|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1-557 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 1207.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPADVPAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIM 80
Cdd:PRK08974 1 MEKVWLNRYPADVPAEINPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGLGLKKGDRVALM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK 160
Cdd:PRK08974 81 MPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPVKHVILTRMGDQLSTAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANG 240
Cdd:PRK08974 161 GTLVNFVVKYIKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 241 AYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFA 320
Cdd:PRK08974 241 AYGPLLHPGKELVVTALPLYHIFALTVNCLLFIELGGQNLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 321 ALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLP 400
Cdd:PRK08974 321 ELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 401 QGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPK 480
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 481 VVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:PRK08974 480 VLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1-555 |
0e+00 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 880.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPADVPAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIM 80
Cdd:PRK07059 1 MEKIWLKSYPPGVPAEIDASQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQS-RGLAKGARVAIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLsAPK 160
Cdd:PRK07059 80 MPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDLL-GFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANG 240
Cdd:PRK07059 159 GHIVNFVVRRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 241 AYAPLLNDGKE----FVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNS 316
Cdd:PRK07059 239 WLQPAFEKKPRpdqlNFVCALPLYHIFALTVCGLLGMRTGGRNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 317 EEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDG 396
Cdd:PRK07059 319 PDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 397 QVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVA 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 477 LHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK07059 479 SHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRDGKA 557
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1-555 |
0e+00 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 794.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPADVPAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIM 80
Cdd:PRK08751 3 QARPWLQSYPAGVAAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGELQLKKGDRVALM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK 160
Cdd:PRK08751 83 MPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANG 240
Cdd:PRK08751 163 AALVNFVVKYVKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 241 --AYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEE 318
Cdd:PRK08751 243 wlAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 319 FAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQV 398
Cdd:PRK08751 323 FDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 399 LPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALH 478
Cdd:PRK08751 403 LAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 479 PKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK08751 483 PGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAK 559
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1-554 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 771.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPADVPAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIM 80
Cdd:PRK05677 2 IENFWKDKYPAGIAAEINPDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK 160
Cdd:PRK05677 82 LPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHVIVTEVADMLPPLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKaQYVKPV-VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAN 239
Cdd:PRK05677 162 RLLINAVVKHVKKMVPAYHLPQAVKFNDALAKGAG-QPVTEAnPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 240 GAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEF 319
Cdd:PRK05677 241 ALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 320 AALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDlAGYNGSIGLPAPSTQIQVRGDDGQVL 399
Cdd:PRK05677 321 RKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 400 PQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHP 479
Cdd:PRK05677 400 PLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALP 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 480 KVVEVAAVGVPHEVSGELVKIFVVAKDK-SLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:PRK05677 480 GVLQCAAIGVPDEKSGEAIKVFVVVKPGeTLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
3-554 |
0e+00 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 701.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 3 QP--WINSLPADVPAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIM 80
Cdd:PRK12492 2 QPdfWNDKRPAGVPSTIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK 160
Cdd:PRK12492 82 MPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLLPAAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKkAQYVKPVVKS-DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAN 239
Cdd:PRK12492 162 GWLVNTVVDKVKKMVPAYHLPQAVPFKQALRQGR-GLSLKPVPVGlDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 240 GAYA-------PLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNA 312
Cdd:PRK12492 241 ACLSqlgpdgqPLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 313 LVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVR 392
Cdd:PRK12492 321 LMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVE 472
Cdd:PRK12492 401 DDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 473 EVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK12492 481 DVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
..
