
....*.
gi 15598495 548 RRELRD 553
Cdd:cd12118 481 KFVLRD 486
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
47-548 |
1.52e-60 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 207.29 E-value: 1.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapqa 206
Cdd:cd05914 84 FVSDE--------------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNP 286
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV--LLGKG-DKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKI 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RdlPSMLKDLGQWKFTGFVGLNTLFV-----------------------ALCNNETFRKLDFSAL--------KLTLSGG 335
Cdd:cd05914 166 P--SAKIIALAFAQVTPTLGVPVPLViekifkmdiipkltlkkfkfklaKKINNRKIRKLAFKKVheafggniKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 MALQLATAERWKEVtGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDgqevPLGERGELCVKGPQVM 415
Cdd:cd05914 244 AKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVM 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 416 KGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILV-SGFNVYPNELEDVLATLPGVLQcAAIGIPDEKS 494
Cdd:cd05914 319 KGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEKKL 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 495 ---------GESIKVFVVVKPGATLtKEQVMQHMHDNLTGYKR-PKAVEFRDSLPTTNVGKILR 548
Cdd:cd05914 398 valayidpdFLDVKALKQRNIIDAI-KWEVRDKVNQKVPNYKKiSKVKIVKEEFEKTPKGKIKR 460
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
28-551 |
2.10e-60 |
|
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: 207.57 E-value: 2.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 28 SVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNP 107
Cdd:cd05920 19 DLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRG-LGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 108 LYTARELEHqfndsgakavvclanmahlvegvlpktgvkqvivtevgdilpplkrfivnfVVKHIKkmVPAYSLPQATKL 187
Cdd:cd05920 98 SHRRSELSA---------------------------------------------------FCAHAE--AVAYIVPDRHAG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 188 TD--ALARgagksfQEAAPQADdVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHIYA 265
Cdd:cd05920 125 FDhrALAR------ELAESIPE-VALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDT---VYLAVLPAAHNFP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 266 FTfhCMAM---MLTGNHNILITNPRDLPSM-LKDLGQWKFTGFV-GLNTLFVALCNNetfRKLDFSALKLTLSGGMALQL 340
Cdd:cd05920 195 LA--CPGVlgtLLAGGRVVLAPDPSPDAAFpLIEREGVTVTALVpALVSLWLDAAAS---RRADLSSLRLLQVGGARLSP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 341 ATAERWKEVTGCAICEGYGMTE-----TAPVVSvnpfQNIQVGTIGIPV-PSTLCKVIGDDGQEVPLGERGELCVKGPQV 414
Cdd:cd05920 270 ALARRVPPVLGCTLQQVFGMAEgllnyTRLDDP----DEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKS 494
Cdd:cd05920 346 IRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELL 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 495 GESIKVFVVVKPgATLTKEQVMQHMHD-NLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd05920 426 GERSCAFVVLRD-PPPSAAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
49-553 |
1.10e-59 |
|
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: 207.09 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLY------TARELEHQFNDSG 122
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPpptpgrHAERLAAILADAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 123 AKAVVCLAnmAHLvegvlpkTGVKQVIVTEVGDILPPLKrfivnfvvkhikkmvpayslpqatkLTDALARGAGKSFQEA 202
Cdd:cd05931 99 PRVVLTTA--AAL-------AAVRAFAASRPAAGTPRLL-------------------------VVDLLPDTSAADWPPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 APQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNegcEILIAPLPLYHIYAFTFHCMAMMLTGNHNIL 282
Cdd:cd05931 145 SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPG---DVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ITnPRdlpSMLKDLGQW-----KFTGfvglnTLFVA------LC----NNETFRKLDFSALKLTLSGGMALQLATAERWK 347
Cdd:cd05931 222 MS-PA---AFLRRPLRWlrlisRYRA-----TISAApnfaydLCvrrvRDEDLEGLDLSSWRVALNGAEPVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 348 EV-TGC-----AICEGYGMTETAPVVSVNP--------------FQNIQVG------------TIGIPVPSTLCKVI-GD 394
Cdd:cd05931 293 EAfAPFgfrpeAFRPSYGLAEATLFVSGGPpgtgpvvlrvdrdaLAGRAVAvaaddpaarelvSCGRPLPDQEVRIVdPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 395 DGQEVPLGERGELCVKGPQVMKGYWQRQEATDEI------LDADGWLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVYP 468
Cdd:cd05931 373 TGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 469 NELEDVLATLPGVLQ---CAAIGIPDEKSGEsikVFVVVKPGATLTKEQVMQHMHD------NLTGYkRPKAVEF--RDS 537
Cdd:cd05931 452 QDIEATAEEAHPALRpgcVAAFSVPDDGEER---LVVVAEVERGADPADLAAIAAAiraavaREHGV-APADVVLvrPGS 527
|
570
....*....|....*.
gi 15598495 538 LPTTNVGKILRRELRD 553
Cdd:cd05931 528 IPRTSSGKIQRRACRA 543
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
49-555 |
1.57e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 206.70 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPN--VLQYPIVVFGamRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLAL-GVRAGDGVAVLARNhrGFVLALYAAG--KVGARIILLNTGFSGPQLAEVAAREGVKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPLkrfivnfvvkhikkmvpayslPQATKLTDALARGAGKSFQeAAPQA 206
Cdd:PRK07788 151 VYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSG---------------------STDETLDDLIAGSSTAPLP-KPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLqyTGGTTGVAKGAMLTHRNL---VANMLQcKALMGANlnegcEILIAPLPLYHIYAFTFHCMAMMLtGNHNILi 283
Cdd:PRK07788 209 GGIVIL--TSGTTGTPKGAPRPEPSPlapLAGLLS-RVPFRAG-----ETTLLPAPMFHATGWAHLTLAMAL-GSTVVL- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 284 tnPR--DLPSMLKDLGQWKFTGFVGLNTL---FVALcNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGY 358
Cdd:PRK07788 279 --RRrfDPEATLEDIAKHKATALVVVPVMlsrILDL-GPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVNPfQNIQV--GTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYwqrqeaTD----EIldAD 432
Cdd:PRK07788 356 GSTEVAFATIATP-EDLAEapGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDgrdkQI--ID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 433 GWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTK 512
Cdd:PRK07788 427 GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDE 506
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15598495 513 EQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:PRK07788 507 DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
29-554 |
4.86e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 205.38 E-value: 4.86e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 29 VLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPL 108
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 109 YTARELEHQFNDSGAKAVVC----LANMAHLVEGVLPKTGVkqVIVTEVGDILPPLKrfivnfvvkhikkmVPAYSLPQA 184
Cdd:PRK06155 105 LRGPQLEHILRNSGARLLVVeaalLAALEAADPGDLPLPAV--WLLDAPASVSVPAG--------------WSTAPLPPL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 185 TKLTDAlargagksfqeAAPQADDVAVLQYTGGTTGVAKGAMLTHrnlvANMLQCKALMGANLNEGC-EILIAPLPLYHI 263
Cdd:PRK06155 169 DAPAPA-----------AAVQPGDTAAILYTSGTTGPSKGVCCPH----AQFYWWGRNSAEDLEIGAdDVLYTTLPLFHT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 264 YAFTFHCMAMmLTGNHniLITNPRDLPS-MLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLAT 342
Cdd:PRK06155 234 NALNAFFQAL-LAGAT--YVLEPRFSASgFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 343 AERwkEVTGCAICEGYGMTETAPVVSVnPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQ---VMKGYW 419
Cdd:PRK06155 311 AFR--ERFGVDLLDGYGSTETNFVIAV-THGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 420 QRQEATDEILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIK 499
Cdd:PRK06155 388 GMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVM 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 15598495 500 VFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK06155 467 AAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
35-554 |
9.31e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 203.58 E-value: 9.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 35 QRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTAREL 114
Cdd:PRK06145 13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHA-RGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 115 EHQFNDSGAKAVVCLANMAhlvegVLPKTGVKQVIVTEvgdilpplkrfivnfvvkhikkmvpayslpQATKLTDALARG 194
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFD-----AIVALETPKIVIDA------------------------------AAQADSRRLAQG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 195 aGKSFQEAAPQA-DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGceiLIAPLPLYHIYAFTFHCMAM 273
Cdd:PRK06145 137 -GLEIPPQAAVApTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASER---LLVVGPLYHVGAFDLPGIAV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 274 MLTGNhNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEV-TGC 352
Cdd:PRK06145 213 LWVGG-TLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVfTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTETapvVSVNPFQNI-----QVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE 427
Cdd:PRK06145 292 RYIDAYGLTET---CSGDTLMEAgreieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 428 ILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPG 507
Cdd:PRK06145 369 AF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598495 508 ATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK06145 448 ATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
48-562 |
2.14e-58 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 201.82 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVv 127
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 clanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksFQEAAPqaD 207
Cdd:cd17640 82 -----------------------------------------------------------------------VVENDS--D 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHIYA-----FTFHC-MAMMLTgnhni 281
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD---RFLSILPIWHSYErsaeyFIFACgCSQAYT----- 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 282 litnprDLPSMLKDLGQWKFTGFVGLNTLFVALCNN--ETFRKLDFSA------------LKLTLSGGMALQLaTAERWK 347
Cdd:cd17640 161 ------SIRTLKDDLKRVKPHYIVSVPRLWESLYSGiqKQVSKSSPIKqflflfflsggiFKFGISGGGALPP-HVDTFF 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 348 EVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEV-PLGERGELCVKGPQVMKGYWQRQEATD 426
Cdd:cd17640 234 EAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATS 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 427 EILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLATLPGVLQCAAIGiPDEKsgesiKVFVVVK 505
Cdd:cd17640 314 KVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG-QDQK-----RLGALIV 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 506 PgatlTKEQVMQHMHDnlTGYKRPKavEFRDSLPTTNVGKILRRELRDEELKKAGQK 562
Cdd:cd17640 388 P----NFEELEKWAKE--SGVKLAN--DRSQLLASKKVLKLYKNEIKDEISNRPGFK 436
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
51-551 |
9.81e-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: 196.52 E-value: 9.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQHTDLKpGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLA 130
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRS-GSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 131 nmahlvegVLPKTGVKQVIVTEVGdilpplkrfivnfvvkhikkmvpaYSLPQATKLtdalargagksfqEAAPQADDVA 210
Cdd:TIGR01923 80 --------LLEEKDFQADSLDRIE------------------------AAGRYETSL-------------SASFNMDQIA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 211 VLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgCEILIapLPLYHI--YAFTFHCM------------AMMLT 276
Cdd:TIGR01923 115 TLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDD-NWLLS--LPLYHIsgLSILFRWLiegatlrivdkfNQLLE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 277 GNHNILITNPRDLPSMLKDLGQwkftgfvglntlfvALCNNETFRKLdfsalkltLSGGMALQLATAERWKEvTGCAICE 356
Cdd:TIGR01923 192 MIANERVTHISLVPTQLNRLLD--------------EGGHNENLRKI--------LLGGSAIPAPLIEEAQQ-YGLPIYL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 357 GYGMTETAP-VVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVplgerGELCVKGPQVMKGYWQRQEATdEILDADGWL 435
Cdd:TIGR01923 249 SYGMTETCSqVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELT-PAFEQQGWF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 436 KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKpgATLTKEQV 515
Cdd:TIGR01923 323 NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKL 400
|
490 500 510
....*....|....*....|....*....|....*.
gi 15598495 516 MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:TIGR01923 401 IAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
40-553 |
1.31e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 197.99 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAF--TNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQ 117
Cdd:PRK13391 13 KPAVimASTGEVVTYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 118 FNDSGAKAVVCLANMAHLVEGVLPKT-GVKQVIVTEVGDILPPLKRFivnfvvkhikkmvpayslpqatklTDALARgag 196
Cdd:PRK13391 92 VDDSGARALITSAAKLDVARALLKQCpGVRHRLVLDGDGELEGFVGY------------------------AEAVAG--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 197 ksfQEAAPQADDV--AVLQYTGGTTGVAKG--AMLTHRNLVANM---LQCKALMGanLNEGCeILIAPLPLYHIyAFTFH 269
Cdd:PRK13391 145 ---LPATPIADESlgTDMLYSSGTTGRPKGikRPLPEQPPDTPLpltAFLQRLWG--FRSDM-VYLSPAPLYHS-APQRA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 270 CMAMMLTGNHNILITNpRDLPSMLKDLGQWKFTGFVGLNTLFVALCN--NETFRKLDFSALKLTLSGGMALQLATAERWK 347
Cdd:PRK13391 218 VMLVIRLGGTVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 348 EVTGCAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLcKVIGDDGQEVPLGERGELCVKGPQVMKgYWQRQEATD 426
Cdd:PRK13391 297 DWWGPIIHEYYAATEGLGFTACDSEEWLaHPGTVGRAMFGDL-HILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 427 EILDADG-WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVV-- 503
Cdd:PRK13391 375 EARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQpv 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 15598495 504 --VKPGATLTKEqVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK13391 455 dgVDPGPALAAE-LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
214-541 |
6.95e-56 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 190.98 E-value: 6.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 214 YTGGTTGVAKGAMLTHRNLVANMLQckALMGANLNEGCeILIAPLPLYHIyAFTFHCMAMMLTGNHNILItnPR-DLPSM 292
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLAQALV--LAVLQAIDEGT-VFLNSGPLFHI-GTLMFTLATFHAGGTNVFV--RRvDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 293 LKDLGQWKFT-GFVGLNTL--FVALcnNETfRKLDFSALK--LTLSGGMALQLATAERWKEVTGcaiceGYGMTETAPVV 367
Cdd:cd17636 81 LELIEAERCThAFLLPPTIdqIVEL--NAD-GLYDLSSLRssPAAPEWNDMATVDTSPWGRKPG-----GYGQTEVMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 368 SVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDG 447
Cdd:cd17636 153 TFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTNDLGRREPDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 448 YMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYK 527
Cdd:cd17636 232 SLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYK 311
|
330
....*....|....
gi 15598495 528 RPKAVEFRDSLPTT 541
Cdd:cd17636 312 KPKSVEFADALPRT 325
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
63-552 |
1.65e-55 |
|
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: 193.81 E-value: 1.65e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 63 AAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAG----LIVVNTNPLYTARELEHQFNDSGAKAVVCLANMAhlveg 138
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 139 vlpktgvkqvivtevgdilpplkrfivnfvvKHIKKMVPAYSLPQATKLTDALaRGAGKSFQEAAPQADDVAVLQYTGGT 218
Cdd:cd05922 81 -------------------------------DRLRDALPASPDPGTVLDADGI-RAARASAPAHEVSHEDLALLLYTSGS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 219 TGVAKGAMLTHRNLVANMLQCKALMGanlNEGCEILIAPLPLYhiYAFTFHCMAMMLTGNHNILITNPRDLP-SMLKDLG 297
Cdd:cd05922 129 TGSPKLVRLSHQNLLANARSIAEYLG---ITADDRALTVLPLS--YDYGLSVLNTHLLRGATLVLTNDGVLDdAFWEDLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 298 QWKFTGFVGLNTLFvalcnnETFRKLDFSALKL------TLSGGmALQLATAERWKEV-TGCAICEGYGMTETAPVVSVN 370
Cdd:cd05922 204 EHGATGLAGVPSTY------AMLTRLGFDPAKLpslrylTQAGG-RLPQETIARLRELlPGAQVYVMYGQTEATRRMTYL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 371 PFQNI--QVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQR-QEATDEILDADGwLKTGDIAIIQEDG 447
Cdd:cd05922 277 PPERIleKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDpPYRRKEGRGGGV-LHTGDLARRDEDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 448 YMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEkSGESIKVFVVVKPGATLtkEQVMQHMHDNLTGYK 527
Cdd:cd05922 356 FLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDP-LGEKLALFVTAPDKIDP--KDVLRSLAERLPPYK 432
|
490 500
....*....|....*....|....*
gi 15598495 528 RPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05922 433 VPATVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
54-555 |
2.00e-54 |
|
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: 192.68 E-value: 2.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 54 ELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLANMA 133
Cdd:cd05928 46 ELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 134 HLVEGVLPKTgvkqvivtevgdilPPLKrfivnfvvkhIKKMVPAYSLPQATKLTDaLARGAGKSFQEAAPQADDVAVLQ 213
Cdd:cd05928 126 PEVDSVASEC--------------PSLK----------TKLLVSEKSRDGWLNFKE-LLNEASTEHHCVETGSQEPMAIY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 214 YTGGTTGVAKgaMLTHRnlvanmlQCKALMGANLNEGCEILIAPLPLYH-------IYAFTFHCMAMMLTGNHNILITNP 286
Cdd:cd05928 181 FTSGTTGSPK--MAEHS-------HSSLGLGLKVNGRYWLDLTASDIMWntsdtgwIKSAWSSLFEPWIQGACVFVHHLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 R-DLPSMLKDLGQWKFTGFVGLNTLFVALCNNEtFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAP 365
Cdd:cd05928 252 RfDPLVILKTLSSYPITTFCGAPTVYRMLVQQD-LSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 366 VVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVK-GPQ----VMKGYWQRQEATDEILDADGWLkTGDI 440
Cdd:cd05928 331 ICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDR 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 441 AIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPG------ATLTKEq 514
Cdd:cd05928 410 GIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQflshdpEQLTKE- 488
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15598495 515 VMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:cd05928 489 LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
50-551 |
8.07e-53 |
|
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: 187.33 E-value: 8.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVcL 129
Cdd:cd05923 29 LTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAV-I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 130 ANMAHLVEGVLPKTGVKQVIVTEVGDILPplkrfivnfvvkhikkmvpaYSlpqatkltdalargAGKSFQEAAPQADDV 209
Cdd:cd05923 107 AVDAQVMDAIFQSGVRVLALSDLVGLGEP--------------------ES--------------AGPLIEDPPREPEQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 210 AVLQYTGGTTGVAKGAMLTHRNLVANML----QCKALMGANlnegcEILIAPLPLYHIYAFtFHCMAMMLTGNHNILITN 285
Cdd:cd05923 153 AFVFYTSGTTGLPKGAVIPQRAAESRVLfmstQAGLRHGRH-----NVVLGLMPLYHVIGF-FAVLVAALALDGTYVVVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETap 365
Cdd:cd05923 227 EFDPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 366 vvsVNPF--QNIQVGTIGIPVPSTLCKV--IGDDGQE-VPLGERGELCVK--GPQVMKGYWQRQEATDEILdADGWLKTG 438
Cdd:cd05923 305 ---MNSLymRDARTGTEMRPGFFSEVRIvrIGGSPDEaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGaTLTKEQVMQH 518
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG-TLSADELDQF 459
|
490 500 510
....*....|....*....|....*....|....
gi 15598495 519 MHDN-LTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd05923 460 CRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
51-554 |
1.83e-52 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 187.65 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLA 130
Cdd:PRK06018 41 TYAQIHDRALKVSQALDR-DGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 131 NMAHLVEGVLPKtgvkqvivtevgdiLPPLKRFIVNFVVKHIkkmvPAYSLPQATKLTDALArGAGKSFQEAAPQADDVA 210
Cdd:PRK06018 120 TFVPILEKIADK--------------LPSVERYVVLTDAAHM----PQTTLKNAVAYEEWIA-EADGDFAWKTFDENTAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 211 VLQYTGGTTGVAKGAMLTHRnlvANMLQckALMGAN---LNEGCEILIAPL-PLYHIYAF--TFHCMAMmltgNHNILIT 284
Cdd:PRK06018 181 GMCYTSGTTGDPKGVLYSHR---SNVLH--ALMANNgdaLGTSAADTMLPVvPLFHANSWgiAFSAPSM----GTKLVMP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 NPR-DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTET 363
Cdd:PRK06018 252 GAKlDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVN----PFQNIQVG-------TIGIPVPSTLCKVIGDDGQEVPLGER--GELCVKGPQVMKGYWQrqeATDEILD 430
Cdd:PRK06018 331 SPLGTLAalkpPFSKLPGDarldvlqKQGYPPFGVEMKITDDAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 431 ADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATL 510
Cdd:PRK06018 408 DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15598495 511 TKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK06018 488 TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
38-556 |
4.55e-52 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 187.02 E-value: 4.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 38 ATKPAFTNLGK----TLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVvntNPLYTA-- 111
Cdd:PRK04319 58 KDKVALRYLDAsrkeKYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEAfm 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 112 -RELEHQFNDSGAKAVVCLANM-AHLVEGVLPKtgVKQV-IVTEVGDILPPLKRFivnfvvkhikkmvpayslpqatklt 188
Cdd:PRK04319 134 eEAVRDRLEDSEAKVLITTPALlERKPADDLPS--LKHVlLVGEDVEEGPGTLDF------------------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEG----CEI----------- 253
Cdd:PRK04319 187 NALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTGKYVL--DLHEDdvywCTAdpgwvtgtsyg 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 254 LIAPLplyhiyaftfhcmammLTGNHNILIT---NPRDLPSMLKDLGQ--WkFTGFVGLNTLFVAlcNNETFRKLDFSAL 328
Cdd:PRK04319 265 IFAPW----------------LNGATNVIDGgrfSPERWYRILEDYKVtvW-YTAPTAIRMLMGA--GDDLVKKYDLSSL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 329 KLTLSGGMALQlATAERW-KEVTGCAICEGYGMTETAPVVSVN-PFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGE 406
Cdd:PRK04319 326 RHILSVGEPLN-PEVVRWgMKVFGLPIHDNWWMTETGGIMIANyPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 407 LCVKG--PQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQC 484
Cdd:PRK04319 405 LAIKKgwPSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEA 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598495 485 AAIGIPDEKSGESIKVFVVVKPGATLT---KEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEEL 556
Cdd:PRK04319 484 GVIGKPDPVRGEIIKAFVALRPGYEPSeelKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWEL 558
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
32-546 |
1.28e-51 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 190.91 E-value: 1.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 32 ESCQRFATKPAFTN-LGKTLTYGELYKLSGDFAAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNplYT 110
Cdd:PRK08633 623 DTAKRNWSRLAVADsTGGELSYGKALTGALALARLLKREL--KDEENVGILLPPSVAGALANLALLLAGKVPVNLN--YT 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 111 ArelehqfNDSGAKAVVCLANMAHLV--EGVLPKTGVKQVIVTevgdiLPPLKRFIvnFV---------VKHIKKMVPAY 179
Cdd:PRK08633 699 A-------SEAALKSAIEQAQIKTVItsRKFLEKLKNKGFDLE-----LPENVKVI--YLedlkakiskVDKLTALLAAR 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 180 SLPQATkltdaLARGAGKSFqeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNegcEILIAPLP 259
Cdd:PRK08633 765 LLPARL-----LKRLYGPTF-----KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRND---DVILSSLP 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQ 339
Cdd:PRK08633 832 FFHSFGLTVTLWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLK 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LATAERWKEVTGCAICEGYGMTETAPVVSVN------PFQNIQV----GTIGIPVPSTLCKVIG-DDGQEVPLGERGELC 408
Cdd:PRK08633 912 PEVADAFEEKFGIRILEGYGATETSPVASVNlpdvlaADFKRQTgskeGSVGMPLPGVAVRIVDpETFEELPPGEDGLIL 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 409 VKGPQVMKGYWQRQEATDEIL---DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPG--VLQ 483
Cdd:PRK08633 992 IGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGgeEVV 1071
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 484 CAAIGIPDEKSGEsiKVFVVVKPGATlTKEQVMQHMHD-NLTGYKRPKAVEFRDSLPTTNVGKI 546
Cdd:PRK08633 1072 FAVTAVPDEKKGE--KLVVLHTCGAE-DVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-556 |
4.65e-51 |
|
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: 181.55 E-value: 4.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYTArelehqFndsgakavvcl 129
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSA------F----------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 130 anMAHLVEGVLPKTGVKQVIVTevgdilPPLKRfivnfvvkhikKMVPayslpqatkltdalargagksfqeaapqaDDV 209
Cdd:cd05969 60 --GPEAIRDRLENSEAKVLITT------EELYE-----------RTDP-----------------------------EDP 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 210 AVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanlnegceilIAPLPLYHIYA------FTFHCM-AMMLTGNHNIL 282
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLD----------LHPDDIYWCTAdpgwvtGTVYGIwAPWLNGVTNVV 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ITNPRDLPSMLKDLGQWKFTGFVGLNTLFVAL--CNNETFRKLDFSALKLTLSGGMALQlATAERW-KEVTGCAICEGYG 359
Cdd:cd05969 162 YEGRFDAESWYGIIERVKVTVWYTAPTAIRMLmkEGDELARKYDLSSLRFIHSVGEPLN-PEAIRWgMEVFGVPIHDTWW 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 360 MTETAPVVSVN-PFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKG--PQVMKGYWQRQEATDEILdADGWLK 436
Cdd:cd05969 241 QTETGSIMIANyPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-IDGWYL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 437 TGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT---KE 513
Cdd:cd05969 320 TGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSdelKE 399
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15598495 514 QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEEL 556
Cdd:cd05969 400 EIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKEL 442
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
27-554 |
5.09e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 183.61 E-value: 5.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 27 LSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVlqyPIVV---FGAMRAGlIVV 103
Cdd:PRK08162 21 LSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNI---PAMVeahFGVPMAG-AVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 104 NT-NPLYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDilpplkrfivnfvvkhikkmvPAYSLP 182
Cdd:PRK08162 96 NTlNTRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDD---------------------PEYPGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 183 QATKLTD--ALARGAGKSFQEAAPQAD-DVAVLQYTGGTTGVAKGAMLTHRnlvanmlqckalmGANLNEGCEILIAPLP 259
Cdd:PRK08162 155 RFIGALDyeAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVYHHR-------------GAYLNALSNILAWGMP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFT---FHC--------MAMMlTGNHNILitnpR--DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFS 326
Cdd:PRK08162 222 KHPVYLWTlpmFHCngwcfpwtVAAR-AGTNVCL----RkvDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGID 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 327 ALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTETAPVVSVNPFQ--------------NIQVGtIGIPVPSTLCKVI 392
Cdd:PRK08162 297 HPVHAMVAGAAPPAAVIAKMEEI-GFDLTHVYGLTETYGPATVCAWQpewdalplderaqlKARQG-VRYPLQEGVTVLD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 393 GDDGQEVPL-GER-GELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNE 470
Cdd:PRK08162 375 PDTMQPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 471 LEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFrDSLPTTNVGKILRRE 550
Cdd:PRK08162 454 VEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFV 532
|
....
gi 15598495 551 LRDE 554
Cdd:PRK08162 533 LREQ 536
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
47-551 |
1.47e-50 |
|
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: 180.03 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapQA 206
Cdd:cd05930 89 LT----------------------------------------------------------------------------DP 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGCEILiaplplyHIYAFTF----HCMAMMLTGNHNIL 282
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY--PLTPGDRVL-------QFTSFSFdvsvWEIFGALLAGATLV 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ITNP---RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRklDFSALKLTLSGGMALQLATAERWKEV-TGCAICEGY 358
Cdd:cd05930 164 VLPEevrKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELlPGARLVNLY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVN--PFQNIQVG--TIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE-----IL 429
Cdd:cd05930 242 GPTEATVDATYYrvPPDDEEDGrvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAErfvpnPF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 430 DADGWL-KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGA 508
Cdd:cd05930 322 GPGERMyRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGG 401
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 15598495 509 TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd05930 402 ELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-553 |
1.64e-50 |
|
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: 182.03 E-value: 1.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQH-TDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLY---TARELEHQFNDSGAKA 125
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLgGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLYdtlGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 126 VVCLANmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmVPAYSLPQATKLtdalarGAGKSFQEAAPQ 205
Cdd:cd05927 83 VFCDAG--------------------------------------------VKVYSLEEFEKL------GKKNKVPPPPPK 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC----KALMGANLNEgceILIAPLPLYHIYAFTFHCMAMMLTGNHNI 281
Cdd:cd05927 113 PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTD---VYISYLPLAHIFERVVEALFLYHGAKIGF 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 282 LITNPRDLPSMLKDLgqwKFTGFVG----------------------LNTLF-VAL------------CNNETFRKLDFS 326
Cdd:cd05927 190 YSGDIRLLLDDIKAL---KPTVFPGvprvlnriydkifnkvqakgplKRKLFnFALnyklaelrsgvvRASPFWDKLVFN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 327 ALK--------LTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIgddgqE 398
Cdd:cd05927 267 KIKqalggnvrLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLV-----D 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 399 VP------LGE--RGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMI-LVSGFNVYPN 469
Cdd:cd05927 342 VPemnydaKDPnpRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 470 ELEDVLATLPGVLQC-----------AAIGIPDEksgESIKVFVVVKPGATLTKEQVMQH----------MH-----DNL 523
Cdd:cd05927 422 KIENIYARSPFVAQIfvygdslksflVAIVVPDP---DVLKEWAASKGGGTGSFEELCKNpevkkailedLVrlgkeNGL 498
|
570 580 590
....*....|....*....|....*....|....*...
gi 15598495 524 TGYKRPKAVEF--------RDSLPTTNvgKILRRELRD 553
Cdd:cd05927 499 KGFEQVKAIHLepepfsveNGLLTPTF--KLKRPQLKK 534
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
208-553 |
2.85e-49 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 173.29 E-value: 2.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIApLPLYHI--YAFTFHCMammLTGNHNILITN 285
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG--FGGGDSWLLS-LPLYHVggLAILVRSL---LAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLpsmLKDLGQWKFTgFVGL--NTLFVALCNNETFRKLDfsALKLTLSGGMALQLATAERWKEvTGCAICEGYGMTET 363
Cdd:cd17630 75 NQAL---AEDLAPPGVT-HVSLvpTQLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVNPFQNIQVGTIGIPVPstlckvigddGQEVPLGERGELCVKGPQVMKGYWQRQEATDeiLDADGWLKTGDIAII 443
Cdd:cd17630 148 ASQVATKRPDGFGRGGVGVLLP----------GRELRIVEDGEIWVGGASLAMGYLRGQLVPE--FNEDGWFTTKDLGEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 444 QEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGEsiKVFVVVKPGATLTKEQVMQHMHDNL 523
Cdd:cd17630 216 HADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQ--RPVAVIVGRGPADPAELRAWLKDKL 293
|
330 340 350
....*....|....*....|....*....|
gi 15598495 524 TGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd17630 294 ARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
49-545 |
2.44e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 175.84 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVC 128
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 LANMAHLVEGVLPKT-GVKQVIVTEVGDILPPlkrfivnfvvkhikkmvpaysLPQATKLTDALARG-AGKSFQEaaPQA 206
Cdd:PRK07798 107 EREFAPRVAEVLPRLpKLRTLVVVEDGSGNDL---------------------LPGAVDYEDALAAGsPERDFGE--RSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLqYTGGTTGVAKGAMLTHRNLVanmlqcKALMG-------------------ANLNEGCEILIAPlPLYHiYAFT 267
Cdd:PRK07798 164 DDLYLL-YTGGTTGMPKGVMWRQEDIF------RVLLGgrdfatgepiedeeelakrAAAGPGMRRFPAP-PLMH-GAGQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 268 FHCMAMMLTGNHNILITNPR-DLPSMLKDLGQWK-----FTGFVGLNTLFVALCNNETFrklDFSALKLTLSGGMALQLA 341
Cdd:PRK07798 235 WAAFAALFSGQTVVLLPDVRfDADEVWRTIEREKvnvitIVGDAMARPLLDALEARGPY---DLSSLFAIASGGALFSPS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 342 TAERWKE-VTGCAICEGYGMTETApvvsvnpFQNIQVGTIGIPVPSTL-------CKVIGDDGQEVPLG--ERGELCVKG 411
Cdd:PRK07798 312 VKEALLElLPNVVLTDSIGSSETG-------FGGSGTVAKGAVHTGGPrftigprTVVLDEDGNPVEPGsgEIGWIARRG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 412 PqVMKGYWQRQEATDEIL-DADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:PRK07798 385 H-IPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 489 IPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGK 545
Cdd:PRK07798 464 VPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
195-553 |
2.21e-47 |
|
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: 172.18 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 195 AGKSFQEAAPQADDVA--VLQYTGGTTGVAKGAMlthRNLVANMLQCKALMGANLNEGC---EILIAPLPLYHIYAFTFh 269
Cdd:cd05929 111 AAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIK---RGLPGGPPDNDTLMAAALGFGPgadSVYLSPAPLYHAAPFRW- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 270 CMAMMLTGNHNILITNpRDLPSMLKDLGQWK--FTGFVglNTLFVALCN--NETFRKLDFSALKLTLSGGMALQLATAER 345
Cdd:cd05929 187 SMTALFMGGTLVLMEK-FDPEEFLRLIERYRvtFAQFV--PTMFVRLLKlpEAVRNAYDLSSLKRVIHAAAPCPPWVKEQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 WKEVTGCAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLCkVIGDDGQEVPLGERGELCVKGPQVmKGYWQRQEA 424
Cdd:cd05929 264 WIDWGGPIIWEYYGGTEGQGLTIINGEEWLtHPGSVGRAVLGKVH-ILDEDGNEVPPGEIGEVYFANGPG-FEYTNDPEK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 425 TDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV 504
Cdd:cd05929 342 TAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQP 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15598495 505 KPGA---TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05929 422 APGAdagTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
51-486 |
1.92e-46 |
|
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: 167.83 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLA 130
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 131 NMAHLVEGVLPktgvkqvivtevGDILPplkrfivnfvvkhikkmvpaySLPQATKLTDALARGAGksfqEAAPQADDVA 210
Cdd:TIGR01733 81 ALASRLAGLVL------------PVILL---------------------DPLELAALDDAPAPPPP----DAPSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 211 VLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILiaplpLYHIYAFTFHCMAMM--LTGNHNILITNPRD 288
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG--LDPDDRVL-----QFASLSFDASVEEIFgaLLAGATLVVPPEDE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 289 LPSMLKDLGQWKFTGFV-------GLNTLFVALcnnetfRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGM 360
Cdd:TIGR01733 197 ERDDAALLAALIAEHPVtvlnltpSLLALLAAA------LPPALASLRLVILGGEALTPALVDRWRARGPGArLINLYGP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 361 TETAPVVSVNPF-----QNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEAT------DEIL 429
Cdd:TIGR01733 271 TETTVWSTATLVdpddaPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTaerfvpDPFA 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 430 DADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAA 486
Cdd:TIGR01733 351 GGDGarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
12-553 |
2.15e-46 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 170.71 E-value: 2.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 12 AGIAAEINPDQYPNIL-----------SVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHTDLKPgDRIAV 80
Cdd:PRK13382 20 AGLIAPMRPDRYLRIVaamrregmgptSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEP-RVVGI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 81 QLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHqfndsgakavvclanmahlvegVLPKTGVKQVIVTEvgDILPPL 160
Cdd:PRK13382 99 MCRNHRGFVEALLAANRIGADILLLNTSFAGPALAE----------------------VVTREGVDTVIYDE--EFSATV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 161 KRFIVNfvVKHIKKMVpAYSLPQATKLTDALARGAGKSFQEAAPQADDVAVLqyTGGTTGVAKGAmltHRNLVANMLQCK 240
Cdd:PRK13382 155 DRALAD--CPQATRIV-AWTDEDHDLTVEVLIAAHAGQRPEPTGRKGRVILL--TSGTTGTPKGA---RRSGPGGIGTLK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 241 ALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTgnhNILITNPR-DLPSMLKDLGQWKFTGFVGLNTLFVALCN--N 317
Cdd:PRK13382 227 AILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLA---CTIVTRRRfDPEATLDLIDRHRATGLAVVPVMFDRIMDlpA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 318 ETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPfQNIQVG--TIGIPVPSTLCKVIGDD 395
Cdd:PRK13382 304 EVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIATATP-ADLRAApdTAGRPAEGTEIRILDQD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 396 GQEVPLGERGELCVKGPQVMKGYwqRQEATDEILDadGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
Cdd:PRK13382 383 FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTL 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 476 ATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK13382 459 ATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
42-553 |
2.68e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 170.69 E-value: 2.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 42 AFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDS 121
Cdd:PRK06164 28 ALIDEDRPLSRAELRALVDRLAAWLAA-QGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 122 GAKAVVCLA-----NMAHLVEGVLPktgvkqvivtevgDILPPLKRFIVnfvVKHIKKMVPAYSLPQATKLTDALARGAG 196
Cdd:PRK06164 107 RARWLVVWPgfkgiDFAAILAAVPP-------------DALPPLRAIAV---VDDAADATPAPAPGARVQLFALPDPAPP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 197 KSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHiyAFTFHCMAMMLT 276
Cdd:PRK06164 171 AAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGA---VLLAALPFCG--VFGFSTLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 277 GNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKlDFSALKL----TLSGGMALQLAtaerWKEVTGC 352
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLfgfaSFAPALGELAA----LARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTETAPVVSV----NPFQNIQVGTiGIPVPSTLCKVIGD--DGQEVPLGERGELCVKGPQVMKGYWQRQEATD 426
Cdd:PRK06164 321 PLTGLYGSSEVQALVALqpatDPVSVRIEGG-GRPASPEARVRARDpqDGALLPDGESGEIEIRAPSLMRGYLDNPDATA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 427 EILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIpdEKSGESIKV-FVVVK 505
Cdd:PRK06164 400 RALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKTVPVaFVIPT 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15598495 506 PGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTT---NVGKILRRELRD 553
Cdd:PRK06164 478 DGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLRE 528
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
24-549 |
3.46e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 170.07 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 24 PNILSVLKESCQRFATKPA--FTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLI 101
Cdd:PRK05852 16 PRIADLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTR-SGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 102 VVNTNPLYTARELEHQFNDSGAKAVvclanmahLVEGvlpktgvkqvivTEVGDILPPLKRFIVNFVvkhikkMVPAYSL 181
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVV--------LIDA------------DGPHDRAEPTTRWWPLTV------NVGGDSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 182 PQATKLTDALARGAGKSFQEAAPQA--DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKAlmGANLNEGcEILIAPLP 259
Cdd:PRK05852 149 PSGGTLSVHLDAATEPTPATSTPEGlrPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT--GYRLSPR-DATVAVMP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 260 LYHIYAFTFHCMAMMLTGNHNILITNPR----DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDfSALKLTLSGG 335
Cdd:PRK05852 226 LYHGHGLIAALLATLASGGAVLLPARGRfsahTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKP-AALRFIRSCS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 MALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVG-----TIGIPVPST--LCKVIGDDGQEVPLGERGELC 408
Cdd:PRK05852 305 APLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvvSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVW 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 409 VKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:PRK05852 385 LRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFG 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 489 IPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRR 549
Cdd:PRK05852 464 VPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-551 |
6.04e-46 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 167.42 E-value: 6.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 35 QRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTAREL 114
Cdd:cd05945 2 AANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 115 EHqfndsgakavvclanmahlvegVLPKTGVKQVIVTEvgdilpplkrfivnfvvkhikkmvpayslpqatkltdalarg 194
Cdd:cd05945 81 RE----------------------ILDAAKPALLIADG------------------------------------------ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 195 agksfqeaapqaDDVAVLQYTGGTTGVAKGAMLTHRNLVA---NMLQckalmGANLNEGCEILiaplplyHIYAFTFHCm 271
Cdd:cd05945 97 ------------DDNAYIIFTSGSTGRPKGVQISHDNLVSftnWMLS-----DFPLGPGDVFL-------NQAPFSFDL- 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 AMM-----------LTGNHNILITNPRDLPSMLKDLGqwkFTGFVGLNTlFVALC-NNETFRKLDFSALKLTLSGGMALQ 339
Cdd:cd05945 152 SVMdlypalasgatLVPVPRDATADPKQLFRFLAEHG---ITVWVSTPS-FAAMClLSPTFTPESLPSLRHFLFCGEVLP 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LATAERWKEVT-GCAICEGYGMTE-TAPVVSVNPFQNIQVG----TIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQ 413
Cdd:cd05945 228 HKTARALQQRFpDARIYNTYGPTEaTVAVTYIEVTPEVLDGydrlPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPS 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 414 VMKGYWQRQEATDEILDAD---GWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVypnELEDV---LATLPGVLQCAAI 487
Cdd:cd05945 308 VSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI---ELEEIeaaLRQVPGVKEAVVV 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 488 GIPDEKSGESIKVFVVVKPGA-----TLTKEQVMQHMHDnltgYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd05945 385 PKYKGEKVTELIAFVVPKPGAeagltKAIKAELAERLPP----YMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
214-548 |
8.66e-46 |
|
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: 163.73 E-value: 8.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 214 YTGGTTGVAKGAMLTHRNLVANMLQCKALMGANlneGCEILIAPLPLYHIYaFTFHCMAMMLTGNHNILITNpRDLPSML 293
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNIS---GEDAILAPGPLSHSL-FLYGAISALYLGGTFIGQRK-FNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 294 KDLGQWKFTGFVGLNTLFVALCNNETfrklDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETAPVVSVNPF 372
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALARTLE----PESKIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYGTSELSFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 373 QNIQVGTIGIPVPSTLCKVIGDDGqevplGERGELCVKGPQVMKGYWQRQEATdeildADGWLKTGDIAIIQEDGYMRIV 452
Cdd:cd17633 158 ESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSN-----PDGWMSVGDIGYVDEEGYLYLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 453 DRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGEsIKVFVVVkpGATLTKEQVMQHMHDNLTGYKRPKAV 532
Cdd:cd17633 228 GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGE-IAVALYS--GDKLTYKQLKRFLKQKLSRYEIPKKI 304
|
330
....*....|....*.
gi 15598495 533 EFRDSLPTTNVGKILR 548
Cdd:cd17633 305 IFVDSLPYTSSGKIAR 320
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-552 |
1.69e-44 |
|
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: 163.46 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYTA---RELEHQFNDSGAKAV 126
Cdd:cd05973 1 LTFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTAfgpKAIEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatKLTDalargagksfqeaapqa 206
Cdd:cd05973 77 VTDAANRH---------------------------------------------------KLDS----------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 dDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqckalMGANLNEGCEI--------LIAPLPLYHIYaftFHCMAMMLTGN 278
Cdd:cd05973 89 -DPFVMMFTSGTTGLPKGVPVPLRALAA--------FGAYLRDAVDLrpedsfwnAADPGWAYGLY---YAITGPLALGH 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKldfSALKLTL----SGGMALqlaTAE--RWKEVT-G 351
Cdd:cd05973 157 PTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVP---ARPKGRLrrvsSAGEPL---TPEviRWFDAAlG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 352 CAICEGYGMTETAPVVSVN--PFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCV---KGPQV-MKGYWQRQEAt 425
Cdd:cd05973 231 VPIHDHYGQTELGMVLANHhaLEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIdiaNSPLMwFRGYQLPDTP- 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 426 deilDADG-WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV 504
Cdd:cd05973 310 ----AIDGgYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVL 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 15598495 505 KPGATLTKE---QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05973 386 RGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
40-551 |
2.31e-44 |
|
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: 163.62 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd12116 3 ATAVRDDDRSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVCLANMAHlvegvlpktgvkqvivtevgdilpplkRFIVNFVVKHIKKMVPAYSLPQATkltdalargagksf 199
Cdd:cd12116 82 DAEPALVLTDDALPD---------------------------RLPAGLPVLLLALAAAAAAPAAPR-------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qeAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQCkalMGANLN--EGCEIL-IAPlplyhiYAFTFHCMAMML- 275
Cdd:cd12116 121 --TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLV-NFLHS---MRERLGlgPGDRLLaVTT------YAFDISLLELLLp 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 276 --TGNHNIL-----ITNPRDLPSMLKDLG----Q-----WKF---TGFVGLNTLfVALCnnetfrkldfsalkltlsGGM 336
Cdd:cd12116 189 llAGARVVIapretQRDPEALARLIEAHSitvmQatpatWRMlldAGWQGRAGL-TALC------------------GGE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 337 ALQLATAERWKEVTGCAIcEGYGMTETAPVVSVnpfQNIQVG----TIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGP 412
Cdd:cd12116 250 ALPPDLAARLLSRVGSLW-NLYGPTETTIWSTA---ARVTAAagpiPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGD 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 413 QVMKGYWQRQEATDEILDADG-------WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCA 485
Cdd:cd12116 326 GVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 486 AIGIPDEKSGEsIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd12116 406 VVVREDGGDRR-LVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
49-553 |
3.19e-44 |
|
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: 164.76 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDsgakavvc 128
Cdd:cd05906 39 FQSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNARLRK-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 LANMAHLVEgvlpktgvKQVIVTE---VGDILPPLKRFivnfvvkhikkmvpaySLPQATKLTDALARGAGKSFQEAAPQ 205
Cdd:cd05906 110 LRHIWQLLG--------SPVVLTDaelVAEFAGLETLS----------------GLPGIRVLSIEELLDTAADHDLPQSR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVAnMLQCKALMgANLNEGCEILIApLPLYHIYAFTF-HCMAMMLtGNHNI--- 281
Cdd:cd05906 166 PDDLALLMLTSGSTGFPKAVPLTHRNILA-RSAGKIQH-NGLTPQDVFLNW-VPLDHVGGLVElHLRAVYL-GCQQVhvp 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 282 ---LITNPRDLpsmLKDLGQWKFTGFVGLNTLFVALCN---NETFRKLDFSALKLTLSGGMALQLATAERWKE------V 349
Cdd:cd05906 242 teeILADPLRW---LDLIDRYRVTITWAPNFAFALLNDlleEIEDGTWDLSSLRYLVNAGEAVVAKTIRRLLRllepygL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TGCAICEGYGMTETAPVVSVN---PFQNIQVGT----IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQ 422
Cdd:cd05906 319 PPDAIRPAFGMTETCSGVIYSrsfPTYDHSQALefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 423 EATDEILDADGWLKTGDIAIIqEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQ--CAAIGIPDEKSG-ESIK 499
Cdd:cd05906 399 EANAEAFTEDGWFRTGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAEtEELA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 500 VFVVV------KPGATLT--KEQVMQHMHdnltgyKRPKAV--EFRDSLPTTNVGKILRRELRD 553
Cdd:cd05906 478 IFFVPeydlqdALSETLRaiRSVVSREVG------VSPAYLipLPKEEIPKTSLGKIQRSKLKA 535
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
48-484 |
5.05e-44 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 166.04 E-value: 5.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYtarelehqfnDS-GAKAV 126
Cdd:PLN02736 77 KWMTYGEAGTARTAIGSGLVQH-GIPKGACVGLYFINRPEWLIVDHACSAYSYVSV---PLY----------DTlGPDAV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHL-VEGVLPKTgvKQVIVTEVGDIlpPLKRFIVnfVVKHIKKMVPaySLPQAT-----KLTDALARGAGKSFQ 200
Cdd:PLN02736 143 KFIVNHAEVaAIFCVPQT--LNTLLSCLSEI--PSVRLIV--VVGGADEPLP--SLPSGTgveivTYSKLLAQGRSSPQP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 EAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqCKALMGANLNEGcEILIAPLPLYHIYaftfHCMAMMLTGNHN 280
Cdd:PLN02736 215 FRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANV--AGSSLSTKFYPS-DVHISYLPLAHIY----ERVNQIVMLHYG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPR-DLPSMLKDLGQWKFTGFVGLNTLF------------------------------VALCNNET----FRKLDF 325
Cdd:PLN02736 288 VAVGFYQgDNLKLMDDLAALRPTIFCSVPRLYnriydgitnavkesgglkerlfnaaynakkQALENGKNpspmWDRLVF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 326 SALKLTLSGGMALQLATA--------ERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIG---- 393
Cdd:PLN02736 368 NKIKAKLGGRVRFMSSGAsplspdvmEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpem 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 394 ---DDGQEVPlgeRGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMI-LVSGFNVYPN 469
Cdd:PLN02736 448 nytSEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPE 524
|
490
....*....|....*
gi 15598495 470 ELEDVLATLPGVLQC 484
Cdd:PLN02736 525 KIENVYAKCKFVAQC 539
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
47-552 |
7.10e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 160.17 E-value: 7.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:PRK13390 22 GEQVSYRQLDDDSAALARVLYD-AGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMahlvEGVLPKTGVKQVIVTEVGDILPPLKRFivnfvvkhikkmvpayslpqatkltDALARGAGKSFQEAaPQA 206
Cdd:PRK13390 101 VASAAL----DGLAAKVGADLPLRLSFGGEIDGFGSF-------------------------EAALAGAGPRLTEQ-PCG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 ddvAVLQYTGGTTGVAKGAM--LTHRNLVANMLQCKALMGANLN-EGCEILIAPLPLYHIYAFTFHCMAMMLTGNhnILI 283
Cdd:PRK13390 151 ---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDiSESDIYYSSAPIYHAAPLRWCSMVHALGGT--VVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 284 TNPRDLPSMLKDLGQWKFTGFVGLNTLFVALC--NNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMT 361
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSST 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 362 ETAPVVSVNPFQNI-QVGTIGIPVPSTLcKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADG--WLKTG 438
Cdd:PRK13390 306 EAHGMTFIDSPDWLaHPGSVGRSVLGDL-HICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVV----VKPGATLTKEq 514
Cdd:PRK13390 385 DLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQlvegIRGSDELARE- 463
|
490 500 510
....*....|....*....|....*....|....*...