gi 655376187 553 EA 554
Cdd:PRK12492 561 IA 562
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-551 |
0e+00 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 688.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 25 LLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVVSNFAstleqvvdqtpvknviitglgDLLSAPKRTlvnfvvkyikrlvpkyslphai 184
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVSFT---------------------DLLAAGAPL---------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 smrralragkkaqYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLnDGKEFVVTALPLYHIFA 264
Cdd:cd05936 117 -------------GERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQIKAWLEDLL-EGDDVVLAALPLFHVFG 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 265 LTVNCLLFLHKGANNLLITNPRDIpGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADK 344
Cdd:cd05936 183 LTVALLLPLALGATIVLIPRFRPI-GVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 345 WQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEE 424
Cdd:cd05936 262 FEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 425 TAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVA 504
Cdd:cd05936 342 TAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 655376187 505 KD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05936 421 KEgASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-557 |
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: 542.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 25 LLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphai 184
Cdd:COG0318 80 NPRLTAEELAYILEDSGARALVT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 smrralragkkaqyvkpvvksddiAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPllnDGKEFVVTALPLYHIFA 264
Cdd:COG0318 103 ------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL---TPGDVVLVALPLFHVFG 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 265 LTVNCLLFLHKGANNLLITNpRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADK 344
Cdd:COG0318 156 LTVGLLAPLLAGATLVLLPR-FDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLER 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 345 WQNITKTRLLEGYGLTEASPLVACCPYDLAG-YNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:COG0318 235 FEERFGVRIVEGYGLTETSPVVTVNPEDPGErRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV 503
Cdd:COG0318 315 ATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVV 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 504 AKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:COG0318 394 LRPgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2-553 |
1.25e-165 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 482.58 E-value: 1.25e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 2 DQPWINSLPADVPAEIDASRyASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMM 81
Cdd:PRK05605 12 DKPWLQSYAPWTPHDLDYGD-TTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLR-ALGVRPGDRVAIVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 82 PNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKR 161
Cdd:PRK05605 90 PNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTPLETIVSVNMIAAMPLLQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 162 TLVNFVVKYIKRLVPKYS--LPHAISMRRALRAGKKAQYVK---PVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVL 236
Cdd:PRK05605 170 LALRLPIPALRKARAALTgpAPGTVPWETLVDAAIGGDGSDvshPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 237 QANgAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPrDIPGFVAELKKTPFTALTGVNTLFNALVNS 316
Cdd:PRK05605 250 QGK-AWVPGLGDGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAP-DIDLILDAMKKHPPTWLPGVPPLYEKIAEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 317 EEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQV--RGD 394
Cdd:PRK05605 328 AEERGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIvdPED 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 395 DGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEV 474
Cdd:PRK05605 408 PDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEV 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 475 VALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIK-HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK05605 487 LREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRaYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREE 566
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
24-553 |
1.19e-152 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 447.43 E-value: 1.19e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVN 103
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 104 VNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTP-VKNVII--TGLGDLLSAPKRTLVNFVvkyikrlvpkysl 180
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPaLEHVVIceTEEDDPHTEKMKTFTDFL------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 181 phaismrralrAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLLNDGKefVVTALPLY 260
Cdd:PRK07656 152 -----------AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNA-ADWAEYLGLTEGDR--YLAANPFF 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 261 HIFALTVNCLLFLHKGANnlLITNPRDIPGFVAEL-KKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGG--MAV 337
Cdd:PRK07656 218 HVFGYKAGVNAPLMRGAT--ILPLPVFDPDEVFRLiETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAasMPV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 Q--RAVADKWQNITktrLLEGYGLTEASPLVACCPYD--LAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQ 413
Cdd:PRK07656 296 AllERFESELGVDI---VLTGYGLSEASGVTTFNRLDddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 414 VMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEV 493
Cdd:PRK07656 373 VMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDER 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 494 SGELVKIFVVAKDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK07656 453 LGEVGKAYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-555 |
4.82e-147 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 434.85 E-value: 4.82e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPADVPAEIdASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIM 80
Cdd:PRK06710 3 VEKPWLKSYPEEIPSTI-SYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQK-LGVEKGDRVAIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK 160
Cdd:PRK06710 81 LPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 RTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQang 240