gi 15598495 515 VMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK13390 464 LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-488 |
2.37e-42 |
|
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: 158.79 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVC- 128
Cdd:cd05932 7 FTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 ----LANMAHLVEGVLPKTgvkqvivtevgdILPPlkrfivnfvvkhikkmvpaYSLPQATKLTDALARGAGKSFQEAAP 204
Cdd:cd05932 86 klddWKAMAPGVPEGLISI------------SLPP-------------------PSAANCQYQWDDLIAQHPPLEERPTR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGceiLIAPLPLYHIYAFTFHCMAMMLTGnhnILIT 284
Cdd:cd05932 135 FPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDR---MLSYLPLAHVTERVFVEGGSLYGG---VLVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 NPRDLPSMLKDLGQWKFTGFVGLNTLFV-------------------------ALCNNETFRKLDFSALKLTLSGGMALQ 339
Cdd:cd05932 209 FAESLDTFVEDVQRARPTLFFSVPRLWTkfqqgvqdkipqqklnlllkipvvnSLVKRKVLKGLGLDQCRLAGCGSAPVP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LATAErWKEVTGCAICEGYGMTETAPVVSVN-PFQNiQVGTIGIPVPstlckvigddGQEVPLGERGELCVKGPQVMKGY 418
Cdd:cd05932 289 PALLE-WYRSLGLNILEAYGMTENFAYSHLNyPGRD-KIGTVGNAGP----------GVEVRISEDGEILVRSPALMMGY 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 419 WQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:cd05932 357 YKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
208-548 |
2.99e-42 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 154.73 E-value: 2.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQckaLMGANLNEGC-EILIAPLPLYHIYAFTFhcMAMMLTGNHNILITNP 286
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDI---LQKEGLNWVVgDVTYLPLPATHIGGLWW--ILTCLIHGGLCVTGGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 R-DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGmALQLATAERWKEVTGCA-ICEGYGMTETA 364
Cdd:cd17635 77 NtTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGG-SRAIAADVRFIEATGLTnTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 365 PVVSVnPFQN--IQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAI 442
Cdd:cd17635 156 TALCL-PTDDdsIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV-----KPGATLTKEQVmq 517
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeldENAIRALKHTI-- 311
|
330 340 350
....*....|....*....|....*....|.
gi 15598495 518 hmHDNLTGYKRPKAVEFRDSLPTTNVGKILR 548
Cdd:cd17635 312 --RRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
47-551 |
9.34e-42 |
|
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: 156.59 E-value: 9.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHLVEGVLPKTGVKQVIVTEVGDILPPlkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaAPQA 206
Cdd:cd12117 99 LTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAV-------------------------------------------PVSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKALMGANLNEGCEILI-APLPLYhiyAFTFHCMAMMLTGNHniLITN 285
Cdd:cd12117 136 DDLAYVMYTSGSTGRPKGVAVTHRGVVR---LVKNTNYVTLGPDDRVLQtSPLAFD---ASTFEIWGALLNGAR--LVLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLPSMLKDLGQwkFTGFVGLNTLFV--ALcnnetFRKLD------FSALKLTLSGGMALQLATAERWKEVT-GCAICE 356
Cdd:cd12117 208 PKGTLLDPDALGA--LIAEEGVTVLWLtaAL-----FNQLAdedpecFAGLRELLTGGEVVSPPHVRRVLAACpGLRLVN 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 357 GYGMTETAPV----VSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAD 432
Cdd:cd12117 281 GYGPTENTTFttshVVTELDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 433 GWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVvkP 506
Cdd:cd12117 361 PFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--A 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15598495 507 GATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd12117 439 EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
204-493 |
3.31e-41 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 155.84 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqckALMGANLNEGC---EILIAPLPLYHIYAFTFHcMAMMLTGNHn 280
Cdd:cd17639 85 GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGI----AGLGDRVPELLgpdDRYLAYLPLAHIFELAAE-NVCLYRGGT- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPRDLPSMLK-----DLGQWKFTGFVG---------------LN-------TLF----------------VALCNN 317
Cdd:cd17639 159 IGYGSPRTLTDKSKrgckgDLTEFKPTLMVGvpaiwdtirkgvlakLNpmgglkrTLFwtayqsklkalkegpgTPLLDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 318 ETF---RKLDFSALKLTLSGGMALQLATaERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIG- 393
Cdd:cd17639 239 LVFkkvRAALGGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDw 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 394 DDGQEVPLGE--RGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMI-LVSGFNVYPNE 470
Cdd:cd17639 318 EEGGYSTDKPppRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVkLQNGEYIALEK 397
|
330 340 350
....*....|....*....|....*....|....
gi 15598495 471 LEDVLATLPGVLQ-----------CAAIGIPDEK 493
Cdd:cd17639 398 LESIYRSNPLVNNicvyadpdksyPVAIVVPNEK 431
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
203-556 |
4.53e-41 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 156.11 E-value: 4.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 APqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHIYAFTfHCMAMMLTGNHNIL 282
Cdd:PLN02860 170 AP--DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDD---VYLHTAPLCHIGGLS-SALAMLMVGACHVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ItnPR-DLPSMLKDLGQWKFTGFVGLNTLFVALC--NNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGY 358
Cdd:PLN02860 244 L--PKfDAKAALQAIKQHNVTSMITVPAMMADLIslTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAY 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTET---------------APVVSVNPFQNIQ-------VGT-IGIPVPSTLCKVIGDDGQEVplgerGELCVKGPQVM 415
Cdd:PLN02860 322 GMTEAcssltfmtlhdptleSPKQTLQTVNQTKsssvhqpQGVcVGKPAPHVELKIGLDESSRV-----GRILTRGPHVM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 416 KGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSG 495
Cdd:PLN02860 397 LGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLT 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 496 ESIKVFVVVKPG--------------ATLTKEQVMQHMHD-NLTGYKRPKA-VEFRDSLPTTNVGKILRRELRDEEL 556
Cdd:PLN02860 477 EMVVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREkNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRREVL 553
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
41-551 |
8.30e-41 |
|
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: 153.23 E-value: 8.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 41 PAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFND 120
Cdd:cd17643 4 VAVVDEDRRLTYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 121 SGAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfq 200
Cdd:cd17643 83 SGPSLLLT------------------------------------------------------------------------ 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 eaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceiliaPLPLYHIYAFTFHCMAM---MLTG 277
Cdd:cd17643 91 ----DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD-------VWTLFHSYAFDFSVWEIwgaLLHG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 278 NHNILITN-----PRDLPSMLKDlgqwkfTGFVGLN---TLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEV 349
Cdd:cd17643 160 GRLVVVPYevarsPEDFARLLRD------EGVTVLNqtpSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TGCA---ICEGYGMTETAPVVSVNPFQN-----IQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQR 421
Cdd:cd17643 234 FGLDrpqLVNMYGITETTVHVTFRPLDAadlpaAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 422 QEATDE--ILDADG-----WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKS 494
Cdd:cd17643 314 PELTAErfVANPFGgpgsrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPG 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 495 GESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17643 394 DTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
35-552 |
1.88e-40 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 153.27 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 35 QRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTAREL 114
Cdd:cd17651 6 ARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 115 EHQFNDSGAKAVVclanmAHlvEGVLPKTGVKQVIVTEVGDilpplkrfivnfvvkhikkmvpaysLPQATKLTDALarg 194
Cdd:cd17651 85 AFMLADAGPVLVL-----TH--PALAGELAVELVAVTLLDQ-------------------------PGAAAGADAEP--- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 195 agksfqEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANML--QCKALMganlnegceiLIAPLPLYHIYAFTFHCMA 272
Cdd:cd17651 130 ------DPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-ANLVawQARASS----------LGPGARTLQFAGLGFDVSV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 273 M-----MLTGNHNILITNP--RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAER 345
Cdd:cd17651 193 QeifstLCAGATLVLPPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTEDLR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 --WKEVTGCAICEGYGMTE----TAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYW 419
Cdd:cd17651 273 efCAGLPGLRLHNHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 420 QRQEATDEILDADGWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEK 493
Cdd:cd17651 353 NRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 494 SGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd17651 433 GEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
72-554 |
5.92e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 152.55 E-value: 5.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 72 LKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSgAKAVVCL-ANMAHLVEGVLPKtgvkqviv 150
Cdd:PRK07008 61 VEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHA-EDRYVLFdLTFLPLVDALAPQ-------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 151 tevgdiLPPLKRFIVnfvvkhikkMVPAYSLP-QATKLTDALARGAGKSFQEAAPQADD--VAVLQYTGGTTGVAKGAML 227
Cdd:PRK07008 132 ------CPNVKGWVA---------MTDAAHLPaGSTPLLCYETLVGAQDGDYDWPRFDEnqASSLCYTSGTTGNPKGALY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 228 THRNLVANMlqckalMGANLNE--GCEILIAPLP---LYHIYAFTFHcMAMMLTGNHNILITNPRDLPSMLKDLGQWKFT 302
Cdd:PRK07008 197 SHRSTVLHA------YGAALPDamGLSARDAVLPvvpMFHVNAWGLP-YSAPLTGAKLVLPGPDLDGKSLYELIEAERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 303 GFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVG---- 378
Cdd:PRK07008 270 FSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLKWKHSQlpld 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 379 -------TIGIPVPSTLCKVIGDDGQEVPLGER--GELCVKGPQVMKGYWqRQEATDEIldaDGWLKTGDIAIIQEDGYM 449
Cdd:PRK07008 350 eqrklleKQGRVIYGVDMKIVGDDGRELPWDGKafGDLQVRGPWVIDRYF-RGDASPLV---DGWFPTGDVATIDADGFM 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 450 RIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRP 529
Cdd:PRK07008 426 QITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIP 505
|
490 500
....*....|....*....|....*
gi 15598495 530 KAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK07008 506 DDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
40-552 |
2.31e-39 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 150.91 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTnpLYTARELEhqfn 119
Cdd:PRK10946 39 AIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNA--LFSHQRSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 dsgakavvcLANMAHLVEGVLpktgvkqvivtEVGDILPPL---KRFIVNFVVKHIK-KMVPAYSLPQATKLTDALARGA 195
Cdd:PRK10946 112 ---------LNAYASQIEPAL-----------LIADRQHALfsdDDFLNTLVAEHSSlRVVLLLNDDGEHSLDDAINHPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 196 GKSFQEAAPqADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCkalmganlNEGCEI-----LIAPLPLYHIYAFT--- 267
Cdd:PRK10946 172 EDFTATPSP-ADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRS--------VEICGFtpqtrYLCALPAAHNYPMSspg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 268 ----FHCmammltGNHNILITNPRDLPSM-LKDLGQWKFTGFV-GLNTLFVALCNNETFRKlDFSALKLTLSGGMALQLA 341
Cdd:PRK10946 243 algvFLA------GGTVVLAPDPSATLCFpLIEKHQVNVTALVpPAVSLWLQAIAEGGSRA-QLASLKLLQVGGARLSET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 342 TAERWKEVTGCAICEGYGMTETApvvsVN------PFQNIqVGTIGIPV-PSTLCKVIGDDGQEVPLGERGELCVKGPQV 414
Cdd:PRK10946 316 LARRIPAELGCQLQQVFGMAEGL----VNytrlddSDERI-FTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKS 494
Cdd:PRK10946 391 FRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELM 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 495 GESIKVFVVVKPGatLTKEQVMQHMHD-NLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK10946 471 GEKSCAFLVVKEP--LKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
42-553 |
2.93e-39 |
|
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: 148.61 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 42 AFTNLGKTLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDS 121
Cdd:cd17653 15 AVESLGGSLTYGELDAASNALANRLLQLG-VVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 122 GAKAVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqe 201
Cdd:cd17653 94 GATLLLT------------------------------------------------------------------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 202 aAPQADDVAVLQYTGGTTGVAKGAMLTHRNlVANMLQckaLMGANLNEGCEILIAplplyHIYAFTFH-CMAMMLT--GN 278
Cdd:cd17653 101 -TDSPDDLAYIIFTSGSTGIPKGVMVPHRG-VLNYVS---QPPARLDVGPGSRVA-----QVLSIAFDaCIGEIFStlCN 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILItnPRDLPSMLKDLGQwkftgfvGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEvtGCAICEGY 358
Cdd:cd17653 171 GGTLV--LADPSDPFAHVAR-------TVDALMSTPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 359 GMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE----ILDADGW 434
Cdd:cd17653 240 GPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 435 L--KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVypnELEDVLATL----PGVLQCAAIgipdeKSGESIKVFVVvkPgA 508
Cdd:cd17653 320 RmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRI---NLEEIEEVVlqsqPEVTQAAAI-----VVNGRLVAFVT--P-E 388
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15598495 509 TLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd17653 389 TVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
49-556 |
4.46e-39 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 150.70 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVC 128
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 LANMAHLVEGVLPKT-GVKQVIVTEVGDIlpplkrfivnfvvkhikkMVPAYSLPQATKLTDALARGAGKSFQEAAPQAD 207
Cdd:PRK05620 118 DPRLAEQLGEILKECpCVRAVVFIGPSDA------------------DSAAAHMPEGIKVYSYEALLDGRSTVYDWPELD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 --DVAVLQYTGGTTGVAKGAMLTHRNLvanMLQCKALMGAN---LNEGCEILIApLPLYHIYAFTFHCMAMMlTGNHNIL 282
Cdd:PRK05620 180 etTAAAICYSTGTTGAPKGVVYSHRSL---YLQSLSLRTTDslaVTHGESFLCC-VPIYHVLSWGVPLAAFM-SGTPLVF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 283 ITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTE 362
Cdd:PRK05620 255 PGPDLSAPTLAKIIATAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 363 TAPVvsvnpfqniqvGTIGIP------------------VPSTLCKVIGDDGQEVPLGER--GELCVKGPQVMKGYWQ-- 420
Cdd:PRK05620 335 TSPV-----------GTVARPpsgvsgearwayrvsqgrFPASLEYRIVNDGQVMESTDRneGEIQVRGNWVTASYYHsp 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 421 -----------RQEATDEILD---ADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAA 486
Cdd:PRK05620 404 teegggaastfRGEDVEDANDrftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 487 IGIPDEKSGESIKVFVVVKPGATLTKE---QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKI----LRRELRDEEL 556
Cdd:PRK05620 484 IGYPDDKWGERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFdkkdLRQHLADGDF 560
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-546 |
5.09e-39 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 153.20 E-value: 5.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 46 LGKTLTYGELykLSGDFA--AYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNplYTArelehqfndsGA 123
Cdd:PRK06814 655 VNGPLTYRKL--LTGAFVlgRKLKKNT--PPGENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FSA----------GI 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 124 KAVV--CLAnmahlvegvlpkTGVKqVIVTEvgdilpplKRFI-----------VNFVVK--HIKKMVPAYSLpqATKLt 188
Cdd:PRK06814 719 ANILsaCKA------------AQVK-TVLTS--------RAFIekarlgplieaLEFGIRiiYLEDVRAQIGL--ADKI- 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgceILIAPLPLYHIYAFTF 268
Cdd:PRK06814 775 KGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPED---KVFNALPVFHSFGLTG 851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 269 HCMAMMLTGNHNILITNP---RDLPSMLKDLGQwkfTGFVGLNTLFVALCNneTFRKLDFSALKLTLSGGMALQLATAER 345
Cdd:PRK06814 852 GLVLPLLSGVKVFLYPSPlhyRIIPELIYDTNA---TILFGTDTFLNGYAR--YAHPYDFRSLRYVFAGAEKVKEETRQT 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 WKEVTGCAICEGYGMTETAPVVSVN-PFQNiQVGTIGIPVP---STLCKVIG-DDGqevplgerGELCVKGPQVMKGYWq 420
Cdd:PRK06814 927 WMEKFGIRILEGYGVTETAPVIALNtPMHN-KAGTVGRLLPgieYRLEPVPGiDEG--------GRLFVRGPNVMLGYL- 996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 421 RQEATDEILD-ADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATL-PGVLQcAAIGIPDEKSGESI 498
Cdd:PRK06814 997 RAENPGVLEPpADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALH-AAVSIPDARKGERI 1075
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598495 499 kvfVVVKPGATLTKEQVMQHMHDN-LTGYKRPKAVEFRDSLPTTNVGKI 546
Cdd:PRK06814 1076 ---ILLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
41-551 |
5.76e-39 |
|
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: 148.96 E-value: 5.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 41 PAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFND 120
Cdd:cd17646 15 PAVVDEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 121 SGAKAVvclanmahLVEGVLPKTGVKQVIVTEVGDILPPLkrfivnfvvkhikkmvPAYSLPQAtkltdalargagksfq 200
Cdd:cd17646 94 AGPAVV--------LTTADLAARLPAGGDVALLGDEALAA----------------PPATPPLV---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 eaAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQ--------------CKALMGANLNeGCEILiapLPLyhiyaF 266
Cdd:cd17646 134 --PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWmqdeyplgpgdrvlQKTPLSFDVS-VWELF---WPL-----V 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 267 TFHCMAMMLTGNHniliTNPRDLPSMLKDLGQwKFTGFV-GLNTLFVALCNNETFRkldfsALKLTLSGGMALQLATAER 345
Cdd:cd17646 203 AGARLVVARPGGH----RDPAYLAALIREHGV-TTCHFVpSMLRVFLAEPAAGSCA-----SLRRVFCSGEALPPELAAR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 346 WKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGT---IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQ 422
Cdd:cd17646 273 FLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPsvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 423 EATDEILDADGW------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGE 496
Cdd:cd17646 353 ALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAA 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 497 SIKVFVVVKPGAT-LTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17646 433 RLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
47-555 |
1.18e-38 |
|
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: 152.32 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPL---YTARELEHQFNDSGA 123
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMVVALLAVLKAGAAYV---PLdpaYPAERLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 124 KAVVCLANMAHLvegvLPKTGVkQVIVtevgdilpplkrfivnfvvkhikkmvpayslpqatkLTDALARGAGKSFQEAA 203
Cdd:COG1020 575 RLVLTQSALAAR----LPELGV-PVLA------------------------------------LDALALAAEPATNPPVP 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILiaplpLYHIYAF---TFHCMAMMLTGNHN 280
Cdd:COG1020 614 VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG--LGPGDRVL-----QFASLSFdasVWEIFGALLSGATL 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITN--PRDLPSMLKDLGQ-----WKFTgfvglNTLFVALCNNETfrkLDFSALKLTLSGGMALQLATAERWKEVT-GC 352
Cdd:COG1020 687 VLAPPeaRRDPAALAELLARhrvtvLNLT-----PSLLRALLDAAP---EALPSLRLVLVGGEALPPELVRRWRARLpGA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTETAPVVSVNPFQNIQVG----TIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE- 427
Cdd:COG1020 759 RLVNLYGPTETTVDSTYYEVTPPDADggsvPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAEr 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 428 -ILDADG-----WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVF 501
Cdd:COG1020 839 fVADPFGfpgarLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAY 918
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 15598495 502 VVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEE 555
Cdd:COG1020 919 VVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPA 972
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
25-556 |
5.08e-38 |
|
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: 148.02 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 25 NILSVLKESCQRFA-TKPAFTNLG-----KTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRA 98
Cdd:cd05968 61 NIVEQLLDKWLADTrTRPALRWEGedgtsRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 99 GLIVVNTNPLYTARELEHQFNDSGAKAVVclanmahLVEGVLPKTgvKQVIVTEVGDILP---PLKRFIVnfVVKHIKKM 175
Cdd:cd05968 140 GGIVVPIFSGFGKEAAATRLQDAEAKALI-------TADGFTRRG--REVNLKEEADKACaqcPTVEKVV--VVRHLGND 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 176 VPAYslPQATKLTDALARGAGKSFQEAAPqaDDVAVLQYTGGTTGVAKGAMLTH-------------------RNLVANM 236
Cdd:cd05968 209 FTPA--KGRDLSYDEEKETAGDGAERTES--EDPLMIIYTSGTTGKPKGTVHVHagfplkaaqdmyfqfdlkpGDLLTWF 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 237 LQCKALMGANLNEGCEILIAPLPLYHIYAftfhcmammltgnhnilitnprDLPsmlkDLGQ-WKFT-----GFVGLN-T 309
Cdd:cd05968 285 TDLGWMMGPWLIFGGLILGATMVLYDGAP----------------------DHP----KADRlWRMVedheiTHLGLSpT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 310 LFVALC--NNETFRKLDFSALKLTLSGGMALQLataERWK---EVTG---CAICEGYGMTETAP-VVSVNPFQNIQVGTI 380
Cdd:cd05968 339 LIRALKprGDAPVNAHDLSSLRVLGSTGEPWNP---EPWNwlfETVGkgrNPIINYSGGTEISGgILGNVLIKPIKPSSF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 381 GIPVPSTLCKVIGDDGQEVPlGERGELCVKGPQV--MKGYWqRQEatDEILDA-----DGWLKTGDIAIIQEDGYMRIVD 453
Cdd:cd05968 416 NGPVPGMKADVLDESGKPAR-PEVGELVLLAPWPgmTRGFW-RDE--DRYLETywsrfDNVWVHGDFAYYDEEGYFYILG 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 454 RKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLT---KEQVMQHMHDNLTGYKRPK 530
Cdd:cd05968 492 RSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPE 571
|
570 580 590
....*....|....*....|....*....|
gi 15598495 531 AVEFRDSLPTTNVGKILRRELR----DEEL 556
Cdd:cd05968 572 RILFVKDLPKTRNAKVMRRVIRaaylGKEL 601
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
51-554 |
8.04e-38 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 146.91 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 51 TYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIV--VNT--NPLYTARELEHqfndSGAKAV 126
Cdd:PLN02479 47 TWAQTYQRCRRLASALAKRS-IGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVncVNIrlNAPTIAFLLEH----SKSEVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANMAHLVEGVLpktgvKQVIVTEVGDILPPLKRFIVNFVVKHikkmvpayslpqaTKLTDALARGA--GKSFQEA-- 202
Cdd:PLN02479 122 MVDQEFFTLAEEAL-----KILAEKKKSSFKPPLLIVIGDPTCDP-------------KSLQYALGKGAieYEKFLETgd 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 -----APQAD--DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCeILIAPLPLYHI--YAFTFHCMAM 273
Cdd:PLN02479 184 pefawKPPADewQSIALGYTSGTTASPKGVVLHHRGAYLMALSNALIWG--MNEGA-VYLWTLPMFHCngWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 274 MLTgnhNILI--TNPRDLPSMLKDLGQWKFTGF-VGLNTLFVAlCNNETFrkLDFSALKLTLSGGMA----LQLATAERw 346
Cdd:PLN02479 261 CGT---NICLrqVTAKAIYSAIANYGVTHFCAApVVLNTIVNA-PKSETI--LPLPRVVHVMTAGAApppsVLFAMSEK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 kevtGCAICEGYGMTET---------------APVVS---VNPFQNIQ-VGTIGIPV--PSTLcKVIGDDGQEVplgerG 405
Cdd:PLN02479 334 ----GFRVTHTYGLSETygpstvcawkpewdsLPPEEqarLNARQGVRyIGLEGLDVvdTKTM-KPVPADGKTM-----G 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 406 ELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCA 485
Cdd:PLN02479 404 EIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEAS 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598495 486 AIGIPDEKSGESIKVFVVVKPGATLTKEQ-----VMQHMHDNLTGYKRPKAVEFrDSLPTTNVGKILRRELRDE 554
Cdd:PLN02479 483 VVARPDERWGESPCAFVTLKPGVDKSDEAalaedIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
44-553 |
2.60e-36 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 143.22 E-value: 2.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 44 TNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLI--VVNTNplYTARELEHQFNDS 121
Cdd:cd05967 77 TGTERTYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsVVFGG--FAAKELASRIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 122 GAKAVVClANMahlveGVLPKtgvkQVIvtevgDILPPLKRFIVNFVVKHIKKMVpaYSLPQATklTDALARGAGKSFQE 201
Cdd:cd05967 154 KPKLIVT-ASC-----GIEPG----KVV-----PYKPLLDKALELSGHKPHHVLV--LNRPQVP--ADLTKPGRDLDWSE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 202 AAPQA---DDVAVLQ-------YTGGTTGVAKGAMlthRN-------LVANMLQCKalmgaNLNEGcEILIAPLPLYHIY 264
Cdd:cd05967 215 LLAKAepvDCVPVAAtdplyilYTSGTTGKPKGVV---RDngghavaLNWSMRNIY-----GIKPG-DVWWAASDVGWVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 265 AFTFHCMAMMLTGNHNILITNprdLPSMLKDLGQ-WKFTGFVGLNTLFVALC----------NNETFRKLDFSALKLTLS 333
Cdd:cd05967 286 GHSYIVYGPLLHGATTVLYEG---KPVGTPDPGAfWRVIEKYQVNALFTAPTairairkedpDGKYIKKYDLSSLRTLFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 334 GGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNP--FQNIQV--GTIGIPVPSTLCKVIGDDGQEVPLGERGELCV 409
Cdd:cd05967 363 AGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPvgLEPLPIkaGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 410 KGP---QVMKGYWQRQEATDE--ILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQC 484
Cdd:cd05967 443 KLPlppGCLLTLWKNDERFKKlyLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC 522
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598495 485 AAIGIPDEKSGESIKVFVVVKPGATLTKEQV----MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05967 523 AVVGVRDELKGQVPLGLVVLKEGVKITAEELekelVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
176-552 |
2.91e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 138.64 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 176 VPAYSLPQATKLTDALARGAgksfqeaaPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGAnlnEGcEILI 255
Cdd:PRK07824 12 VPAQDERRAALLRDALRVGE--------PIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGG---PG-QWLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 256 ApLPLYHIYAFTFhCMAMMLTGNHNILIT-----NPRDLPSMLKDL-GQWKFTGFVGLNtLFVALCNNETFRKL-DFSAL 328
Cdd:PRK07824 80 A-LPAHHIAGLQV-LVRSVIAGSEPVELDvsagfDPTALPRAVAELgGGRRYTSLVPMQ-LAKALDDPAATAALaELDAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 329 kltLSGGMALQLATAERWKEVtGCAICEGYGMTETAPvvsvnpfqniqvGTI--GIPVPSTLCKVigDDGQeVPLGerge 406
Cdd:PRK07824 157 ---LVGGGPAPAPVLDAAAAA-GINVVRTYGMSETSG------------GCVydGVPLDGVRVRV--EDGR-IALG---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 407 lcvkGPQVMKGYwqRQEATDEILDADGWLKTGDIAIIqEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAA 486
Cdd:PRK07824 214 ----GPTLAKGY--RNPVDPDPFAEPGWFRTDDLGAL-DDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAV 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 487 IGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK07824 287 FGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
40-558 |
1.15e-34 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 139.01 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTnLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPlytarELehqfn 119
Cdd:PRK06060 22 RPAFY-AADVVTHGQIHDGAARLGEVLRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANP-----EL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 dsgakavvclanmaHLVEGVLPKTGVKQVIVTEVGdilPPLKRFIVNFVVKhikkmvPAYSLPQATKltdalargAGKSF 199
Cdd:PRK06060 90 --------------HRDDHALAARNTEPALVVTSD---ALRDRFQPSRVAE------AAELMSEAAR--------VAPGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAApQADDVAVLQYTGGTTGVAKGAMLTHRNLVA--NMLQCKALMGANLNEGceilIAPLPLYHIYAFTFHCMAMMLTG 277
Cdd:PRK06060 139 YEPM-GGDALAYATYTSGTTGPPKAAIHRHADPLTfvDAMCRKALRLTPEDTG----LCSARMYFAYGLGNSVWFPLATG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 278 NHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLF---VALCNNETFRkldfsALKLTLSGGMALQLATAERWKEV-TGCA 353
Cdd:PRK06060 214 GSAVINSAPVTPEAAAILSARFGPSVLYGVPNFFarvIDSCSPDSFR-----SLRCVVSAGEALELGLAERLMEFfGGIP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEAtdeILDADG 433
Cdd:PRK06060 289 ILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDS---PVANEG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 434 WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLtKE 513
Cdd:PRK06060 366 WLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATI-DG 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 15598495 514 QVMQHMH----DNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKK 558
Cdd:PRK06060 445 SVMRDLHrgllNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQSPTK 493
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
40-551 |
1.21e-34 |
|
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: 136.63 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd12114 3 ATAVICGDGTLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVvclanmahLVEGVLPKTGVkqvivtEVGDILPPlkrfivnfvvkhikkmvpayslpqatkltDALARGAGKSF 199
Cdd:cd12114 82 DAGARLV--------LTDGPDAQLDV------AVFDVLIL-----------------------------DLDALAAPAPP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAAPQADDVAVLQYTGGTTGVAKGAMLTHR---NLVANMLQCKALmGANLNegceIL-IAPL----PLYHIYAftfhcm 271
Cdd:cd12114 119 PPVDVAPDDLAYVIFTSGSTGTPKGVMISHRaalNTILDINRRFAV-GPDDR----VLaLSSLsfdlSVYDIFG------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 amMLTGNHNILITNP---RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGG--MALQLATaeRW 346
Cdd:cd12114 188 --ALSAGATLVLPDEarrRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGdwIPLDLPA--RL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 KEVT-GCAICEGYGMTETA------PVVSVNPfqniQVGTI--GIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKG 417
Cdd:cd12114 264 RALApDARLISLGGATEASiwsiyhPIDEVPP----DWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 418 YWQRQEATDE--ILDADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIpDEK 493
Cdd:cd12114 340 YLGDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDP 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 494 SGESIKVFVVVKPGAT-LTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd12114 419 GGKRLAAFVVPDNDGTpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
175-555 |
2.39e-34 |
|
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: 135.00 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 175 MVPAYSLPQATKLTDALARGAG-KSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEI 253
Cdd:cd05974 52 VIPATTLLTPDDLRDRVDRGGAvYAAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIG--LKPGDVH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 254 LIAPLPLYHIYAFTfhCMAMMLTGNHNILITN-PR-DLPSMLKDLGQWKFTGFVGLNTLFVALCNnETFRKLDfSALKLT 331
Cdd:cd05974 130 WNISSPGWAKHAWS--CFFAPWNAGATVFLFNyARfDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFD-VKLREV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 332 LSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVplgERGELCV-- 409
Cdd:cd05974 206 VGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPA---TEGEVALdl 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 410 ---KGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAA 486
Cdd:cd05974 283 gdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598495 487 IGIPDEKSGESIKVFVVVKPGATLTKE---QVMQHMHDNLTGYKRPKAVEFRDsLPTTNVGKILRRELRDEE 555
Cdd:cd05974 362 VPSPDPVRLSVPKAFIVLRAGYEPSPEtalEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRRE 432
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
24-551 |
7.67e-34 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 135.14 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 24 PNILSVLKESCQRFATKPAFTNLGKT--LTYGELYKLSGDFAAYLQQHTdLKPGDRIAVQLPNVLQYPIVVFGAMRAGLI 101
Cdd:PRK05857 14 STVLDRVFEQARQQPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQS-VSRGSRVLVISDNGPETYLSVLACAKLGAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 102 VVntnplytarelehqfndsgakavvclanmahLVEGVLPKTGVKQVI-VTEVGDILPPLKRFIVNFVVKHIKKMVPAYS 180
Cdd:PRK05857 93 AV-------------------------------MADGNLPIAAIERFCqITDPAAALVAPGSKMASSAVPEALHSIPVIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 181 LpQATKLTDALARGAGKSFQEAAPQ--ADDVAVLQYTGGTTGVAKGAMLTHRNLVA--NMLQCKALMGANLNEGcEILIA 256
Cdd:PRK05857 142 V-DIAAVTRESEHSLDAASLAGNADqgSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNWVTWVVG-ETTYS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 257 PLPLYHIYAFTFHCMAMMLTGnhnILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGm 336
Cdd:PRK05857 220 PLPATHIGGLWWILTCLMHGG---LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 337 ALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQN-----IQVGTIGIPVPSTLCKVIGDDG------QEVPLGERG 405
Cdd:PRK05857 296 SRAIAADVRFIEATGVRTAQVYGLSETGCTALCLPTDDgsivkIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 406 ELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCA 485
Cdd:PRK05857 376 TLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 486 AIGIPDEKSGESIKVFVVV-----KPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK05857 455 CYEIPDEEFGALVGLAVVAsaeldESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
208-553 |
1.38e-33 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 134.76 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNlvANMLQCKALMGANLNEgCEILIAPLPLYHIYAFTFhCMAMMLTGNHNILITNPr 287
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRG--AYLSTLSAIIGWEMGT-CPVYLWTLPMFHCNGWTF-TWGTAARGGTSVCMRHV- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVtGCAICEGYGMTE-TAPV 366
Cdd:PLN03102 262 TAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEaTGPV 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 367 -----------------VSVNPFQNIQVGTIG-IPVPST-LCKVIGDDGQEVplgerGELCVKGPQVMKGYWQRQEATDE 427
Cdd:PLN03102 341 lfcewqdewnrlpenqqMELKARQGVSILGLAdVDVKNKeTQESVPRDGKTM-----GEIVIKGSSIMKGYLKNPKATSE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 428 ILDaDGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPG 507
Cdd:PLN03102 416 AFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKG 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 508 ATLTKEQV----------MQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PLN03102 495 ETTKEDRVdklvtrerdlIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
207-550 |
2.72e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 133.58 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcKALM-GANLNEGCEILIAPLPLyhiyaftFHCMAM-------MLTGN 278
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANA---EAMFvAAEFDVETDVMVSWLPL-------FHDMGMvgfltvpMYFGA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITnP----RDLPSMLKDLGQWKFTGFVGLNTLF--VA--LCNNETFRKLDFSALKLTLSGGMALQLATAERWKEVT 350
Cdd:PRK07768 222 ELVKVT-PmdflRDPLLWAELISKYRGTMTAAPNFAYalLArrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 351 G------CAICEGYGMTETAPVVSVNPFQNIQV--------------------------GTIGIPVPSTLCKVIGDDGQE 398
Cdd:PRK07768 301 ArfglrpEAILPAYGMAEATLAVSFSPCGAGLVvdevdadllaalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 399 VPLGERGELCVKGPQVMKGYwQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATL 478
Cdd:PRK07768 381 LPPRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARV 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 479 PGVLQ-CA-AIGIPDEKSGESIKVFVVVK---PGATLT--KEQVMQHMHDNLTgyKRPKAVEF--RDSLPTTNVGKiLRR 549
Cdd:PRK07768 460 EGVRPgNAvAVRLDAGHSREGFAVAVESNafeDPAEVRriRHQVAHEVVAEVG--VRPRNVVVlgPGSIPKTPSGK-LRR 536
|
.
gi 15598495 550 E 550
Cdd:PRK07768 537 A 537
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
48-552 |
6.89e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 131.83 E-value: 6.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQhTDLKPgDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:PRK07638 25 RVLTYKDWFESVCKVANWLNE-KESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 CLANMAHlvegvlPKTGVKqvivTEVGDIlpplkrfivnfvvKHIKKMVPAYslpqatkltdaLARGAGKSFQEAAPqad 207
Cdd:PRK07638 103 TERYKLN------DLPDEE----GRVIEI-------------DEWKRMIEKY-----------LPTYAPIENVQNAP--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 dvAVLQYTGGTTGVAKGAMLTHRNLVANmLQCKAlMGANLNEGCEILIaPLPLYHIYaFTFHCMAMMLTGNHNILIT--N 285
Cdd:PRK07638 146 --FYMGFTSGSTGKPKAFLRAQQSWLHS-FDCNV-HDFHMKREDSVLI-AGTLVHSL-FLYGAISTLYVGQTVHLMRkfI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDlpsMLKDLGQWKFTGFVGLNTLFVALCNNETFRKldfSALKLTLSG---GMALQLATAERWKEVTgcaICEGYGMTE 362
Cdd:PRK07638 220 PNQ---VLDKLETENISVMYTVPTMLESLYKENRVIE---NKMKIISSGakwEAEAKEKIKNIFPYAK---LYEFYGASE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 363 TAPVVSVNPFQNIQVGT-IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEiLDADGWLKTGDIA 441
Cdd:PRK07638 291 LSFVTALVDEESERRPNsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNADGWMTVRDVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 442 IIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGEsiKVFVVVKPGAtlTKEQVMQHMHD 521
Cdd:PRK07638 370 YEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE--KPVAIIKGSA--TKQQLKSFCLQ 445
|
490 500 510
....*....|....*....|....*....|.
gi 15598495 522 NLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:PRK07638 446 RLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
47-553 |
1.22e-32 |
|
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: 132.30 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLI--VVNTNplYTARELEHQFNDSGAK 124
Cdd:cd05966 82 SRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVhsVVFAG--FSAESLADRINDAQCK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVClANMAHLVEGVLPktgVKQvIVTEVGDILPPLKRFIVnfvVKHIKKMVPAYslPQATKLTDALARGAGksfQEAAP 204
Cdd:cd05966 159 LVIT-ADGGYRGGKVIP---LKE-IVDEALEKCPSVEKVLV---VKRTGGEVPMT--EGRDLWWHDLMAKQS---PECEP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 Q---ADDVAVLQYTGGTTGVAKGAMLTHrnlVANMLQCKALMGanlnegceiliaplplyhiYAFTFH------CMAMM- 274
Cdd:cd05966 226 EwmdSEDPLFILYTSGSTGKPKGVVHTT---GGYLLYAATTFK-------------------YVFDYHpddiywCTADIg 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 275 -LTGnHNILITNP-------------RDLPsmlkDLGQW-------KFTGFVGLNTLFVALC--NNETFRKLDFSALKLT 331
Cdd:cd05966 284 wITG-HSYIVYGPlangattvmfegtPTYP----DPGRYwdivekhKVTIFYTAPTAIRALMkfGDEWVKKHDLSSLRVL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 332 LSGGMALQlatAERWK---EVTG---CAICEGYGMTET-----APVVSVNPfqnIQVGTIGIPVPSTLCKVIGDDGQEVP 400
Cdd:cd05966 359 GSVGEPIN---PEAWMwyyEVIGkerCPIVDTWWQTETggimiTPLPGATP---LKPGSATRPFFGIEPAILDEEGNEVE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 401 LGERGELCVKGP-------------QVMKGYWQRQEatdeildadGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVY 467
Cdd:cd05966 433 GEVEGYLVIKRPwpgmartiygdheRYEDTYFSKFP---------GYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 468 PNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGAT----LTKEqVMQHMHDNLTGYKRPKAVEFRDSLPTTNV 543
Cdd:cd05966 504 TAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEpsdeLRKE-LRKHVRKEIGPIATPDKIQFVPGLPKTRS 582
|
570
....*....|
gi 15598495 544 GKILRRELRD 553
Cdd:cd05966 583 GKIMRRILRK 592
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
25-517 |
5.27e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 130.02 E-value: 5.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 25 NILSVLKESCQRFATKPA----------FTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFG 94
Cdd:PRK09274 7 NIARHLPRAAQERPDQLAvavpggrgadGKLAYDELSFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 95 AMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVCLAnMAHLVEGVLP--KTGVKQVIVteVGDILpplkrfivnfvvkhi 172
Cdd:PRK09274 86 LFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIP-KAHLARRLFGwgKPSVRRLVT--VGGRL--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 173 kkmvpaysLPQATKLTDALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKAL-----MGANl 247
Cdd:PRK09274 148 --------LWGGTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA---QIEALredygIEPG- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 248 negcEILIAPLPLyhiyaFTFHCMAMmltGNHNIL--------IT-NPRDLpsmLKDLGQWKFTGFVGLNTLFVALCNNE 318
Cdd:PRK09274 216 ----EIDLPTFPL-----FALFGPAL---GMTSVIpdmdptrpATvDPAKL---FAAIERYGVTNLFGSPALLERLGRYG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 319 TFRKLDFSALKLTLSGGMALQLATAERWKEV--TGCAICEGYGMTETAPVVSV----------------------NPFQN 374
Cdd:PRK09274 281 EANGIKLPSLRRVISAGAPVPIAVIERFRAMlpPDAEILTPYGATEALPISSIesreilfatraatdngagicvgRPVDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 375 IQVGTIGI---PVPSTlckvigDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE--ILDADG--WLKTGDIAIIQEDG 447
Cdd:PRK09274 361 VEVRIIAIsdaPIPEW------DDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLakIPDGQGdvWHRMGDLGYLDAQG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 448 YMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPdeKSGESIKVFVV-VKPGATLTKEQVMQ 517
Cdd:PRK09274 435 RLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVG--VPGAQRPVLCVeLEPGVACSKSALYQ 503
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
45-552 |
5.38e-32 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 130.13 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 45 NLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTnPLYTA---RE-----LEH 116
Cdd:PRK09192 45 QLEEALPYQTLRARAEAGARRLLAL-GLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL-PLPMGfggREsyiaqLRG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 117 QFNDSGAKAVVCLANMAHLVEGVLPKTGVKQVIVTEVGDILPplkrfivnfvvkhikkmVPAYSLPQatkltdalargag 196
Cdd:PRK09192 123 MLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALP-----------------EADVALPR------------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 197 ksfqeaaPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmLQCKALMGANLNEG--CeilIAPLPLYH---IYAFTFHCM 271
Cdd:PRK09192 173 -------PTPDDIAYLQYSSGSTRFPRGVIITHRALMAN-LRAISHDGLKVRPGdrC---VSWLPFYHdmgLVGFLLTPV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 AMMLTGNHniLITNP---RDLpsmlkdlgQW-----KFTGFVGLNTLF-VALC----NNETFRKLDFSALKLTLSGG--- 335
Cdd:PRK09192 242 ATQLSVDY--LPTRDfarRPL--------QWldlisRNRGTISYSPPFgYELCarrvNSKDLAELDLSCWRVAGIGAdmi 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 -MALQLATAERWKEV--TGCAICEGYGMTETAPVVSVNPF-QNIQVGTI---------------------------GIPV 384
Cdd:PRK09192 312 rPDVLHQFAEAFAPAgfDDKAFMPSYGLAEATLAVSFSPLgSGIVVEEVdrdrleyqgkavapgaetrrvrtfvncGKAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 385 PSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEiLDADGWLKTGDIAIIqEDGYMRIVDRKKDMILVSGF 464
Cdd:PRK09192 392 PGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDV-LAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 465 NVYPNELEDVLATLPGVLQ--CAAIGIPDEkSGESIKVFVVVKPGATLTKEQvmqhMHDNLTGYKR-----PKAVEF--R 535
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRSgdAAAFSIAQE-NGEKIVLLVQCRISDEERRGQ----LIHALAALVRsefgvEAAVELvpP 544
|
570
....*....|....*..
gi 15598495 536 DSLPTTNVGKILRRELR 552
Cdd:PRK09192 545 HSLPRTSSGKLSRAKAK 561
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
48-488 |
2.20e-31 |
|
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: 128.31 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVlqyPIVVFGAMRAGLIVVNTNPLYT---ARELEHQFNDSGAK 124
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLA-LGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVClanmahlvegvlpkTGVKQV-IVTEVGDILPPLkRFIVNFVVKHIKKMVPAY--SLPQATKLTDALARGAGKSFQE 201
Cdd:cd17641 86 VVIA--------------EDEEQVdKLLEIADRIPSV-RYVIYCDPRGMRKYDDPRliSFEDVVALGRALDRRDPGLYER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 202 --AAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKALMGAN-LNEGCEILiAPLPLYHIYAFTFHCMAMMLTGN 278
Cdd:cd17641 151 evAAGKGEDVAVLCTTSGTTGKPKLAMLSHGNFLG---HCAAYLAADpLGPGDEYV-SVLPLPWIGEQMYSVGQALVCGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 hniLITNPRDLPSMLKDLGQ------------WK---------------FTGFV---GLNTLFVALcnNETFR------- 321
Cdd:cd17641 227 ---IVNFPEEPETMMEDLREigptfvllpprvWEgiaadvrarmmdatpFKRFMfelGMKLGLRAL--DRGKRgrpvslw 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 322 ------------------KLDFSALKLTLSGGMALQLATAeRWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIP 383
Cdd:cd17641 302 lrlaswladallfrplrdRLGFSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 384 VPSTlckvigddgqEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKD-MILVS 462
Cdd:cd17641 381 FPGT----------EVRIDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDvGTTSD 450
|
490 500
....*....|....*....|....*.