Cdd:PRK06710 161 NLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLM--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 241 AYAPLLN--DGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLItnPR-DIPGFVAELKKTPFTALTGVNTLFNALVNSE 317
Cdd:PRK06710 238 GVQWLYNckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLI--PKfDMKMVFEAIKKHKVTLFPGAPTIYIALLNSP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 318 EFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRG-DDG 396
Cdd:PRK06710 316 LLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 397 QVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 477 LHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK06710 475 EHEKVQEVVTIGVPDPYRGETVKAFVVLKeGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEK 554
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
20-555 |
1.77e-140 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 416.51 E-value: 1.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 20 SRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGM 99
Cdd:PRK06187 3 DYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 100 VVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTP-VKNVIITGLGDLLSAPKRtlvnfvvkyikrlVPKY 178
Cdd:PRK06187 82 VLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPtVRTVIVEGDGPAAPLAPE-------------VGEY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 179 SlphaismrrALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAyaPLLNDGKEFVVtALP 258
Cdd:PRK06187 149 E---------ELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAW--LKLSRDDVYLV-IVP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 259 LYHIFALTVnCLLFLHKGANNLLItnPRDIPGFVAEL--KKTPfTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMA 336
Cdd:PRK06187 217 MFHVHAWGL-PYLALMAGAKQVIP--RRFDPENLLDLieTERV-TFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 337 VQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYD-----LAGYNGSIGLPAPSTQIQVRGDDGQVLP--QGETGELFA 409
Cdd:PRK06187 293 LPPALLREFKEKFGIDLVQGYGMTETSPVVSVLPPEdqlpgQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 410 KGPQVMLGYWQRPEETAKVIDkDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGV 489
Cdd:PRK06187 373 RGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGV 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 490 PHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK06187 452 PDEKWGERPVAVVVLKPgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
29-547 |
4.10e-133 |
|
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: 394.67 E-value: 4.10e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 29 LESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLY 108
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALR-ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 109 TPRELKHQLVDSGAKAIVvvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrr 188
Cdd:cd17631 80 TPPEVAYILADSGAKVLF-------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 189 alragkkaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqANGAYAPLLNDGKEFVVtaLPLYHIFALTVN 268
Cdd:cd17631 98 -----------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV-NALAALDLGPDDVLLVV--APLFHIGGLGVF 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 CLLFLHKGANNLLITNPRdiPG-FVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN 347
Cdd:cd17631 158 TLPTLLRGGTVVILRKFD--PEtVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ItKTRLLEGYGLTEASPLVACCPYDLA-GYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETA 426
Cdd:cd17631 236 R-GVKFVQGYGMTETSPGVTFLSPEDHrRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATA 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 427 KVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD 506
Cdd:cd17631 315 AAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP 393
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655376187 507 KS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILR 547
Cdd:cd17631 394 GAeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
29-462 |
7.28e-130 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 385.51 E-value: 7.28e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 29 LESAVNTYADQPAFVNM-GATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPL 107
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 108 YTPRELKHQLVDSGAKAIVVVSNFasTLEQVVDQTP-VKNVIITGLGDLLSAPKRTLVNFVVKYIKrlvpkyslphaism 186
Cdd:pfam00501 80 LPAEELAYILEDSGAKVLITDDAL--KLEELLEALGkLEVVKLVLVLDRDPVLKEEPLPEEAKPAD-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 rralragkKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVV-TALPLYHIFAL 265
Cdd:pfam00501 144 --------VPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVlSTLPLFHDFGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 266 TVNCLLFLHKGANNLLI--TNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVAD 343
Cdd:pfam00501 216 SLGLLGPLLAGATVVLPpgFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 344 KWQNITKTRLLEGYGLTEASPLVACCPY--DLAGYNGSIGLPAPSTQIQVRGDD-GQVLPQGETGELFAKGPQVMLGYWQ 420
Cdd:pfam00501 296 RFRELFGGALVNGYGLTETTGVVTTPLPldEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 655376187 421 RPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVS 462
Cdd:pfam00501 376 DPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
46-546 |
8.35e-127 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 380.02 E-value: 8.35e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRK-LGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNFASTLEQVVDQTPVKNVIITgLGDLLSApkrtlvnfvVKYIKRLVPKYSLphaismrralrAGKKAQYVKPVVKS 205
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKIIV-LDDKPDG---------VLSIEDLLSPTLG-----------EEDEDLPPPLKDGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYaPLLNDGKEFVVTALPLYHIFAL--TVNCLLFLHKgannLLIT 283
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFL-YGNDGSNDVILGFLPLYHIYGLftTLASLLNGAT----VIIM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 284 NPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN-ITKTRLLEGYGLTEA 362
Cdd:cd05911 221 PKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKrFPNATIKQGYGMTET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVACCPYDLAGYnGSIGLPAPSTQIQVRGDDG-QVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIG 441
Cdd:cd05911 301 GGILTVNPDGDDKP-GSVGRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 442 YMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV-AKDKSLTEKELIKHCRH 520
Cdd:cd05911 380 YFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrKPGEKLTEKEVKDYVAK 459
|
490 500
....*....|....*....|....*....