gi 15598495 463 GFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAEAVVLG 476
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
47-551 |
5.29e-31 |
|
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: 125.44 E-value: 5.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAkav 126
Cdd:cd17652 10 DETLTYAELNARANRLARLLAAR-GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARP--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 vclanmahlvegvlpktgvkQVIVTEVGDilpplkrfivnfvvkhikkmvPAYSLpqatkltdalargagksfqeaapqa 206
Cdd:cd17652 86 --------------------ALLLTTPDN---------------------LAYVI------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 ddvavlqYTGGTTGVAKGAMLTHRNLvANMLQCKAlMGANLNEGCEILiaplplyHIYAFTFH------CMAMmLTGNHN 280
Cdd:cd17652 100 -------YTSGSTGRPKGVVVTHRGL-ANLAAAQI-AAFDVGPGSRVL-------QFASPSFDasvwelLMAL-LAGATL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPRDLPSM-LKDLGQWKFTGFVGLNTlfVALCNNETFRKLDFSALkltLSGGMALQLATAERWkeVTGCAICEGYG 359
Cdd:cd17652 163 VLAPAEELLPGEpLADLLREHRITHVTLPP--AALAALPPDDLPDLRTL---VVAGEACPAELVDRW--APGRRMINAYG 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 360 MTE-TAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGW---- 434
Cdd:cd17652 236 PTEtTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapg 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 435 ---LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQcAAIGIPDEKSGESIKV-FVVVKPGATL 510
Cdd:cd17652 316 srmYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDKRLVaYVVPAPGAAP 394
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15598495 511 TKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17652 395 TAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
32-551 |
5.33e-31 |
|
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: 125.51 E-value: 5.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 32 ESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTA 111
Cdd:cd12115 7 AQAARTPDAIALVCGDESLTYAELNRRANRLAARLR-AAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 112 RELEHQFNDSGAKAVvclanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkLTDAl 191
Cdd:cd12115 86 ERLRFILEDAQARLV------------------------------------------------------------LTDP- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 192 argagksfqeaapqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGAnlnegcEILIAPLplyhiyAFT---- 267
Cdd:cd12115 105 ---------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSA------EELAGVL------ASTsicf 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 268 ----FHCMAMMLTGNHNILITNPRDLPsmlkDLGQWKFTGFvgLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATA 343
Cdd:cd12115 158 dlsvFELFGPLATGGKVVLADNVLALP----DLPAAAEVTL--INTVPSAAAELLRHDALPASVRVVNLAGEPLPRDLVQ 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 344 ERWKEVTGCAICEGYGMTE--TAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQR 421
Cdd:cd12115 232 RLYARLQVERVVNLYGPSEdtTYSTVAPVPPGASGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGR 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 422 QEATDEILDADGWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSG 495
Cdd:cd12115 312 PGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGE 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 496 ESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd12115 392 RRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-554 |
1.23e-30 |
|
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: 125.29 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLqckALMGANLNEGCEILIAPLPLYHIYAF-TFHCMAMMLTGNHNILit 284
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMF---AILNSTEWKTKDRILSWMPLTHDMGLiAFHLAPLIAGMNQYLM-- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 nPRDL----PSM-LKDLGQWKFTGFVGLN---TLFVALCNNETFRKLDFSALKLTLSG------GMALQLATAERWKEVT 350
Cdd:cd05908 180 -PTRLfirrPILwLKKASEHKATIVSSPNfgyKYFLKTLKPEKANDWDLSSIRMILNGaepidyELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 351 GCAICEGYGMTE-------------TAPVVSVNPFQNIQVG---------------TIGIPVPSTLCKVIGDDGQEVPLG 402
Cdd:cd05908 259 RNAILPVYGLAEasvgaslpkaqspFKTITLGRRHVTHGEPepevdkkdsecltfvEVGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 403 ERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVL 482
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIR-NGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 483 --QCAAIGIPDEKS-GESIKVFVVVKPGAT----LTKeQVMQHMHDNlTGYKRPKAVEFRdSLPTTNVGKILRRELRDE 554
Cdd:cd05908 418 lgRVVACGVNNSNTrNEEIFCFIEHRKSEDdfypLGK-KIKKHLNKR-GGWQINEVLPIR-RIPKTTSGKVKRYELAQR 493
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
48-456 |
1.73e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 126.24 E-value: 1.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAE-LGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 CLA-NMAHLVEGVlPKTGVKQVIVTEVGDiLPPlkrfivnFVVKHIKKMVPayslpqatkLTDALARGAGKSFQEAAPQA 206
Cdd:PTZ00216 199 CNGkNVPNLLRLM-KSGGMPNTTIIYLDS-LPA-------SVDTEGCRLVA---------WTDVVAKGHSAGSHHPLNIP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 ---DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCK----ALMGaNLNEGcEILIAPLPLYHIYAFTfhCMAMMLTGNH 279
Cdd:PTZ00216 261 ennDDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEdrlnDLIG-PPEED-ETYCSYLPLAHIMEFG--VTNIFLARGA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILITNPRDLPSMLK----DLGQWKFTGFVGLNTLF------------------------------VALCN-------NE 318
Cdd:PTZ00216 337 LIGFGSPRTLTDTFArphgDLTEFRPVFLIGVPRIFdtikkaveaklppvgslkrrvfdhayqsrlRALKEgkdtpywNE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 319 T----FRKLDFSALKLTLSGGMALQLATAERWKEVTGCAIcEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGD 394
Cdd:PTZ00216 417 KvfsaPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGMVI-QGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLLDT 495
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 395 DG-----QEVPlgeRGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKK 456
Cdd:PTZ00216 496 EEykhtdTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
33-518 |
1.76e-30 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 126.36 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 33 SCQRF-ATKPAFTNLG-KTLTYGELYKLSGDFAAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNplYT 110
Cdd:PRK08043 213 AQYRYgAGKPCIEDVNfTPDSYRKLLKKTLFVGRILEKYS--VEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YT 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 111 A--RELEHQFNDSGAKAVVC------LANMAHLVEGVlpkTGVKQVIVTEV-GDILPPLKRFIVNFVVKHIKKMVPAysl 181
Cdd:PRK08043 289 AgvKGLTSAITAAEIKTIFTsrqfldKGKLWHLPEQL---TQVRWVYLEDLkDDVTTADKLWIFAHLLMPRLAQVKQ--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 182 pqatkltdalargagksfqeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGceiLIAPLPLY 261
Cdd:PRK08043 363 -----------------------QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDR---FMSALPLF 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 262 HIYAFTFHCMAMMLTGNHNILITNP---RDLPSMLKDLgqwKFTGFVGLNTLfvaLCNNETF-RKLDFSALKLTLSGGMA 337
Cdd:PRK08043 417 HSFGLTVGLFTPLLTGAEVFLYPSPlhyRIVPELVYDR---NCTVLFGTSTF---LGNYARFaNPYDFARLRYVVAGAEK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 338 LQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEvplgERGELCVKGPQVMKG 417
Cdd:PRK08043 491 LQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLSVPGIE----QGGRLQLKGPNIMNG 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 418 YWqRQEATDEI-----------LDAdGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAA 486
Cdd:PRK08043 567 YL-RVEKPGVLevptaenargeMER-GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHAT 644
|
490 500 510
....*....|....*....|....*....|..
gi 15598495 487 IGIPDEKSGESIKVFVVvkpGATLTKEQVMQH 518
Cdd:PRK08043 645 AIKSDASKGEALVLFTT---DSELTREKLQQY 673
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
40-551 |
2.40e-30 |
|
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: 124.36 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:cd17655 13 HTAVVFEDQTLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKavvclanmahlvegvlpktgvkqVIVTEvgDILPPLKRFIvnfvvKHIKKMVPayslpqatkltDALARGAGKSF 199
Cdd:cd17655 92 DSGAD-----------------------ILLTQ--SHLQPPIAFI-----GLIDLLDE-----------DTIYHEESENL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 qEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGCEI-LIAPlplYHIYAFTFHCMAMMLTGN 278
Cdd:cd17655 131 -EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI--YQGEHLRVaLFAS---ISFDASVTEIFASLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILITNPRDLP--SMLKDLGQWKFTGFVGLNTLFVALcnnETFRKLDFSALKLTLSGGMALQLATAERWKEV--TGCAI 354
Cdd:cd17655 205 TLYIVRKETVLDgqALTQYIRQNRITIIDLTPAHLKLL---DAADDSEGLSLKHLIVGGEALSTELAKKIIELfgTNPTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 355 CEGYGMTET---APVVSVNPFQNIQVGT-IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILD 430
Cdd:cd17655 282 TNAYGPTETtvdASIYQYEPETDQQVSVpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFV 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 431 ADGWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVV 504
Cdd:cd17655 362 DDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 15598495 505 KPgaTLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17655 442 EK--ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
48-547 |
2.76e-30 |
|
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: 125.00 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLD-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 CLAnmahlvEGVLPKTGVKQVIVteVGDILPPLKRFIVNFVVKHiKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQAD 207
Cdd:cd17634 162 TAD------GGVRAGRSVPLKKN--VDDALNPNVTSVEHVIVLK-RTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHrnlvanmlqckalmganlneGCEILIAPLPLYHIYAF-------TFHCMAMMLtgNHN 280
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVLHTT--------------------GGYLVYAATTMKYVFDYgpgdiywCTADVGWVT--GHS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPRDL----------PSMLKDLGQWKFTGFVGLNTLF--------VALCNNETFRKLDFSALKLTLSGGMALQLAT 342
Cdd:cd17634 291 YLLYGPLACgattllyegvPNWPTPARMWQVVDKHGVNILYtaptairaLMAAGDDAIEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 343 AERWKEVTG---CAICEGYGMTETA-PVVSVNP-FQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGP---QV 414
Cdd:cd17634 371 YEWYWKKIGkekCPVVDTWWQTETGgFMITPLPgAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgQT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEILDA-DGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEK 493
Cdd:cd17634 451 RTLFGDHERFEQTYFSTfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAI 530
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 494 SGESIKVFVVVKPGATLT-------KEQVMQHMHDNLTgykrPKAVEFRDSLPTTNVGKIL 547
Cdd:cd17634 531 KGQAPYAYVVLNHGVEPSpelyaelRNWVRKEIGPLAT----PDVVHWVDSLPKTRSGKIM 587
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
26-550 |
4.78e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 124.28 E-value: 4.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 26 ILSVLKESCQRFATKPAFT---------NLGKTLTYGELYKLSGDFAAYLQQHTDlkPGDRIAVQLPNVLQYPIVVFGAM 96
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTfidyeqdpaGVAETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 97 RAGLIVVntnPLYT-ARELEHQfndsgakavvclanmahLVEGVLPKTGVKQVIVTevgdilpplkrfivNFVVKHIKKM 175
Cdd:PRK05850 81 QAGLIAV---PLSVpQGGAHDE-----------------RVSAVLRDTSPSVVLTT--------------SAVVDDVTEY 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 176 VPAYSLPQATKLT--DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQckaLMGANL-NEGCe 252
Cdd:PRK05850 127 VAPQPGQSAPPVIevDLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQ---LMSDYFgDTGG- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 253 ilIAP--------LPLYHIYAFTFHCMAMMLTGNHNILiTNP--------RDLPSMLKDLGQW----KFtGFvglnTLFV 312
Cdd:PRK05850 203 --VPPpdttvvswLPFYHDMGLVLGVCAPILGGCPAVL-TSPvaflqrpaRWMQLLASNPHAFsaapNF-AF----ELAV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 313 ALCNNETFRKLDFSALKLTLSGGMALQLATAERWKE------VTGCAICEGYGMTE------------TAPVVSVNPfQN 374
Cdd:PRK05850 275 RKTSDDDMAGLDLGGVLGIISGSERVHPATLKRFADrfapfnLRETAIRPSYGLAEatvyvatrepgqPPESVRFDY-EK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 375 IQVGTI--------------GIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDA--------- 431
Cdd:PRK05850 354 LSAGHAkrcetgggtplvsyGSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpspgt 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 432 -DG-WLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVYPnelEDVLATL----PGvlQCAAIGIPDEKSGESIKVFVVVK 505
Cdd:PRK05850 434 pEGpWLRTGDLGFIS-EGELFIVGRIKDLLIVDGRNHYP---DDIEATIqeitGG--RVAAISVPDDGTEKLVAIIELKK 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 506 PGAtlTKEQVMQHMHD---NLT-GYKRPKAVEFRD-------SLPTTNVGKILRRE 550
Cdd:PRK05850 508 RGD--SDEEAMDRLRTvkrEVTsAISKSHGLSVADlvlvapgSIPITTSGKIRRAA 561
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
14-554 |
6.06e-30 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 124.22 E-value: 6.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 14 IAAEINPDQYPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVF 93
Cdd:PRK08279 27 RTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 94 GAMRAGLIV--VNTNplYTARELEHQFNDSGAKAVVCLANMAHLVEGVLPktgvkqvivtevgdilpplkrfivnfvvkH 171
Cdd:PRK08279 106 GLAKLGAVValLNTQ--QRGAVLAHSLNLVDAKHLIVGEELVEAFEEARA-----------------------------D 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 172 IKKMVPAYSLPQATKLT-------DALARGAGKSFQEAAP--QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKAL 242
Cdd:PRK08279 155 LARPPRLWVAGGDTLDDpegyedlAAAAAGAPTTNPASRSgvTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 243 MGANLNEgceILIAPLPLYHIYAFTFhCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETfRK 322
Cdd:PRK08279 235 LRLTPDD---VLYCCLPLYHNTGGTV-AWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPP-KP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 323 LDfSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTEtAPVVSVNpFQNIqVGTIGIpVPSTLCK----------- 390
Cdd:PRK08279 310 TD-RDHRLRLMIGNGLRPDIWDEFQQRFGIPrILEFYAASE-GNVGFIN-VFNF-DGTVGR-VPLWLAHpyaivkydvdt 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 391 ---VIGDDG--QEVPLGERGELC--VKGPQVMKGYWQRQEATDEIL-----DADGWLKTGDIAIIQEDGYMRIVDRKKDM 458
Cdd:PRK08279 385 gepVRDADGrcIKVKPGEVGLLIgrITDRGPFDGYTDPEASEKKILrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDT 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 459 ILVSGFNVYPNELEDVLATLPGVLQCAAIG--IP--DEKSGesiKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEF 534
Cdd:PRK08279 465 FRWKGENVATTEVENALSGFPGVEEAVVYGveVPgtDGRAG---MAAIVLADGAEFDLAALAAHLYERLPAYAVPLFVRL 541
|
570 580
....*....|....*....|
gi 15598495 535 RDSLPTTNVGKILRRELRDE 554
Cdd:PRK08279 542 VPELETTGTFKYRKVDLRKE 561
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
215-551 |
6.48e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 123.57 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 215 TGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILIApLPLYHIYAFTFHCMAMMLTGNhnILITNPRDLPSMLK 294
Cdd:PRK13383 182 TSGTTGKPKGVPRAPQLRSAVGVWVTILDRTRLRTGSRISVA-MPMFHGLGLGMLMLTIALGGT--VLTHRHFDAEAALA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 295 DLGQWKFTGFVGLNTLFVALCN--NETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPF 372
Cdd:PRK13383 259 QASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 373 Q-NIQVGTIGIPVPSTLCKVIGDDGQevPLGER--GELCVKGPQVMKGYwqrqeaTDEILDA--DGWLKTGDIAIIQEDG 447
Cdd:PRK13383 339 DlRDAPETVGKPVAGCPVRILDRNNR--PVGPRvtGRIFVGGELAGTRY------TDGGGKAvvDGMTSTGDMGYLDNAG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 448 YMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYK 527
Cdd:PRK13383 411 RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFE 490
|
330 340
....*....|....*....|....
gi 15598495 528 RPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK13383 491 QPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
63-556 |
1.11e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 123.69 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 63 AAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYTARELEHQ------FNDSGAKAVVCLANMAhlv 136
Cdd:PRK07769 69 GARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVgrlhavLDDCTPSAILTTTDSA--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 137 EGVlpktgvkqvivtevgdilpplKRFIvnfvvkhikKMVPAYSLPQATKLtDALARGAGKSFQEAAPQADDVAVLQYTG 216
Cdd:PRK07769 141 EGV---------------------RKFF---------RARPAKERPRVIAV-DAVPDEVGATWVPPEANEDTIAYLQYTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 217 GTTGVAKGAMLTHRNLVANMLQckALMGANLNEGCEiLIAPLPLYHIYAFTFHCMAMMltGNHNILITNPRdlpSMLKDL 296
Cdd:PRK07769 190 GSTRIPAGVQITHLNLPTNVLQ--VIDALEGQEGDR-GVSWLPFFHDMGLITVLLPAL--LGHYITFMSPA---AFVRRP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 297 GQW------KFTGFVGLntlFVALCN------------NETFRKLDFSALKLTLSGGMALQLATAERWKEVTG------C 352
Cdd:PRK07769 262 GRWirelarKPGGTGGT---FSAAPNfafehaaarglpKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFApyglppT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTETAPVVSVNPFQNI----------------------------QVGTIGIPVPSTLCKVIGDDGQEVPLGER 404
Cdd:PRK07769 339 AIKPSYGMAEATLFVSTTPMDEEptviyvdrdelnagrfvevpadapnavaQVSAGKVGVSEWAVIVDPETASELPDGQI 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 405 GELCVKGPQVMKGYWQRQEATDE----ILD-------ADG------WLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVY 467
Cdd:PRK07769 419 GEIWLHGNNIGTGYWGKPEETAAtfqnILKsrlseshAEGapddalWVRTGDYGVYF-DGELYITGRVKDLVIIDGRNHY 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 468 PNELEDVL-----ATLPGVLqcAAIGIP----------DEKSG------ESIKVFVVVKPGATLTKEQVMQHMHDNL-TG 525
Cdd:PRK07769 498 PQDLEYTAqeatkALRTGYV--AAFSVPanqlpqvvfdDSHAGlkfdpeDTSEQLVIVAERAPGAHKLDPQPIADDIrAA 575
|
570 580 590
....*....|....*....|....*....|....*...
gi 15598495 526 YKRPKAVEFRD-------SLPTTNVGKILRRELRDEEL 556
Cdd:PRK07769 576 IAVRHGVTVRDvllvpagSIPRTSSGKIARRACRAAYL 613
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
24-551 |
2.02e-29 |
|
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: 121.43 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 24 PNILSVLKESCQrfatkpaftnlgktLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVV 103
Cdd:cd17656 2 PDAVAVVFENQK--------------LTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 104 NTNPLYTARELEHQFNDSGAKAVVCLANMAHLVEgvlpktgvkqvivtevgdilpplkrfiVNFVVKHIKKMVPAYSLPQ 183
Cdd:cd17656 67 PIDPEYPEERRIYIMLDSGVRVVLTQRHLKSKLS---------------------------FNKSTILLEDPSISQEDTS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 184 ATKLTDAlargagksfqeaapqADDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQCKaLMGANLNEGCEILIAPLPLYHI 263
Cdd:cd17656 120 NIDYINN---------------SDDLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFE-REKTNINFSDKVLQFATCSFDV 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 264 -YAFTFhcmAMMLTGNHNILITNP--RDLPSmLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDF-SALKLTLSGGMALQ 339
Cdd:cd17656 183 cYQEIF---STLLSGGTLYIIREEtkRDVEQ-LFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFpTCVKHIITAGEQLV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 340 LA-TAERWKEVTGCAICEGYGMTETAPVV--SVNPFQNIQ-VGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVM 415
Cdd:cd17656 259 ITnEFKEMLHEHNVHLHNHYGPSETHVVTtyTINPEAEIPeLPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVA 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 416 KGYWQRQEATDEILDADGW------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGI 489
Cdd:cd17656 339 RGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDK 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598495 490 PDEKSGESIKVFVVvkPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17656 419 ADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
50-459 |
2.95e-29 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 122.53 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQQ--HtdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVAlgH---NKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 C----LANMAHLVEGVlpkTGVKQVI-VTEVGDILPPLKRFIVNFVVKhikkmvpaySLPQATKLtdalarGAGKSFQEA 202
Cdd:PLN02387 184 CdskqLKKLIDISSQL---ETVKRVIyMDDEGVDSDSSLSGSSNWTVS---------SFSEVEKL------GKENPVDPD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 APQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqcKALMGA--NLNEGcEILIAPLPLYHIYAFTFHCM--------- 271
Cdd:PLN02387 246 LPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATV---AGVMTVvpKLGKN-DVYLAYLPLAHILELAAESVmaavgaaig 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 ---AMMLTGNHN----------------ILITNP------RD-----------LPSMLKDL----------GQWkfTGFV 305
Cdd:PLN02387 322 ygsPLTLTDTSNkikkgtkgdasalkptLMTAVPaildrvRDgvrkkvdakggLAKKLFDIaykrrlaaieGSW--FGAW 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 306 GLNTLfvaLCNNETFRKLDfSAL----KLTLSGGMALQLATaERWKEVT-GCAICEGYGMTETAPVVSVNPFQNIQVGTI 380
Cdd:PLN02387 400 GLEKL---LWDALVFKKIR-AVLggriRFMLSGGAPLSGDT-QRFINIClGAPIGQGYGLTETCAGATFSEWDDTSVGRV 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 381 GIPVPSTLCKVIG-DDG----QEVPLgERGELCVKGPQVMKGYWQRQEATDEILDADG----WLKTGDIAIIQEDGYMRI 451
Cdd:PLN02387 475 GPPLPCCYVKLVSwEEGgyliSDKPM-PRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEI 553
|
....*...
gi 15598495 452 VDRKKDMI 459
Cdd:PLN02387 554 IDRKKDIV 561
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
41-554 |
1.15e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.79 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 41 PAFTNLGKTLTYGELYKLSGDFAAYLQqhtDLKPGDR---IAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQ 117
Cdd:PRK07867 20 RGLYFEDSFTSWREHIRGSAARAAALR---ARLDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 118 FNDSGAKAVVCLANMAHLVEGVLPktGVKqVIVTEVgdilpplkrfivnfvvkhikkmvPAYslpqatklTDALARGAGK 197
Cdd:PRK07867 97 IAHADCQLVLTESAHAELLDGLDP--GVR-VINVDS-----------------------PAW--------ADELAAHRDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 198 SFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLV--ANMLQCKALMGANlnegcEILIAPLPLyhiyaftFHCMAMM- 274
Cdd:PRK07867 143 EPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVAsaGVMLAQRFGLGPD-----DVCYVSMPL-------FHSNAVMa 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 275 -----LTGNHNILITNPRDLPSMLKDLGQWKFT--GFVGL----------------NTLFVALCNNETFRKLDfsalklt 331
Cdd:PRK07867 211 gwavaLAAGASIALRRKFSASGFLPDVRRYGATyaNYVGKplsyvlatperpddadNPLRIVYGNEGAPGDIA------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 332 lsggmalqlATAERWkevtGCAICEGYGMTETApvVSVNPFQNIQVGTIGIPVPSTlcKVIG-DDGQEVPLGER------ 404
Cdd:PRK07867 284 ---------RFARRF----GCVVVDGFGSTEGG--VAITRTPDTPPGALGPLPPGV--AIVDpDTGTECPPAEDadgrll 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 405 ------GELC-VKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT 477
Cdd:PRK07867 347 nadeaiGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598495 478 LPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMH--DNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK07867 426 YPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAaqPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAE 504
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
48-442 |
1.83e-28 |
|
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: 119.46 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHqfndsgakavv 127
Cdd:cd05921 24 RRVTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMSQDL----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 clANMAHLVEGVLPKtgvkqVIVTEVGdilPPLKRFIVNFVVKHiKKMVPAYSLPQ---ATKLTDALARGAGKSFQEAAP 204
Cdd:cd05921 92 --AKLKHLFELLKPG-----LVFAQDA---APFARALAAIFPLG-TPLVVSRNAVAgrgAISFAELAATPPTAAVDAAFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QA--DDVAVLQYTGGTTGVAKGAMLTHRNLVAN---MLQCKALMGanlnEGCEILIAPLPLYHIYAFTfHCMAMMLTGNH 279
Cdd:cd05921 161 AVgpDTVAKFLFTSGSTGLPKAVINTQRMLCANqamLEQTYPFFG----EEPPVLVDWLPWNHTFGGN-HNFNLVLYNGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILITNPRDLPSM----LKDLGQ----WKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEV-- 349
Cdd:cd05921 236 TLYIDDGKPMPGGfeetLRNLREisptVYFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALav 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 --TGCAI--CEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVigddgqeVPLGERGELCVKGPQVMKGYWQRQEAT 425
Cdd:cd05921 316 atVGERIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELT 388
|
410
....*....|....*..
gi 15598495 426 DEILDADGWLKTGDIAI 442
Cdd:cd05921 389 AQAFDEEGFYCLGDAAK 405
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
29-551 |
3.57e-28 |
|
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: 117.27 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 29 VLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPL 108
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 109 YTARELEHQFNDSGAKavvclanmahlvegvlpktgvkqVIVTevgdilpplkrfivnfvvkhikkmvpayslpqatklt 188
Cdd:cd17645 82 YPGERIAYMLADSSAK-----------------------ILLT------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 dalargagksfqeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILIAplplYHIYAFTF 268
Cdd:cd17645 102 ----------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYAS----FSFDASAW 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 269 HCMAMMLTGNHNILITNPRDLPsmLKDLGQWKFTGFVGLNTLFVALCnnETFRKLDFSALKLTLSGGMALQLATAERWKe 348
Cdd:cd17645 162 EIFPHLTAGAALHVVPSERRLD--LDALNDYFNQEGITISFLPTGAA--EQFMQLDNQSLRVLLTGGDKLKKIERKGYK- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 349 vtgcaICEGYGMTETAPVVSV----NPFQNIqvgTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEA 424
Cdd:cd17645 237 -----LVNNYGPTENTVVATSfeidKPYANI---PIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPEL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 425 TDEILDADGWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESI 498
Cdd:cd17645 309 TAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYL 388
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15598495 499 KVFVVVKPGATLtkEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17645 389 VAYVTAPEEIPH--EELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
47-554 |
6.40e-28 |
|
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: 116.68 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIV--VNTNplYTARELEHQFNDSGAK 124
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAalINYN--LRGESLAHCLNVSSAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVClanmahlvegvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaap 204
Cdd:cd05940 78 HLVV---------------------------------------------------------------------------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 qadDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQCKALMGANLNEgcEILIAPLPLYHIYAFTFhCMAMMLTGNHNILIT 284
Cdd:cd05940 82 ---DAALYIYTSGTTGLPKAAIISHRRAW-RGGAFFAGSGGALPS--DVLYTCLPLYHSTALIV-GWSACLASGATLVIR 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 NPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNneTFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTEt 363
Cdd:cd05940 155 KKFSASNFWDDIRKYQATIFQYIGELCRYLLN--QPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPrIAEFYAATE- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVNPFQNIqvGTIGIpVPSTLCKVIGD----------------DG--QEVPLGERGELC--VKGPQVMKGYWQRQE 423
Cdd:cd05940 232 GNSGFINFFGKP--GAIGR-NPSLLRKVAPLalvkydlesgepirdaEGrcIKVPRGEPGLLIsrINPLEPFDGYTDPAA 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 424 ATDEIL-----DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIP----DEKS 494
Cdd:cd05940 309 TEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGRA 388
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 495 GESIkvfVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:cd05940 389 GMAA---IVLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
50-487 |
6.63e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 118.22 E-value: 6.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELyKLSGDfaAYLQQHTDLK--PGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQ---------- 117
Cdd:PRK12582 81 VTYGEA-KRAVD--ALAQALLDLGldPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLMSHDHAklkhlfdlvk 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 118 ----FNDSGAKAVVCLAnmahlvegVLPKTGVKQVIVTEVGDILPPLkrfivnfvvkHIKKMVpayslpqATKLTDALAr 193
Cdd:PRK12582 158 prvvFAQSGAPFARALA--------ALDLLDVTVVHVTGPGEGIASI----------AFADLA-------ATPPTAAVA- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 194 gagKSFQEAAPqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCEILIAPLPLYHIYA--FTFHcm 271
Cdd:PRK12582 212 ---AAIAAITP--DTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGgnANFN-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 aMMLTGNHNILITNPRDLPSM----LKDLGQWKFTGF----VGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATA 343
Cdd:PRK12582 285 -GLLWGGGTLYIDDGKPLPGMfeetIRNLREISPTVYgnvpAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLY 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 344 ERWKEVTGCAICE------GYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVigddgqeVPLGERGELCVKGPQVMKG 417
Cdd:PRK12582 364 ERMQALAVRTTGHripfytGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 418 YWQRQEATDEILDADGWLKTGDIAI----------IQEDGymRIVDrkkDMILVSGFNVYPNELE-DVLATLPGVLQCAA 486
Cdd:PRK12582 437 YHKDPELTAAAFDEEGFYRLGDAARfvdpddpekgLIFDG--RVAE---DFKLSTGTWVSVGTLRpDAVAACSPVIHDAV 511
|
.
gi 15598495 487 I 487
Cdd:PRK12582 512 V 512
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
48-551 |
9.90e-28 |
|
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: 115.96 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 48 KTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVV 127
Cdd:cd17648 11 KRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 128 clanmahlvegvlpkTGVKqvivtevgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapqad 207
Cdd:cd17648 91 ---------------TNST------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANlNEGCEILIaplpLYHIYAFTFHC--MAMMLTGNHNILITN 285
Cdd:cd17648 95 DLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR-DNGDEAVL----FFSNYVFDFFVeqMTLALLNGQKLVVPP 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 prdlPSMLKDlgQWKFTGFVGLNTLFVALCNNETFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTE 362
Cdd:cd17648 170 ----DEMRFD--PDRFYAYINREKVTYLSGTPSVLQQYDLArlpHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 363 TA--PVVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEIL----------D 430
Cdd:cd17648 244 TTvtNHKRFFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFlpnpfqteqeR 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 431 ADG----WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKV-----F 501
Cdd:cd17648 324 ARGrnarLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQkylvgY 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15598495 502 VVVKPGaTLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17648 404 YLPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
49-439 |
3.12e-27 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 116.13 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARelehqfndSGAkavvc 128
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDR-GLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLV--------SQD----- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 LANMAHLVEGVLPKTgvkqVIVTEVG------DILPPLKRFIVnfVVKHIKKMVPAYSLPQ--ATKLTDALARGAgksfq 200
Cdd:PRK08180 135 FGKLRHVLELLTPGL----VFADDGAafaralAAVVPADVEVV--AVRGAVPGRAATPFAAllATPPTAAVDAAH----- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 eAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgANLNEGCEILIAPLPLYHiyafTF---HCMAMMLTG 277
Cdd:PRK08180 204 -AAVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPPVLVDWLPWNH----TFggnHNLGIVLYN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 278 NHNILITNPRDLP----SMLKDL----GQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLATAERWKEV 349
Cdd:PRK08180 278 GGTLYIDDGKPTPggfdETLRNLreisPTVYFNVPKGWEMLVPALERDAALRRRFFSRLKLLFYAGAALSQDVWDRLDRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TG--C----AICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVigddgqeVPLGERGELCVKGPQVMKGYWQRQE 423
Cdd:PRK08180 358 AEatCgeriRMMTGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPE 430
|
410
....*....|....*.
gi 15598495 424 ATDEILDADGWLKTGD 439
Cdd:PRK08180 431 LTAEAFDEEGYYRSGD 446
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
205-553 |
3.12e-27 |
|
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: 114.95 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCeiliaplplYHIYAFTF------HCMAMMLTGN 278
Cdd:cd05918 104 SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRV---------LQFASYTFdvsileIFTTLAAGGC 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 hnILITNPRDLPSmlkDLgqwkfTGFV---GLNTLF----VAlcnnETFRKLDFSALKLTLSGGMALQLATAERWKEvtG 351
Cdd:cd05918 175 --LCIPSEEDRLN---DL-----AGFInrlRVTWAFltpsVA----RLLDPEDVPSLRTLVLGGEALTQSDVDTWAD--R 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 352 CAICEGYGMTETAPVVSVNPFQNI-QVGTIGIPVPSTLCKVI-GDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEI- 428
Cdd:cd05918 239 VRLINAYGPAECTIAATVSPVVPStDPRNIGRPLGATCWVVDpDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAf 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 429 LDADGWL------------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL-ATLPGVLQCAA--IGIPDEK 493
Cdd:cd05918 319 IEDPAWLkqegsgrgrrlyRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLrQSLPGAKEVVVevVKPKDGS 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 494 SGESIKVFVVVKPGATLTKE-----------------QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:cd05918 399 SSPQLVAFVVLDGSSSGSGDgdslflepsdefralvaELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
25-557 |
3.88e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 114.99 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 25 NILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQqhtDLKPGDRiavqlpnvlqYPIVVFGAM-------- 96
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFID---SLKLPDK----------SPIIVFGHMspemlatf 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 97 ----RAG--LIVVNTnplYTARELEHQFND-SGAKAVVCLANMAHLVEGVlpktgvkQVIvtevgdilpplkrfivnfvv 169
Cdd:PRK04813 70 lgavKAGhaYIPVDV---SSPAERIEMIIEvAKPSLIIATEELPLEILGI-------PVI-------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 170 khikkmvpayslpQATKLTDALArgAGKSFQEAAP-QADDVAVLQYTGGTTGVAKGAMLTHRNLV--AN-MLQckalmGA 245
Cdd:PRK04813 120 -------------TLDELKDIFA--TGNPYDFDHAvKGDDNYYIIFTSGTTGKPKGVQISHDNLVsfTNwMLE-----DF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 246 NLNEGCEILI-APlplyhiYAFTFHCMAMMLT----GNHNIL----ITNPRDLPSMLK--DLGQWKFTgfvglnTLFVAL 314
Cdd:PRK04813 180 ALPEGPQFLNqAP------YSFDLSVMDLYPTlasgGTLVALpkdmTANFKQLFETLPqlPINVWVST------PSFADM 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 315 C-NNETFRKLDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETAPVVSvnpfqNIQVgT-----------IG 381
Cdd:PRK04813 248 ClLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSAtIYNTYGPTEATVAVT-----SIEI-TdemldqykrlpIG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 382 IPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEIL-DADGW--LKTGDIAIIqEDGYMRIVDRKKDM 458
Cdd:PRK04813 322 YAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYL-EDGLLFYQGRIDFQ 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 459 IlvsGFNVYPNELEDV---LATLPGVLQCAAigIPDEKSGesiKV-----FVVVKPG-----ATLTKeQVMQHMHDNLTG 525
Cdd:PRK04813 401 I---KLNGYRIELEEIeqnLRQSSYVESAVV--VPYNKDH---KVqyliaYVVPKEEdfereFELTK-AIKKELKERLME 471
|
570 580 590
....*....|....*....|....*....|..
gi 15598495 526 YKRPKAVEFRDSLPTTNVGKILRRELRDEELK 557
Cdd:PRK04813 472 YMIPRKFIYRDSLPLTPNGKIDRKALIEEVNK 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-475 |
3.22e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 114.49 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHTDlkPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARElEHQfndsgakav 126
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPPESARR-HHQ--------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 vclANMAHLVEGVLPKtgvkqvIVTEVGDILPPLKRFivnfvvkhikKMVPAYSLPQATKLtDALARGAGKSFQEAAPQA 206
Cdd:PRK05691 106 ---ERLLSIIADAEPR------LLLTVADLRDSLLQM----------EELAAANAPELLCV-DTLDPALAEAWQEPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILITNP 286
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPD-DVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 287 RDLPSMLKDL---GQWKFTGFVGLNTLFvALCN----NETFRKLDFSALKLTLSGGMALQLATAERWKE-VTGCAICE-- 356
Cdd:PRK05691 245 YFLERPLRWLeaiSEYGGTISGGPDFAY-RLCServsESALERLDLSRWRVAYSGSEPIRQDSLERFAEkFAACGFDPds 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 357 ---GYGMTETAPVVS----------------------VNPFQNIQVGTIGIPVPSTLCKVIG-DDGQEVPLGERGELCVK 410
Cdd:PRK05691 324 ffaSYGLAEATLFVSggrrgqgipaleldaealarnrAEPGTGSVLMSCGRSQPGHAVLIVDpQSLEVLGDNRVGEIWAS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 411 GPQVMKGYWQRQEATDEI---LDADGWLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
Cdd:PRK05691 404 GPSIAHGYWRNPEASAKTfveHDGRTWLRTGDLGFLR-DGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-545 |
4.49e-26 |
|
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: 109.78 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 204 PQADDVAVLqYTGGTTGVAKGAMLTHRNL------VANMLQCKALMGANL------NEGCEILIAPlPLYHiYAFTFHCM 271
Cdd:cd05924 1 RSADDLYIL-YTGGTTGMPKGVMWRQEDIfrmlmgGADFGTGEFTPSEDAhkaaaaAAGTVMFPAP-PLMH-GTGSWTAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 272 AMMLTGNHNILITNPRDLPSMLKDLGQWK-----FTGFVGLNTLFVALCNNETFrklDFSALKLTLSGGMALQLATAERW 346
Cdd:cd05924 78 GGLLGGQTVVLPDDRFDPEEVWRTIEKHKvtsmtIVGDAMARPLIDALRDAGPY---DLSSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 KE-VTGCAICEGYGMTET---------APVVSVNPFQNIQVGTIgipvpstlckVIGDDGQEVPLGE--RGELCVKGpQV 414
Cdd:cd05924 155 LElVPNITLVDAFGSSETgftgsghsaGSGPETGPFTRANPDTV----------VLDDDGRVVPPGSggVGWIARRG-HI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEIL-DADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPD 491
Cdd:cd05924 224 PLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15598495 492 EKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGK 545
Cdd:cd05924 304 ERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
189-529 |
1.89e-25 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 110.68 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVAN-------MLQCKALMGANlnegcEILIAPLPLY 261
Cdd:PLN02430 202 DFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFvrgvdlfMEQFEDKMTHD-----DVYLSFLPLA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 262 HIY-----AFTFHCMAMM--LTGNHNILitnpRDlpsmlkDLGQWKFTGFVGLNTLF--------VALCNNETFRKLDFS 326
Cdd:PLN02430 277 HILdrmieEYFFRKGASVgyYHGDLNAL----RD------DLMELKPTLLAGVPRVFerihegiqKALQELNPRRRLIFN 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 327 AL-------------------------------------KLTLSGGMALQLATaERWKEVTGCA-ICEGYGMTETAPVVS 368
Cdd:PLN02430 347 ALykyklawmnrgyshkkaspmadflafrkvkaklggrlRLLISGGAPLSTEI-EEFLRVTSCAfVVQGYGLTETLGPTT 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 369 VN-PFQNIQVGTIGIP-VPSTLCKvigddgQEV------PLGE--RGELCVKGPQVMKGYWQRQEATDEILdADGWLKTG 438
Cdd:PLN02430 426 LGfPDEMCMLGTVGAPaVYNELRL------EEVpemgydPLGEppRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 439 DIAIIQEDGYMRIVDRKKDMILVS-GFNVYPNELEDVLATLPGVLQCAAIGipdeKSGESIKVFVVVkpgatLTKEQVMQ 517
Cdd:PLN02430 499 DIGEILPNGVLKIIDRKKNLIKLSqGEYVALEYLENVYGQNPIVEDIWVYG----DSFKSMLVAVVV-----PNEENTNK 569
|
410
....*....|..
gi 15598495 518 HMHDNltGYKRP 529
Cdd:PLN02430 570 WAKDN--GFTGS 579
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
196-554 |
3.60e-25 |
|
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: 108.70 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 196 GKSFQEAAPQ-------ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGcEILIAPLPLYHIYAftf 268
Cdd:cd05910 67 KQCLQEAEPDafigipkADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG--IRPG-EVDLATFPLFALFG--- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 269 hcMAMMLTG-----NHNILI-TNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNEtfrKLDFSALKLTLSGGMALQLAT 342
Cdd:cd05910 141 --PALGLTSvipdmDPTRPArADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH---GITLPSLRRVLSAGAPVPIAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 343 AERWKEVT--GCAICEGYGMTETAPVVSV---------NPFQNIQVGT-IGIPVPSTLCKVIG---------DDGQEVPL 401
Cdd:cd05910 216 AARLRKMLsdEAEILTPYGATEALPVSSIgsrellattTAATSGGAGTcVGRPIPGVRVRIIEiddepiaewDDTLELPR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 402 GERGELCVKGPQVMKGYWQRQEAT--DEILDADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAT 477
Cdd:cd05910 296 GEIGEITVTGPTVTPTYVNRPVATalAKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNT 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 478 LPGVLQCAAIGIpdEKSGESIKVFVV-VKPGATLTKEQVMQHMHDNLTGY---KRPKAVEFRDSLPTT--NVGKILRREL 551
Cdd:cd05910 376 HPGVRRSALVGV--GKPGCQLPVLCVePLPGTITPRARLEQELRALAKDYphtQRIGRFLIHPSFPVDirHNAKIFREKL 453
|
...
gi 15598495 552 RDE 554
Cdd:cd05910 454 AVW 456
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
191-481 |
4.35e-25 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 109.72 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 191 LARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGaNLNEGC---EILIAPLPLYHIY--- 264
Cdd:PLN02614 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLK-SANAALtvkDVYLSYLPLAHIFdrv 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 265 ---AFTFHCMAM-MLTGNHNILITN------------PRDLPSMLKDLGQW--------KFTGFVGLNTLFVALCNNET- 319
Cdd:PLN02614 286 ieeCFIQHGAAIgFWRGDVKLLIEDlgelkptifcavPRVLDRVYSGLQKKlsdggflkKFVFDSAFSYKFGNMKKGQSh 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 320 ------FRKLDFSALKLTLSGGMALQLATA-------ERWKEVTGCA-ICEGYGMTET-APVVSVNPFQNIQVGTIGIPV 384
Cdd:PLN02614 366 veasplCDKLVFNKVKQGLGGNVRIILSGAaplashvESFLRVVACChVLQGYGLTEScAGTFVSLPDELDMLGTVGPPV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 385 PSTLCKVigddgQEVP------LGE--RGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKK 456
Cdd:PLN02614 446 PNVDIRL-----ESVPemeydaLAStpRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKK 519
|
330 340
....*....|....*....|....*.
gi 15598495 457 DMI-LVSGFNVYPNELEDVLATLPGV 481
Cdd:PLN02614 520 NIFkLSQGEYVAVENIENIYGEVQAV 545
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
351-554 |
6.32e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 108.58 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 351 GCAICEGYGMTETAPVVSVNPfqNIQVGTIGIPVPStLCKVIGDDGQEVP---LGERGELC-----------VKGPQVMK 416
Cdd:PRK13388 288 GCQVEDGYGSSEGAVIVVREP--GTPPGSIGRGAPG-VAIYNPETLTECAvarFDAHGALLnadeaigelvnTAGAGFFE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 417 GYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGE 496
Cdd:PRK13388 365 GYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGD 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 497 SIKVFVVVKPGATLTKEQVMQHMH--DNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:PRK13388 444 QVMAALVLRDGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
47-554 |
6.34e-25 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 108.53 E-value: 6.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAV 126
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLANmahLVEGVLPktgvkqvivtevgdILPPLKRFIVnfvvkHIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQA 206
Cdd:cd05938 83 VVAPE---LQEAVEE--------------VLPALRADGV-----SVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 ---DDVAVLQYTGGTTGVAKGAMLTHRnlvanmlqcKALMGANLNEGC-----EILIAPLPLYHIYAFTFHCMAMMLTGN 278
Cdd:cd05938 141 vtiKSPALYIYTSGTTGLPKAARISHL---------RVLQCSGFLSLCgvtadDVIYITLPLYHSSGFLLGIGGCIELGA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 279 HNILitNPRDLPSML-KDLGQWKFTGFVGLNTLFVALCNneTFRKLDFSALKLTLSGGMALQlatAERWKEVT----GCA 353
Cdd:cd05938 212 TCVL--KPKFSASQFwDDCRKHNVTVIQYIGELLRYLCN--QPQSPNDRDHKVRLAIGNGLR---ADVWREFLrrfgPIR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ICEGYGMTEtAPVVSVNpfQNIQVGTIG-------IPVPSTLCK--------VIGDDGQ--EVPLGERGELCVKGPQV-- 414
Cdd:cd05938 285 IREFYGSTE-GNIGFFN--YTGKIGAVGrvsylykLLFPFELIKfdvekeepVRDAQGFciPVAKGEPGLLVAKITQQsp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDEIL------DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIG 488
Cdd:cd05938 362 FLGYAGDKEQTEKKLlrdvfkKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 489 --IPDEKsGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:cd05938 442 vtVPGHE-GRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
40-551 |
1.04e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.48 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 40 KPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFN 119
Cdd:PRK12467 528 RPALVFGEQVLSYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLD 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 120 DSGAKAVVclaNMAHLVEGVLPKTGVKQVIVTEVGDILpplkrfivnfvvkhikkmvpayslpqatkltdalaRGAGKSF 199
Cdd:PRK12467 607 DSGVRLLL---TQSHLLAQLPVPAGLRSLCLDEPADLL-----------------------------------CGYSGHN 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLV---------------ANMLQCKA---------LMGAnLNEGCEILI 255
Cdd:PRK12467 649 PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALAnyvcviaerlqlaadDSMLMVSTfafdlgvteLFGA-LASGATLHL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 256 APlPLYHIYAFTFHCmammLTGNHNILITNPrdLPSMLKDLgqwkftgfvgLNTLFVALCnnetfrkldfSALKLTLSGG 335
Cdd:PRK12467 728 LP-PDCARDAEAFAA----LMADQGVTVLKI--VPSHLQAL----------LQASRVALP----------RPQRALVCGG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 336 MALQLATAERWKEVT-GCAICEGYGMTETAPVVSVNPF----QNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVK 410
Cdd:PRK12467 781 EALQVDLLARVRALGpGARLINHYGPTETTVGVSTYELsdeeRDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIG 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 411 GPQVMKGYWQRQEATDEILDADGW-------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQ 483
Cdd:PRK12467 861 GAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVRE 940
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598495 484 CAAIGIPDEkSGESIKVFVVVKPGATLTKEQ-----VMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK12467 941 AVVLAQPGD-AGLQLVAYLVPAAVADGAEHQatrdeLKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
207-552 |
1.33e-24 |
|
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: 106.68 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCKALMGA-NLNEGCEILiaplplyHIYAFTFHCMAMMLtgnHNILITN 285
Cdd:cd17649 94 RQLAYVIYTSGSTGTPKGVAVSHGPLAAH---CQATAERyGLTPGDREL-------QFASFNFDGAHEQL---LPPLICG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLpsmLKDLGQWKFTGFV-------GLNTL---------FVALCNNETFRklDFSALKLTLSGGMALQLATAERWKeV 349
Cdd:cd17649 161 ACVV---LRPDELWASADELaemvrelGVTVLdlppaylqqLAEEADRTGDG--RPPSLRLYIFGGEALSPELLRRWL-K 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TGCAICEGYGMTET--APVVSVNPFQNIQVGT---IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEA 424
Cdd:cd17649 235 APVRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 425 TDE--ILDADG-----WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEkSGES 497
Cdd:cd17649 315 TAErfVPDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQ 393
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 498 IKVFVVVKPGATL--TKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd17649 394 LVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
205-551 |
1.37e-24 |
|
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: 106.78 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLvanmlqckALMGANLNEGCEILIAPLPLYHIYAFTFHCMA-----MMLTGNh 279
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNV--------AHAAHAWRREYELDSFPVRLLQMASFSFDVFAgdfarSLLNGG- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 nILITNPRDL---PSMLKD-LGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGmalQLATAERWKEVT----- 350
Cdd:cd17650 162 -TLVICPDEVkldPAALYDlILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIVGS---DGCKAQDFKTLAarfgq 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 351 GCAICEGYGMTETAPVVSV-----NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEAT 425
Cdd:cd17650 238 GMRIINSYGVTEATIDSTYyeegrDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 426 DEILDADGW------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIK 499
Cdd:cd17650 318 AERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15598495 500 VFVVvkPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17650 398 AYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
205-551 |
2.50e-24 |
|
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: 105.98 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanlnegceiLIAPLPLYHIYAFTFHCMA-----MMLTGNH 279
Cdd:cd17644 104 QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYG---------ITSSDRVLQFASIAFDVAAeeiyvTLLSGAT 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 280 NILITNP--RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDF-SALKLTLSGGMALQLATAERWKEVTGCAI-- 354
Cdd:cd17644 175 LVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVGNFIql 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 355 CEGYGMTETAPVVSV-----NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEIL 429
Cdd:cd17644 255 INVYGPTEATIAATVcrltqLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKF 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 430 DADGWL--------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVF 501
Cdd:cd17644 335 ISHPFNsseserlyKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAY 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15598495 502 VVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17644 415 IVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
63-556 |
1.82e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 104.44 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 63 AAYLQQHTdlKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYT------ARELEHQFNDSGAKAVVCLANMAHLV 136
Cdd:PRK12476 82 GARLQQVA--GPGDRVAILAPQGIDYVAGFFAAIKAGTIAV---PLFApelpghAERLDTALRDAEPTVVLTTTAAAEAV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 137 EGVLPKtgvkqvivtevgdiLPPLKRFIVNFVvkhikkmvpayslpqatkltDALARGAGKSFQEAAPQADDVAVLQYTG 216
Cdd:PRK12476 157 EGFLRN--------------LPRLRRPRVIAI--------------------DAIPDSAGESFVPVELDTDDVSHLQYTS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 217 GTTGVAKGAMLTHRNLVANMLQcKALMGANLNEGCEIlIAPLPLYHIYAFTfhcMAMM--LTGNHNILITnP----RDLP 290
Cdd:PRK12476 203 GSTRPPVGVEITHRAVGTNLVQ-MILSIDLLDRNTHG-VSWLPLYHDMGLS---MIGFpaVYGGHSTLMS-PtafvRRPQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 291 SMLKDLGQWKFTGFVglntlfVALCNNETFR------------KLDFSALKLtLSGGMALQLATAERWKEVTG------C 352
Cdd:PRK12476 277 RWIKALSEGSRTGRV------VTAAPNFAYEwaaqrglpaegdDIDLSNVVL-IIGSEPVSIDAVTTFNKAFApyglprT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 353 AICEGYGMTE-TAPVVSVNP--------FQNIQVGT-IGIPVPS----------------TLCKVIGDD--GQEVPLGER 404
Cdd:PRK12476 350 AFKPSYGIAEaTLFVATIAPdaepsvvyLDREQLGAgRAVRVAAdapnavahvscgqvarSQWAVIVDPdtGAELPDGEV 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 405 GELCVKGPQVMKGYWQRQEATDEI--------LD----ADG------WLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNV 466
Cdd:PRK12476 430 GEIWLHGDNIGRGYWGRPEETERTfgaklqsrLAegshADGaaddgtWLRTGDLGVYL-DGELYITGRIADLIVIDGRNH 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 467 YPNELE-DVLATLPGVLQ--CAAIGIPDEKSGEsikvFVVVKPGATLTKEQVMQHMHDNL-TGYKRPKAVEFRD------ 536
Cdd:PRK12476 509 YPQDIEaTVAEASPMVRRgyVTAFTVPAEDNER----LVIVAERAAGTSRADPAPAIDAIrAAVSRRHGLAVADvrlvpa 584
|
570 580
....*....|....*....|.