gi 655376187 521 HLTGYKvpKL---VEFRDELPKTNVGKIL 546
Cdd:cd05911 460 KVASYK--QLrggVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
13-555 |
1.48e-126 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 381.62 E-value: 1.48e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 13 VPAEIDASRyASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALF 92
Cdd:PRK08314 1 LPKSLTLPE-TSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 93 GVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSA-PKRTLVNFVVKyi 171
Cdd:PRK08314 80 AILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDYLPAePEIAVPAWLRA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 172 KRLVPKYSLPHAISMRRALRAGKKAqyvKPV-VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAngayAPLLNDGK 250
Cdd:PRK08314 158 EPPLQALAPGGVVAWKEALAAGLAP---PPHtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGS----VLWSNSTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 251 EFVVTA-LPLYHIFALtVNCLLF-LHKGANNLLITN-PRDIPGFVAELKKTpfTALTGVNTLFNALVNSEEFAALDFSRL 327
Cdd:PRK08314 231 ESVVLAvLPLFHVTGM-VHSMNApIYAGATVVLMPRwDREAAARLIERYRV--THWTNIPTMVVDFLASPGLAERDLSSL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 328 KLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTE-ASPLVAcCPYDlAGYNGSIGLPAPSTQIQV-RGDDGQVLPQGETG 405
Cdd:PRK08314 308 RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTEtMAQTHS-NPPD-RPKLQCLGIPTFGVDARViDPETLEELPPGEVG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 406 ELFAKGPQVMLGYWQRPEETAKV-IDKDG--WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVV 482
Cdd:PRK08314 386 EIVVHGPQVFKGYWNRPEATAEAfIEIDGkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 483 EVAAVGVPHEVSGELVKIFVVAKDKS---LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
207-546 |
7.81e-114 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 341.57 E-value: 7.81e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLlnDGKEFVVTALPLYHIFALTVNcLLFLHKGANNLLITnPR 286
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAA-AALAASGGL--TEGDVFLSTLPLFHIGGLFGL-LGALLAGGTVVLLP-KF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLV 366
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 367 A-CCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKViDKDGWLATGDIGYMDE 445
Cdd:cd04433 156 AtGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 446 KGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTG 524
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPgADLDAEELRAHVRERLAP 314
|
330 340
....*....|....*....|..
gi 655376187 525 YKVPKLVEFRDELPKTNVGKIL 546
Cdd:cd04433 315 YKVPRRVVFVDALPRTASGKID 336
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
36-550 |
9.93e-113 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 344.60 E-value: 9.93e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 36 YADQPAFVN--MGATLTYRKLEERSRAFAAYLQNDLkLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPREL 113
Cdd:cd05904 18 HPSRPALIDaaTGRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 114 KHQLVDSGAKAIVVVSNFASTLEQVVDQtpvknVIITGlgdllSAPKrtlvnfvvkyikrlvpkyslpHAISMRRALRAG 193
Cdd:cd05904 97 AKQVKDSGAKLAFTTAELAEKLASLALP-----VVLLD-----SAEF---------------------DSLSFSDLLFEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 194 KKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANgAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFL 273
Cdd:cd05904 146 DEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV-AGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 HKGANnLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKW-QNITKTR 352
Cdd:cd05904 225 RLGAT-VVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFrAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVACCPYD--LAGYNGSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI 429
Cdd:cd05904 304 LGQGYGMTESTGVVAMCFAPekDRAKYGSVGRLVPNVEAKiVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKS- 508
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSs 463
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655376187 509 LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05904 464 LTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
14-557 |
6.33e-108 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 333.05 E-value: 6.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 14 PAEIDASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFG 93
Cdd:PRK08316 2 MERSTRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALL-DLGLKKGDRVAALGHNSDAYALLWLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 94 VLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKRTLvnfvvkyikr 173
Cdd:PRK08316 81 CARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWL---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 174 lvpkyslphaiSMRRALRAGKKAQyVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQA--NGAYAPllNDgke 251
Cdd:PRK08316 151 -----------DFADWAEAGSVAE-PDVELADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCivAGDMSA--DD--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 252 FVVTALPLYHIFALTVNCLLFLHKGANNLLITNPrDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSI 331
Cdd:PRK08316 214 IPLHALPLYHCAQLDVFLGPYLYVGATNVILDAP-DPELILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 332 GGGMAVQRAVADKWQN-ITKTRLLEGYGLTEASPL-VACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFA 409
Cdd:PRK08316 293 YGASIMPVEVLKELRErLPGLRFYNCYGQTEIAPLaTVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 410 KGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGV 489
Cdd:PRK08316 373 RSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGL 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 490 PHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:PRK08316 452 PDPKWIEAVTAVVVPKAgATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
13-554 |
1.50e-102 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 320.14 E-value: 1.50e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 13 VPAEIDASRYAsllemLESAVNTYADQPAFVNMGA-----TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQY 87
Cdd:COG0365 4 VGGRLNIAYNC-----LDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 88 PIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFA---------STLEQVVDQTP-VKNVIItglgdlls 157
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggkvidlkEKVDEALEELPsLEHVIV-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 158 apkrtlvnfvvkyIKRLVPKYSLPHAISMRRALRAgkKAQYVKPV-VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVL 236
Cdd:COG0365 150 -------------VGRTGADVPMEGDLDWDELLAA--ASAEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 237 qangAYAPLLNDGKE----------FVVTALPLYHIFALTVNCLLFLHKGAnnlliTNPRDiPGFVAEL-KKTPFTALTG 305
Cdd:COG0365 215 ----TTAKYVLDLKPgdvfwctadiGWATGHSYIVYGPLLNGATVVLYEGR-----PDFPD-PGRLWELiEKYGVTVFFT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 306 VNTLFNALVNSEEF--AALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLP 383
Cdd:COG0365 285 APTAIRALMKAGDEplKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVKPGSMGKP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 384 APSTQIQVRGDDGQVLPQGETGELFAKGPQ--VMLGYWQRPEETAKVI--DKDGWLATGDIGYMDEKGFFYIVDRKKDMI 459
Cdd:COG0365 365 VPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVI 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 460 LVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSL----TEKELIKHCRHHLTGYKVPKLVEFRD 535
Cdd:COG0365 445 NVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEpsdeLAKELQAHVREELGPYAYPREIEFVD 524
|
570
....*....|....*....