gi 15598495 537 -SLPTTNVGKILRRELRDEEL 556
Cdd:PRK12476 585 gAIPRTTSGKLARRACRAQYL 605
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
205-473 |
3.67e-23 |
|
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: 103.59 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQC-KALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGNhNILI 283
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAAsQHMDLRPATVGQESVVSYLPLSHIAAQILDIWLPIKVGG-QVYF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 284 TNPR----DLPSMLKDLGQWKFTGF-------------------------------VGLNT------------LFVALCN 316
Cdd:cd05933 227 AQPDalkgTLVKTLREVRPTAFMGVprvwekiqekmkavgaksgtlkrkiaswakgVGLETnlklmggespspLFYRLAK 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 317 NETFRK----LDFSALKLTLSGGMALQLATAERWKEVTgCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPVPSTLCKVI 392
Cdd:cd05933 307 KLVFKKvrkaLGLDRCQKFFTGAAPISRETLEFFLSLN-IPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIH 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 393 --GDDGQevplgerGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNVYPN 469
Cdd:cd05933 386 npDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAgGENVPPV 458
|
....
gi 15598495 470 ELED 473
Cdd:cd05933 459 PIED 462
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
205-504 |
3.93e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 103.77 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEGCE--ILIAPLPLYHIY--AFTFHCMAM-----ML 275
Cdd:PLN02861 218 QKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATEedSYFSYLPLAHVYdqVIETYCISKgasigFW 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 276 TGNHNILITNPRDL-PSML-------------------------KDLGQWKFTgfVGLNTLFVALCNNET---FRKLDFS 326
Cdd:PLN02861 298 QGDIRYLMEDVQALkPTIFcgvprvydriytgimqkissggmlrKKLFDFAYN--YKLGNLRKGLKQEEAsprLDRLVFD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 327 ALKLTLSGGMALQLATA-------ERWKEVTGCA-ICEGYGMTET-----APVVSVNPFqniqVGTIGIPVPSTLCKV-- 391
Cdd:PLN02861 376 KIKEGLGGRVRLLLSGAaplprhvEEFLRVTSCSvLSQGYGLTEScggcfTSIANVFSM----VGTVGVPMTTIEARLes 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 392 ---IGDDG-QEVPlgeRGELCVKGPQVMKGYWQRQEATDEILdADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS-GFNV 466
Cdd:PLN02861 452 vpeMGYDAlSDVP---RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSqGEYV 527
|
330 340 350
....*....|....*....|....*....|....*...
gi 15598495 467 YPNELEDVLATLPGVLQCAAIGipdeKSGESIKVFVVV 504
Cdd:PLN02861 528 AVENLENTYSRCPLIASIWVYG----NSFESFLVAVVV 561
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
22-551 |
1.81e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.73 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 22 QYPNILSV---LKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRA 98
Cdd:PRK12316 3052 EYPLERGVhrlFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIE-RGVGPDVLVGVAVERSLEMVVGLLAILKA 3130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 99 GLIVVNTNPLYTARELEHQFNDSGAKAvvcLANMAHLVegvLPKTGVKQVIVTEVGDilpplkrfivnfvvkhikkmvpa 178
Cdd:PRK12316 3131 GGAYVPLDPEYPEERLAYMLEDSGAQL---LLSQSHLR---LPLAQGVQVLDLDRGD----------------------- 3181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 179 yslpqatkltdalargagKSFQEAAPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLvaNMLQCkaLMGANLNEGCEIL 254
Cdd:PRK12316 3182 ------------------ENYAEANPAirtmPENLAYVIYTSGSTGKPKGVGIRHSAL--SNHLC--WMQQAYGLGVGDR 3239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 255 IAPLPLYHIYAFTFHCMAMMLTGNHNIL-----ITNPRDLPSMLKDLGQWKFTGFVGLNTLFValcnnETFRKLDFSALK 329
Cdd:PRK12316 3240 VLQFTTFSFDVFVEELFWPLMSGARVVLagpedWRDPALLVELINSEGVDVLHAYPSMLQAFL-----EEEDAHRCTSLK 3314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 330 LTLSGGMALQLATAERWkeVTGCAICEGYGMTETAPVVSVNPFQNIQVGT--IGIPVPSTLCKVIGDDGQEVPLGERGEL 407
Cdd:PRK12316 3315 RIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGEL 3392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 408 CVKGPQVMKGYWQRQEATDEILDADGW------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGV 481
Cdd:PRK12316 3393 YLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWV 3472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 482 LQCAAIGIpdekSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK12316 3473 REAVVLAV----DGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
208-552 |
2.85e-22 |
|
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: 100.20 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 208 DVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCkALMGANLNEGCEILIAPLPLYHIYAFTFHCMAMMLTGnhniLITNPR 287
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVLHSLAA-SLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGA----KQVLPG 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 288 DLPS---MLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGG-----MALQLATAERWKEVTGCAICEGYG 359
Cdd:cd05915 229 PRLDpasLVELFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGsaaprSLIARFERMGVEVRQGYGLTETSP 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 360 MT---------ETAPV-----VSVNPFQNIQVGTIGIPVPSTLCkvIGDDGQEVPLgergeLCVKGPQVMKGYWQRQEAT 425
Cdd:cd05915 309 VVvqnfvkshlESLSEeekltLKAKTGLPIPLVRLRVADEEGRP--VPKDGKALGE-----VQLKGPWITGGYYGNEEAT 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 426 DEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVK 505
Cdd:cd05915 382 RSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15598495 506 PgATLTKEQVMQHMHDNLTGYKR-PKAVEFRDSLPTTNVGKILRRELR 552
Cdd:cd05915 462 G-EKPTPEELNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-561 |
4.62e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 101.19 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 20 PDQYPNILSVLKESCQRFATKPAFTNL---GKTLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAM 96
Cdd:PRK12316 1996 PEAYPRGPGVHQRIAEQAARAPEAIAVvfgDQHLSYAELDSRANRLAHRLRA-RGVGPEVRVAIAAERSFELVVALLAVL 2074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 97 RAGLIVVNTNPLYTARELEHQFNDSGAKAVVClanMAHLVEGVLPKTGVKQVIVTEVGDIlpplkrfivnfvvkhikkmv 176
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLT---QRHLLERLPLPAGVARLPLDRDAEW-------------------- 2131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 177 payslpqatkltdalargagKSFQEAAPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKAlMGANLNEG-- 250
Cdd:PRK12316 2132 --------------------ADYPDTAPAvqlaGENLAYVIYTSGSTGLPKGVAVSHGALVA---HCQA-AGERYELSpa 2187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 251 -CEIliaplplyHIYAFTF-----HCMAMMLTGNHNILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLD 324
Cdd:PRK12316 2188 dCEL--------QFMSFSFdgaheQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGR 2259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 325 FSALKLTLSGGMALQLATAERWKE-VTGCAICEGYGMTETAPVVSVNPFQNIQ-VGTIGIPVPSTLCK----VIGDDGQE 398
Cdd:PRK12316 2260 PPAVRVYCFGGEAVPAASLRLAWEaLRPVYLFNGYGPTEAVVTPLLWKCRPQDpCGAAYVPIGRALGNrrayILDADLNL 2339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 399 VPLGERGELCVKGPQVMKGYWQRQEATDEILDADGW-------LKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNEL 471
Cdd:PRK12316 2340 LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEI 2419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 472 EDVLATLPGVLQCAAIGIpDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK12316 2420 EARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
570
....*....|
gi 15598495 552 RDEELKKAGQ 561
Cdd:PRK12316 2499 PKPDVSQLRQ 2508
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
49-483 |
5.01e-22 |
|
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: 99.84 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVntnPLYT---ARELEHQFNDSGAKa 125
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSV---PLQAgasAAQLAPILAETEPR- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 126 vVCLANMAHL---VEGVLPKTGVKQVIV----TEVGDILPPLKRfivnfvvkhIKKMVPAYSLPQATkLTDALARGAGKS 198
Cdd:cd17632 143 -LLAVSAEHLdlaVEAVLEGGTPPRLVVfdhrPEVDAHRAALES---------ARERLAAVGIPVTT-LTLIAVRGRDLP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 199 FQEA---APQADDVAVLQYTGGTTGVAKGAMLTHRnLVANMLQcKALMGANLNEGCEILIAPLPLYHIYAftfhcmamml 275
Cdd:cd17632 212 PAPLfrpEPDDDPLALLIYTSGSTGTPKGAMYTER-LVATFWL-KVSSIQDIRPPASITLNFMPMSHIAG---------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 276 tgnHNILITN-----------PRDLPSMLKDLGQWKFT--GFVG-------------LNTLFVALCNNETFRKLDFSALK 329
Cdd:cd17632 280 ---RISLYGTlarggtayfaaASDMSTLFDDLALVRPTelFLVPrvcdmlfqryqaeLDRRSVAGADAETLAERVKAELR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 330 LTLSGG--MALQLATAERWKEVT-------GCAICEGYGMTEtAPVVSVNpfqniqvGTIGIPvPSTLCKVIgddgqEVP 400
Cdd:cd17632 357 ERVLGGrlLAAVCGSAPLSAEMKafmesllDLDLHDGYGSTE-AGAVILD-------GVIVRP-PVLDYKLV-----DVP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 401 -LG--------ERGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDiaIIQEDGYMRI--VDRKKDMI-LVSGFNVYP 468
Cdd:cd17632 423 eLGyfrtdrphPRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD--VMAELGPDRLvyVDRRNNVLkLSQGEFVTV 500
|
490
....*....|....*
gi 15598495 469 NELEDVLATLPGVLQ 483
Cdd:cd17632 501 ARLEAVFAASPLVRQ 515
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-551 |
1.72e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 15 AAEINPDQyPNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFG 94
Cdd:PRK12316 503 TAAEYPLQ-RGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIER-GVGPDVLVGVAMERSIEMVVALLA 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 95 AMRAGLIVVNTNPLYTARELEHQFNDSGAkavvclanmahlvegvlpktgvkQVIVTE--VGDILPpLKRFIVNFVVKHI 172
Cdd:PRK12316 581 ILKAGGAYVPLDPEYPAERLAYMLEDSGV-----------------------QLLLSQshLGRKLP-LAAGVQVLDLDRP 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 173 KKMVPAYSlpqatkltdalargagksfqEAAPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMlqCKALMGANLN 248
Cdd:PRK12316 637 AAWLEGYS--------------------EENPGtelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRL--CWMQQAYGLG 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 249 EGCEILiaplplyHIYAFTFHCMAMMLTG---NHNILITNPRDLPSMLKDLgqWKFTGFVGLNTL-FV-----ALCNNEt 319
Cdd:PRK12316 695 VGDTVL-------QKTPFSFDVSVWEFFWplmSGARLVVAAPGDHRDPAKL--VELINREGVDTLhFVpsmlqAFLQDE- 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 320 fRKLDFSALKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETApvVSVNPFQNIQVG----TIGIPVPSTLCKVIGD 394
Cdd:PRK12316 765 -DVASCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGgdsvPIGRPIANLACYILDA 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 395 DGQEVPLGERGELCVKGPQVMKGYWQRQEAT------DEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYP 468
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTaerfvpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 469 NELEDVLATLPGVLQCAAIGIpdekSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILR 548
Cdd:PRK12316 922 GEIEARLLEHPWVREAAVLAV----DGKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
...
gi 15598495 549 REL 551
Cdd:PRK12316 998 KAL 1000
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
321-552 |
2.00e-21 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 98.10 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETA-PVVSVNP---FQNIQVGTIGIPVPSTLCKVIGD-D 395
Cdd:PRK10524 350 RKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGwPILAIARgveDRPTRLGSPGVPMYGYNVKLLNEvT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 396 GQEVPLGERGELCVKGP--------------QVMKGYWqrqEATDEILDAdgwlkTGDIAIIQEDGYMRIVDRKKDMILV 461
Cdd:PRK10524 430 GEPCGPNEKGVLVIEGPlppgcmqtvwgdddRFVKTYW---SLFGRQVYS-----TFDWGIRDADGYYFILGRTDDVINV 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 462 SGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE--------QVMQHMHDNLTGYKRPKAVE 533
Cdd:PRK10524 502 AGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADRearlalekEIMALVDSQLGAVARPARVW 581
|
250
....*....|....*....
gi 15598495 534 FRDSLPTTNVGKILRRELR 552
Cdd:PRK10524 582 FVSALPKTRSGKLLRRAIQ 600
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
470-545 |
2.95e-21 |
|
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: 87.60 E-value: 2.95e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598495 470 ELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGK 545
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
46-493 |
5.36e-21 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 96.42 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 46 LGKtLTYGELYKLSGDFAAYLQQHtdlkPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEhqfndsgaka 125
Cdd:PRK06334 43 LGK-LSYNQVRKAVIALATKVSKY----PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVT---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 126 vVClANMAHLVEGVLPKTGVKQVIVTEVGDILPPLKRFIVNFVVKHI----KKMVPAY-SLPqatklTDALARGAGKSFQ 200
Cdd:PRK06334 108 -AC-ANLVGVTHVLTSKQLMQHLAQTHGEDAEYPFSLIYMEEVRKELsfweKCRIGIYmSIP-----FEWLMRWFGVSDK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 EAapqaDDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNegcEILIAPLPLYHIYAFTFHCMAMMLTGNHN 280
Cdd:PRK06334 181 DP----EDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKED---DVMMSFLPPFHAYGFNSCTLFPLLSGVPV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 281 ILITNPRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETFRKLDFSALKLTLSGGMALQLAT-AERWKEVTGCAICEGYG 359
Cdd:PRK06334 254 VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLyQEALKTFPHIQLRQGYG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 360 MTETAPVVSVNPFQNIQVGT-IGIPVPSTLCKVIGDDGQ-EVPLGERGELCVKGPQVMKGYWQRQEATDEI-LDADGWLK 436
Cdd:PRK06334 334 TTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYV 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598495 437 TGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLA---TLP---GVLQCAAIGIPDEK 493
Cdd:PRK06334 414 TGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfGQNaadHAGPLVVCGLPGEK 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-551 |
7.91e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.34 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 19 NPDQYPNILSV---LKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGA 95
Cdd:PRK12316 4543 TDAGYPATRCVhqlVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAV 4621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 96 MRAGLIVVNTNPLYTARELEHQFNDSGAKavvCLANMAHLVEGvlpktgvkqvivtevgdiLPplkrfivnfvvkhIKKM 175
Cdd:PRK12316 4622 LKAGGAYVPLDPEYPRERLAYMMEDSGAA---LLLTQSHLLQR------------------LP-------------IPDG 4667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 176 VPAYSLPQATKLTDalargagksFQEAAPQ----ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANlNEGC 251
Cdd:PRK12316 4668 LASLALDRDEDWEG---------FPAHDPAvrlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT-PDDR 4737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 252 EILIAPlplyhiYAFTFHCMAMM--LTGNHNILITNPR--DLPSMLKDLGQWKFTGFVGLNTLFVALCNNETfRKLDFSA 327
Cdd:PRK12316 4738 VLQFMS------FSFDGSHEGLYhpLINGASVVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPPS 4810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 328 LKLTLSGGMALQLATAER-WKEVTGCAICEGYGMTETAPVVSV-----NPFQNIQVGTIGIPVPSTLCKVIGDDGQEVPL 401
Cdd:PRK12316 4811 LRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLwkardGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPV 4890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 402 GERGELCVKGPQVMKGYWQRQEATDE-----ILDADG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
Cdd:PRK12316 4891 GVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEAR 4970
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 475 LATLPGVLQcaAIGIPDEKSGESIKVFVVVKPGATLT---------KEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGK 545
Cdd:PRK12316 4971 LREHPAVRE--AVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelRDELKAALRERLPEYMVPAHLVFLARMPLTPNGK 5048
|
....*.
gi 15598495 546 ILRREL 551
Cdd:PRK12316 5049 LDRKAL 5054
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-560 |
7.59e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 94.46 E-value: 7.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 11 PAGIAAEINP--DQYPNILSV---LKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNV 85
Cdd:PRK12467 3077 RRQVLHAWNAtaAAYPSERLVhqlIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAI-GVGPDVLVGVAVERS 3155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 86 LQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAvvcLANMAHLVEGvLPKTGVKQVIVTEVGDILPPLKRFIV 165
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL---LLTQAHLLEQ-LPAPAGDTALTLDRLDLNGYSENNPS 3231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 166 NFVvkhikkmvpayslpqatkltdalargagksfqeaapQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGA 245
Cdd:PRK12467 3232 TRV------------------------------------MGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYEL 3275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 246 NLNEGcEILIAPlplYHIYAFTFHCMAMMLTGNHNILITNPRDLPSMLkdlgqWKFTGFVGLNTL-FV-----ALCNNET 319
Cdd:PRK12467 3276 DANDR-VLLFMS---FSFDGAQERFLWTLICGGCLVVRDNDLWDPEEL-----WQAIHAHRISIAcFPpaylqQFAEDAG 3346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 320 FRklDFSALKLTLSGGMALQLATAERWKEVTGCA-ICEGYGMTETAPVVSV-----NPFQNIQVGTIGIPVPSTLCKVIG 393
Cdd:PRK12467 3347 GA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEAVVTVTLwkcggDAVCEAPYAPIGRPVAGRSIYVLD 3424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 394 DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDADGWL-------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNV 466
Cdd:PRK12467 3425 GQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgsggrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRI 3504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 467 YPNELEDVLATLPGVLQCAAIGIpDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKI 546
Cdd:PRK12467 3505 ELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKV 3583
|
570
....*....|....
gi 15598495 547 LRRELRDEELKKAG 560
Cdd:PRK12467 3584 DRKALPDPDAKGSR 3597
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
41-551 |
8.81e-20 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 93.96 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 41 PAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFND 120
Cdd:PRK10252 475 PALADARYQFSYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLED 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 121 SGAKAVVCLANMAHlvegvlpktgvkqvivtevgdilpplkRFivnfvvKHIKKMVPA-YSLPqatkltdaLARGAGKSF 199
Cdd:PRK10252 554 ARPSLLITTADQLP---------------------------RF------ADVPDLTSLcYNAP--------LAPQGAAPL 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAAPQadDVAVLQYTGGTTGVAKGAMLTHRNLVANML--QCKALMGAN---------------------LNEGCEILIA 256
Cdd:PRK10252 593 QLSQPH--HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLwmQNHYPLTADdvvlqktpcsfdvsvweffwpFIAGAKLVMA 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 257 PlPLYH---IYaftfhcMAMMLtgnHNILITNPRDLPSMLkdlgqwkftgfvglnTLFVALCNNETFRKlDFSALKLTLS 333
Cdd:PRK10252 671 E-PEAHrdpLA------MQQFF---AEYGVTTTHFVPSML---------------AAFVASLTPEGARQ-SCASLRQVFC 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 334 GGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPF--QNIQVGT-----IGIPVPSTLCKVIGDDGQEVPLGERGE 406
Cdd:PRK10252 725 SGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAfgEELAAVRgssvpIGYPVWNTGLRILDARMRPVPPGVAGD 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 407 LCVKGPQVMKGYWQRQEATDEILDADGWL------KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPG 480
Cdd:PRK10252 805 LYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPD 884
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 481 VLQ-----CAAIGIPDEKSGESIKV-FVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK10252 885 VEQavthaCVINQAAATGGDARQLVgYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
358-553 |
1.19e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 91.59 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 358 YGMTETAP-VVSVNPFQNIQVGT-IGIPVPS---TLCKvigddgqevplGERGELCVKGPQVMKGYWQrqeatdEILDAD 432
Cdd:PRK07445 261 YGMTETASqIATLKPDDFLAGNNsSGQVLPHaqiTIPA-----------NQTGNITIQAQSLALGYYP------QILDSQ 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 433 GWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATlTK 512
Cdd:PRK07445 324 GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSI-SL 402
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598495 513 EQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK07445 403 EELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-551 |
1.25e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.69 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKav 126
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVE-- 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 vCLANMAHLVEGvlpktgvkqvivtevgdilpplkrfivnfvvkhikkmvpaysLPQATKLTD-ALARGAGKSFQEAAP- 204
Cdd:PRK05691 1231 -LLLTQSHLLER------------------------------------------LPQAEGVSAiALDSLHLDSWPSQAPg 1267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 ---QADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQckaLMGAN--LNEGcEILIAPLPLyhiyAF---TFHCMAMMLT 276
Cdd:PRK05691 1268 lhlHGDNLAYVIYTSGSTGQPKGVGNTHAAL-AERLQ---WMQATyaLDDS-DVLMQKAPI----SFdvsVWECFWPLIT 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 277 GNHnILITNP---RDLPSMLKDLGQWKFTG--FV-GLNTLFValcnnETFRKLDFSALKLTLSGGMALQLATAERWKEV- 349
Cdd:PRK05691 1339 GCR-LVLAGPgehRDPQRIAELVQQYGVTTlhFVpPLLQLFI-----DEPLAAACTSLRRLFSGGEALPAELRNRVLQRl 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 350 TGCAICEGYGMTETApvVSVNPFQ----NIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEAT 425
Cdd:PRK05691 1413 PQVQLHNRYGPTETA--INVTHWQcqaeDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALT 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 426 DE--ILDADG-----WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQcAAIGIPDEKSGESI 498
Cdd:PRK05691 1491 AErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ-AAVLVREGAAGAQL 1569
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 15598495 499 KVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK05691 1570 VGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
344-553 |
4.23e-19 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 90.97 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 344 ERWK---EVTG---CAICEGYGMTET-----APVVSVNPfqnIQVGTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGP 412
Cdd:PRK00174 382 EAWEwyyKVVGgerCPIVDTWWQTETggimiTPLPGATP---LKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDP 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 413 ---QVM----------KGYWQRqeatdeildADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLP 479
Cdd:PRK00174 459 wpgMMRtiygdherfvKTYFST---------FKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHP 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598495 480 GVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE---QVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRD 553
Cdd:PRK00174 530 KVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDElrkELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRK 606
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
207-462 |
2.41e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 88.62 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVaNML--QCKALMGANLNEgcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILit 284
Cdd:PTZ00342 304 DFITSIVYTSGTSGKPKGVMLSNKNLY-NTVvpLCKHSIFKKYNP--KTHLSYLPISHIYERVIAYLSFMLGGTINIW-- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 285 nPRDLPSMLKDLGQWKFTGFVGLNTLF-------------------------VAL---CNNETFRKL-----DFSA---- 327
Cdd:PTZ00342 379 -SKDINYFSKDIYNSKGNILAGVPKVFnriytnimteinnlpplkrflvkkiLSLrksNNNGGFSKFlegitHISSkikd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 328 -----LKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETAPVVSVNPFQNIQVGTIGIPV-PSTLCKVIG----DDGQ 397
Cdd:PTZ00342 458 kvnpnLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTwetyKATD 537
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598495 398 EVPlgeRGELCVKGPQVMKGYWQRQEATDEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVS 462
Cdd:PTZ00342 538 TLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
189-552 |
2.88e-18 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 87.90 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 189 DALARGAGKSFQEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANM--LQCKALMGANLNEGCeiliAPLPLYHIYAF 266
Cdd:PRK05851 134 LATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLrgLNARVGLDAATDVGC----SWLPLYHDMGL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 267 TFhCMAMMLTGnhnilitnprdLPSMLKDLGQWKFTGFVGLNTL------FVALCN---------NETFRKLDFSALKLT 331
Cdd:PRK05851 210 AF-LLTAALAG-----------APLWLAPTTAFSASPFRWLSWLsdsratLTAAPNfaynligkyARRVSDVDLGALRVA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 332 LSGGMALQLATAERWKEVTG------CAICEGYGMTETAPVVSV-NPFQNIQVGTIGIPVPSTLCK--VIGD--DGQEV- 399
Cdd:PRK05851 278 LNGGEPVDCDGFERFATAMApfgfdaGAAAPSYGLAESTCAVTVpVPGIGLRVDEVTTDDGSGARRhaVLGNpiPGMEVr 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 400 --------PLGER--GELCVKGPQVMKGYwqrqeATDEILDADGWLKTGDIAIIQEDGYMrIVDRKKDMILVSGFNVYPN 469
Cdd:PRK05851 358 ispgdgaaGVAGReiGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPT 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 470 ELEDVLATLPGVLQCA--AIGIpDEKSgesikvfvvVKPGATLTKE-----------QVMQHMHDNlTGYKrPKAVEFRD 536
Cdd:PRK05851 432 EIERVAAQVRGVREGAvvAVGT-GEGS---------ARPGLVIAAEfrgpdeagarsEVVQRVASE-CGVV-PSDVVFVA 499
|
410
....*....|....*...
gi 15598495 537 --SLPTTNVGKILRRELR 552
Cdd:PRK05851 500 pgSLPRTSSGKLRRLAVK 517
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
47-486 |
1.56e-17 |
|
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: 85.86 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELehqfndsgakav 126
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQL------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 vclanmahlvEGVLPKTGVKQVIVTEVgdILPPLKRFIVNFVVK-HIKKMVPAYSLPQATKLTDALARGAGKSFQEAAPQ 205
Cdd:cd05905 80 ----------GFLLGTCKVRVALTVEA--CLKGLPKKLLKSKTAaEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCKAL-MGANLNEGcEILIAPLPLYHIYAFTFHCMAMMLTGNHNILI- 283
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLA---HCRALkEACELYES-RPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 284 -----TNPrdlPSMLKDLGQWK-FTGFVGLNTL---FVALCNNETFRKL---DFSALK-LTLSGGMALQLATAERW---- 346
Cdd:cd05905 224 pelmkTNP---LLWLQTLSQYKvRDAYVKLRTLhwcLKDLSSTLASLKNrdvNLSSLRmCMVPCENRPRISSCDSFlklf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 347 ----------KEVTGC----AIC-EGYGMTETAP--------------VVSVNPFQNIQVGTIGIPVPSTLCKVIGDDGQ 397
Cdd:cd05905 301 qtlglspravSTEFGTrvnpFICwQGTSGPEPSRvyldmralrhgvvrLDERDKPNSLPLQDSGKVLPGAQVAIVNPETK 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 398 EVPL-GERGELCVKGPQVMKGYWQRQEATDEILDA------------DGWLKTGDIAIIQ----------EDGYMRIVDR 454
Cdd:cd05905 381 GLCKdGEIGEIWVNSPANASGYFLLDGETNDTFKVfpstrlstgitnNSYARTGLLGFLRptkctdlnveEHDLLFVVGS 460
|
490 500 510
....*....|....*....|....*....|...
gi 15598495 455 KKDMILVSGFNVYPNELED-VLATLPGVLQCAA 486
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAV 493
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
12-561 |
2.19e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.29 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 12 AGIAAEINPDQypNILSVLKESCQRFATKPAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIV 91
Cdd:PRK05691 2178 AGEAGEARLDQ--TLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVG 2254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 92 VFGAMRAGLIVVNTNPLYTARELEHQFNDSGakaVVCLANMAHLVE--GVLPkTGVKQVIVTEVGDILPplkrfivnfvv 169
Cdd:PRK05691 2255 LLAILKAGGAYVPLDPEYPLERLHYMIEDSG---IGLLLSDRALFEalGELP-AGVARWCLEDDAAALA----------- 2319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 170 khikkmvpAYSlpqatklTDALARGAGKSFQeaapqaddvAVLQYTGGTTGVAKGAMLTHRNLVanmLQCKALMGA--NL 247
Cdd:PRK05691 2320 --------AYS-------DAPLPFLSLPQHQ---------AYLIYTSGSTGKPKGVVVSHGEIA---MHCQAVIERfgMR 2372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 248 NEGCEIliaplplyHIYAFTFHC-----MAMMLTGNHNILitnprdlpsmlKDLGQWKFTGFVGL------NTL-FVALC 315
Cdd:PRK05691 2373 ADDCEL--------HFYSINFDAaserlLVPLLCGARVVL-----------RAQGQWGAEEICQLireqqvSILgFTPSY 2433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 316 NNETFRKL----DFSALKLTLSGGMALqlaTAERWKEVTGC----AICEGYGMTETA--PVVSVNPfQNIQVGTIGIPVP 385
Cdd:PRK05691 2434 GSQLAQWLagqgEQLPVRMCITGGEAL---TGEHLQRIRQAfapqLFFNAYGPTETVvmPLACLAP-EQLEEGAASVPIG 2509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 386 StlckVIG--------DDGQEVPLGERGELCVKGPQVMKGYWQRQEATDEILDAD------GWL-KTGDIAIIQEDGYMR 450
Cdd:PRK05691 2510 R----VVGarvayildADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADpfaadgGRLyRTGDLVRLRADGLVE 2585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 451 IVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIpDEKSGESIKVFVVVKPG-------ATLtKEQVMQHMHDNL 523
Cdd:PRK05691 2586 YVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAgqddeaqAAL-REALKAHLKQQL 2663
|
570 580 590
....*....|....*....|....*....|....*...
gi 15598495 524 TGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKKAGQ 561
Cdd:PRK05691 2664 PDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQ 2701
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
41-551 |
3.55e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.52 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 41 PAFTNLGKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFND 120
Cdd:PRK12467 1591 VALVFGEQELTYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIED 1669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 121 SGAKavvCLANMAHLVEGVLPKTGVKQVIVTEVGDILpplkrfivnfvvkhikkmvpayslpqatkltdalaRGAGKSFQ 200
Cdd:PRK12467 1670 SGIE---LLLTQSHLQARLPLPDGLRSLVLDQEDDWL-----------------------------------EGYSDSNP 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 201 EAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGANLNEgCEILiaplplYHIYAFTFHC---MAMMLTG 277
Cdd:PRK12467 1712 AVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD-VVLQ------FTSFAFDVSVwelFWPLING 1784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 278 NhNILITNP---RDLPSMLKDLGQWKFTGFVGLNTLFVALCNNETfRKLDFSALKLTLSGGMALQLATAERWKEVTG-CA 353
Cdd:PRK12467 1785 A-RLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDE-QVEHPLSLRRVVCGGEALEVEALRPWLERLPdTG 1862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 354 ICEGYGMTETA------PVVSVNPFQNIQVgTIGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEATDE 427
Cdd:PRK12467 1863 LFNLYGPTETAvdvthwTCRRKDLEGRDSV-PIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAE 1941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 428 --ILDADGWL-----KTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQcaAIGIPDEKSGESIKV 500
Cdd:PRK12467 1942 rfVADPFGTVgsrlyRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVRE--AVVIAQDGANGKQLV 2019
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 501 FVVVKPGATLTKEQVMQ---------HMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK12467 2020 AYVVPTDPGLVDDDEAQvalrailknHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
200-562 |
2.26e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 78.76 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 200 QEAAPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGCEILIApLPLYHI---------------- 263
Cdd:PRK09029 128 HAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLM--PFTAQDSWLLS-LPLFHVsgqgivwrwlyagatl 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 264 YAFTFHCMAMMLTG-NHNILItnprdlPSMLKDLgqwkftgfvgLNTLFVALcnnetfrkldfsALKLTLSGGMALQLAT 342
Cdd:PRK09029 205 VVRDKQPLEQALAGcTHASLV------PTQLWRL----------LDNRSEPL------------SLKAVLLGGAAIPVEL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 343 AERWKEVTGCAICeGYGMTETApvvsvnpfqniqvgtigipvpSTLCKVIGDDGQEV--PLGER------GELCVKGPQV 414
Cdd:PRK09029 257 TEQAEQQGIRCWC-GYGLTEMA---------------------STVCAKRADGLAGVgsPLPGRevklvdGEIWLRGASL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 415 MKGYWQRQEATDeILDADGWLKTGDIAIIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKS 494
Cdd:PRK09029 315 ALGYWRQGQLVP-LVNDEGWFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEF 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 495 GEsiKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEfrdSLPTT--NVG-KILRRELRDEELKKAGQK 562
Cdd:PRK09029 393 GQ--RPVAVVESDSEAAVVNLAEWLQDKLARFQQPVAYY---LLPPElkNGGiKISRQALKEWVAQQLGNN 458
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
47-554 |
2.58e-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: 78.63 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNplytarelehqFNDSGAKAV 126
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN-----------YNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 VCLAnmahlvegvlpKTGVKQVIVTEvgdilpplkrfivnfvvkhikkmvpayslpqatkltdalargagksfqeaapqa 206
Cdd:cd05937 72 HCLK-----------LSGSRFVIVDP------------------------------------------------------ 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 207 DDVAVLQYTGGTTGVAKGAMLT-HRNLVANMLQCKalmGANLNEGcEILIAPLPLYHIYAFtFHCMAMMLTGNHNILITN 285
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISwRRTLVTSNLLSH---DLNLKNG-DRTYTCMPLYHGTAA-FLGACNCLMSGGTLALSR 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 PRDLPSMLKD--LGQWKFTGFVGlntlfvalcnnETFRKL-------DFSALKLTLSGGMALQLATAERWKEVTGCA-IC 355
Cdd:cd05937 162 KFSASQFWKDvrDSGATIIQYVG-----------ELCRYLlstppspYDRDHKVRVAWGNGLRPDIWERFRERFNVPeIG 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 356 EGYGMTE---TAPVVSVNPFQNIQVGTIG-----------IPVpstlcKVIGDDGQ-----------EVPLGERGELCVK 410
Cdd:cd05937 231 EFYAATEgvfALTNHNVGDFGAGAIGHHGlirrwkfenqvVLV-----KMDPETDDpirdpktgfcvRAPVGEPGEMLGR 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 411 GPQVMK----GYWQRQEAT------DEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPG 480
Cdd:cd05937 306 VPFKNReafqGYLHNEDATesklvrDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPD 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 481 VLQ----------------CAAIGIPDEKSGESikvfvvvkpgaTLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVG 544
Cdd:cd05937 386 IAEanvygvkvpghdgragCAAITLEESSAVPT-----------EFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNH 454
|
570
....*....|
gi 15598495 545 KILRRELRDE 554
Cdd:cd05937 455 KQQKGVLRDE 464
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
423-558 |
2.86e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.15 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 423 EATDEIL--DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKV 500
Cdd:PRK08308 279 NAPEEIVvkMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598495 501 FVVVKPGATLtkEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDEELKK 558
Cdd:PRK08308 359 KVISHEEIDP--VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
322-548 |
3.17e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 75.55 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 322 KLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETApVVSVNPFQ--NIQVGTIGIPVPSTLCKVIGDDGQEV 399
Cdd:PTZ00237 376 KYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGYGQTEIG-ITYLYCYGhiNIPYNATGVPSIFIKPSILSEDGKEL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 400 PLGERGELCVK---GPQVMKGYWQRQEATDEILDA-DGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVL 475
Cdd:PTZ00237 455 NVNEIGEVAFKlpmPPSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSI 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 476 ATLPGVLQCAAIGI--PDEKSgesikvfvvvKPGATLTKEQVMQHMH---------------DNLTGYKRPKAVEFRDSL 538
Cdd:PTZ00237 535 LKHPLVLECCSIGIydPDCYN----------VPIGLLVLKQDQSNQSidlnklkneinniitQDIESLAVLRKIIIVNQL 604
|
250
....*....|
gi 15598495 539 PTTNVGKILR 548
Cdd:PTZ00237 605 PKTKTGKIPR 614
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
47-554 |
8.05e-13 |
|
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: 70.53 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 47 GKTLTYGELYKLSGDFAAYLQQHtDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLI--VVNTNplYTARELEHQFNDSGAK 124
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVEtaLINSN--LRLESLLHCITVSKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 125 AVVClanmahlvegvlpktgvkqvivtevgDILPPLKRFIVnfvvKHIKKMVPayslpqatkltdalargagKSFqeaap 204
Cdd:cd05939 78 ALIF--------------------------NLLDPLLTQSS----TEPPSQDD-------------------VNF----- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 205 qaDDVAVLQYTGGTTGVAKGAMLTH-RNLVANMLQCKAlMGANLNEgceILIAPLPLYHIyAFTFHCMAMMLTGNHNILI 283
Cdd:cd05939 104 --RDKLFYIYTSGTTGLPKAAVIVHsRYYRIAAGAYYA-FGMRPED---VVYDCLPLYHS-AGGIMGVGQALLHGSTVVI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 284 TNPRDLPSMLKDLGQWKFT--GFVG------LNTlfvALCNNETFRKLdfsalKLTLSGGMALQLataerWKEVTG---- 351
Cdd:cd05939 177 RKKFSASNFWDDCVKYNCTivQYIGeicrylLAQ---PPSEEEQKHNV-----RLAVGNGLRPQI-----WEQFVRrfgi 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 352 CAICEGYGMTE-TAPVVSVNPfqniQVGTIG-IPV------PSTLCKVIGD--------DGQEVPL--GERGELC---VK 410
Cdd:cd05939 244 PQIGEFYGATEgNSSLVNIDN----HVGACGfNSRilpsvyPIRLIKVDEDtgelirdsDGLCIPCqpGEPGLLVgkiIQ 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 411 GPQVMK--GYWQRQEATDEIL-----DADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQ 483
Cdd:cd05939 320 NDPLRRfdGYVNEGATNKKIArdvfkKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLED 399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598495 484 CAAIGIPDEKSGESIKVFVVVKPGATLTKEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDE 554
Cdd:cd05939 400 VVVYGVEVPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
49-552 |
2.30e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 69.54 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 49 TLTYGELYKLSGDFAAYLQQhTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPLYTARELEHQFNDSGAKAVVC 128
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKD-VGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVIT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 129 LANMahlvegvlpKTGVKQVivtevgdilpPLKRFIVNFVVKHIKKMVP-----AYSLPQATKLTDA-LARGAGKSFQEA 202
Cdd:PLN02654 199 CNAV---------KRGPKTI----------NLKDIVDAALDESAKNGVSvgiclTYENQLAMKREDTkWQEGRDVWWQDV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 203 APQ-----------ADDVAVLQYTGGTTGVAKGAMLThrnlvanmlqckalmganlNEGCEILIAPLplyHIYAFTFH-- 269
Cdd:PLN02654 260 VPNyptkcevewvdAEDPLFLLYTSGSTGKPKGVLHT-------------------TGGYMVYTATT---FKYAFDYKpt 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 270 ----CMA--------------MMLTGNHNILITNPRDLPsmlkDLG-------QWKFTGFVGLNTLFVALCNNETFRKLD 324
Cdd:PLN02654 318 dvywCTAdcgwitghsyvtygPMLNGATVLVFEGAPNYP----DSGrcwdivdKYKVTIFYTAPTLVRSLMRDGDEYVTR 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 325 FSALKLTLSGGMALQL-ATAERW-KEVTG---CAICEGYGMTETA--------------PVVSVNPFQNIQvgtigiPVp 385
Cdd:PLN02654 394 HSRKSLRVLGSVGEPInPSAWRWfFNVVGdsrCPISDTWWQTETGgfmitplpgawpqkPGSATFPFFGVQ------PV- 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 386 stlckVIGDDGQEVPLGERGELCVKGP-----QVMKGYWQRQEATdEILDADGWLKTGDIAIIQEDGYMRIVDRKKDMIL 460
Cdd:PLN02654 467 -----IVDEKGKEIEGECSGYLCVKKSwpgafRTLYGDHERYETT-YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVIN 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 461 VSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE---QVMQHMHDNLTGYKRPKAVEFRDS 537
Cdd:PLN02654 541 VSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHWAPG 620
|
570
....*....|....*
gi 15598495 538 LPTTNVGKILRRELR 552
Cdd:PLN02654 621 LPKTRSGKIMRRILR 635
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
206-551 |
1.97e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCKALMGanLNEGCEILIAPLPLYHIYAFTFhcMAMMLTGNHNILITN 285
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLA--LSEADVIAQTASQSFDISVWQF--LAAPLFGARVEIVPN 3943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 286 --PRDLPSMLKDLGQWKFTGFVGLNTLFVALCNNEtfrKLDFSALKLTLSGGMALQLATAERW-KEVTGCAICEGYGMTE 362
Cdd:PRK05691 3944 aiAHDPQGLLAHVQAQGITVLESVPSLIQGMLAED---RQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAE 4020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 363 TAPVVSVnpFQNIQVGT------IGIPVPSTLCKVIGDDGQEVPLGERGELCVKGPQVMKGYWQRQEAT-----DEILDA 431
Cdd:PRK05691 4021 CSDDVAF--FRVDLASTrgsylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTalafvPHPFGA 4098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 432 DG--WLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQcAAIGIPDEKSGESIKVFVV-----V 504
Cdd:PRK05691 4099 PGerLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVphqtvL 4177
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15598495 505 KPGATLtkEQVMQHMHDNLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:PRK05691 4178 AQGALL--ERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
292-523 |
1.25e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 57.08 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 292 MLKDLGQwkfTGFVGLNTLFVALCnnETFRKLDFSALKLTLSGGmalqLATAERW--------KEVTGCAICEGYGMTET 363
Cdd:COG1541 170 LMQDFGP---TVLVGTPSYLLYLA--EVAEEEGIDPRDLSLKKG----IFGGEPWseemrkeiEERWGIKAYDIYGLTEV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVN-PFQNiqvgtiGIPVP--STLCKVI-GDDGQEVPLGERGELCVkgpqvmkgywqrqeaTdeILDADGW----L 435
Cdd:COG1541 241 GPGVAYEcEAQD------GLHIWedHFLVEIIdPETGEPVPEGEEGELVV---------------T--TLTKEAMplirY 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 436 KTGDIAIIQED------GYMRIV---DRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKP 506
Cdd:COG1541 298 RTGDLTRLLPEpcpcgrTHPRIGrilGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAP 377
|
250
....*....|....*....
gi 15598495 507 GATL--TKEQVMQHMHDNL 523
Cdd:COG1541 378 GASLeaLAEAIAAALKAVL 396
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
50-513 |
3.18e-08 |
|
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: 56.51 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 50 LTYGELYKLSGDFAAYLQqHTDLKPGDRIAVQLPNVLQYPIVVFGAMRAGLIVVNTNPlytarelehqfnDSGAKAV--- 126
Cdd:cd05943 99 VTWAELRRRVARLAAALR-ALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSP------------DFGVPGVldr 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 127 -------VCLANMAHLVEG-VLPKTGVKQVIVTEvgdiLPPLKRFI-VNFVVKHIKKMVPAYslPQATKLTDALARGAGK 197
Cdd:cd05943 166 fgqiepkVLFAVDAYTYNGkRHDVREKVAELVKG----LPSLLAVVvVPYTVAAGQPDLSKI--AKALTLEDFLATGAAG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 198 SFQ-EAAPQADDVAVLqYTGGTTGVAK-------GAMLTHrnLVANMLQCkalmgaNLNEGCEILiaplplyhiYAFTfh 269
Cdd:cd05943 240 ELEfEPLPFDHPLYIL-YSSGTTGLPKcivhgagGTLLQH--LKEHILHC------DLRPGDRLF---------YYTT-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 270 CMAMMLtgnhNILIT-------------NP--RDLPSMLKDLGQWKFTGFvGLNTLFVALCNNETF---RKLDFSALKLT 331
Cdd:cd05943 300 CGWMMW----NWLVSglavgativlydgSPfyPDTNALWDLADEEGITVF-GTSAKYLDALEKAGLkpaETHDLSSLRTI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 332 LSGGMALqLATAERW--KEVT----------GCAICEGYGMteTAPVVSVNPFQnIQVGTIGIPVpstlcKVIGDDGQEV 399
Cdd:cd05943 375 LSTGSPL-KPESFDYvyDHIKpdvllasisgGTDIISCFVG--GNPLLPVYRGE-IQCRGLGMAV-----EAFDEEGKPV 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 400 PlGERGEL-CVKG-PQVMKGYWQrqeatdeilDADG--------------WlKTGDIAIIQEDGYMRIVDRKKDMILVSG 463
Cdd:cd05943 446 W-GEKGELvCTKPfPSMPVGFWN---------DPDGsryraayfakypgvW-AHGDWIEITPRGGVVILGRSDGTLNPGG 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15598495 464 FNVYPNELEDVLATLPGVLQCAAIGIPDEKSGESIKVFVVVKPGATLTKE 513
Cdd:cd05943 515 VRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE 564
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
215-551 |
6.28e-08 |
|
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: 55.17 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 215 TGGTTGVAKGAMLTHRNLVANMLQCKALMgaNLNEGCEILIAPLPLYHIYAFTFhcmaMMLTGNHNILITNP---RDLPS 291
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCILPNIQHFRSLF--NITSEDILFLTSPLTFDPSVVEI----FLSLSSGATLLIVPtsvKVLPS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 292 MLKD-LGQWKFTGFVGLN-TLF----VALCNNETFRKLdfSALKLTLSGGMAL-QLATAERW-KEVTGCAICEGYGMTET 363
Cdd:cd17654 200 KLADiLFKRHRITVLQATpTLFrrfgSQSIKSTVLSAT--SSLRVLALGGEPFpSLVILSSWrGKGNRTRIFNIYGITEV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 364 APVVSVNPFQNIQVGT-IGIPVPSTLCKVIGDDGQEVplgeRGELCVKGPQ---VMKGYWQRQEATdeildadgWLKTGD 439
Cdd:cd17654 278 SCWALAYKVPEEDSPVqLGSPLLGTVIEVRDQNGSEG----TGQVFLGGLNrvcILDDEVTVPKGT--------MRATGD 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 440 IAIIQeDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEKsgesIKVFVVVKPGATLTKEQVMQHM 519
Cdd:cd17654 346 FVTVK-DGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGESSSSRIHKELQLTL 420
|
330 340 350
....*....|....*....|....*....|..
gi 15598495 520 hdnLTGYKRPKAVEFRDSLPTTNVGKILRREL 551
Cdd:cd17654 421 ---LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
438-562 |
2.10e-05 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 47.38 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 438 GDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATL-PGVLQCAAIGIPDEKSG-ESIKVFVVVK--PGATLTKE 513
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCNAAdESVLETAAIGVPPPGGGpEQLVIAAVLKdpPGSNPDLN 673
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15598495 514 QVMQ----HMHDNLTGYKRPKAVEFRDSLPTTNVGKILRRELRDeELKKAGQK 562
Cdd:PLN03052 674 ELKKifnsAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQ-QLAQELSR 725
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
431-560 |
4.02e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 40.09 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598495 431 ADGWLKTGDIAIIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLATLPGVLQCAAIGIPDEksGESIKV-FVVVKPGAT 509
Cdd:PRK07868 834 ADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVG--GRQLAVaAVTLRPGAA 911
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 15598495 510 LTKEQVMQHMHDNLTGYkRPKAVEFRDSLPTTNVGKILRRELRDEELKKAG 560
Cdd:PRK07868 912 ITAADLTEALASLPVGL-GPDIVHVVPEIPLSATYRPTVSALRAAGIPKPG 961
|
|
| |