gi 655376187 536 ELPKTNVGKILRRELRDEA 554
Cdd:COG0365 525 ELPKTRSGKIMRRLLRKIA 543
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
49-550 |
6.67e-102 |
|
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: 314.42 E-value: 6.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVV 128
Cdd:cd05935 2 LTYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SNFastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvksDDI 208
Cdd:cd05935 81 SEL--------------------------------------------------------------------------DDL 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApllNDGKEFVVTALPLYHIfALTVNCLLFLHKGANNLLITNPRDI 288
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTG---LTPSDVILACLPLFHV-TGFVGSLNTAVYVGGTYVLMARWDR 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 289 PGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVAC 368
Cdd:cd05935 163 ETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 369 CPYdLAGYNGSIGLPAPSTQIQV-RGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKV---IDKDGWLATGDIGYMD 444
Cdd:cd05935 243 NPP-LRPKLQCLGIP*FGVDARViDIETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESfieIKGRRFFRTGDLGYMD 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 445 EKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDK---SLTEKELIKHCRHH 521
Cdd:cd05935 322 EEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEyrgKVTEEDIIEWAREQ 401
|
490 500
....*....|....*....|....*....
gi 655376187 522 LTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05935 402 MAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
37-552 |
9.48e-102 |
|
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: 315.79 E-value: 9.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 37 ADQPAFVNMGAT--LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELK 114
Cdd:cd05926 1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAA-LGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 115 HQLVDSGAKAIVVVSNFASTleqvvdqtpvknviitglgDLLSAPKRTL----VNFVVKYIKRLVPKYSLPhaismrrAL 190
Cdd:cd05926 80 FYLADLGSKLVLTPKGELGP-------------------ASRAASKLGLaileLALDVGVLIRAPSAESLS-------NL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 191 RAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApLLNDGKEFVVtaLPLYHIFALTVNCL 270
Cdd:cd05926 134 LADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNITNTYK-LTPDDRTLVV--MPLFHVHGLVASLL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 LFLHKGANNLLitnPrdiPGFVA-----ELKKTPFTALTGVNTLFNALVNSE------EFAALDFSRlklSIGGGMAVqr 339
Cdd:cd05926 211 STLAAGGSVVL---P---PRFSAstfwpDVRDYNATWYTAVPTIHQILLNRPepnpesPPPKLRFIR---SCSASLPP-- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 340 AVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYN-GSIGLPApSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGY 418
Cdd:cd05926 280 AVLEALEATFGAPVLEAYGMTEAAHQMTSNPLPPGPRKpGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGY 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 419 WQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELV 498
Cdd:cd05926 359 LNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEV 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 499 KIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05926 439 AAAVVLReGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-554 |
4.85e-98 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 308.89 E-value: 4.85e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 5 WINSLPADVPaeiDASRY----ASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIM 80
Cdd:PRK06178 14 QQAAWPAGIP---REPEYphgeRPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQ-RGVGAGDRVAVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSA-P 159
Cdd:PRK06178 90 LPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSLRHVIVTSLADVLPAeP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 160 KRTLVNFVvkyikrLVPKYSLPHAISMRRALRAgKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAN 239
Cdd:PRK06178 170 TLPLPDSL------RAPRLAAAGAIDLLPALRA-CTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 240 GAYAPLLNDgkEFVVTALPLYHIfALTVNCLLF-LHKGANNLLITnpR-DIPGFVAELKKTPFTALTGVNTLFNALVNSE 317
Cdd:PRK06178 243 AVAVVGGED--SVFLSFLPEFWI-AGENFGLLFpLFSGATLVLLA--RwDAVAFMAAVERYRVTRTVMLVDNAVELMDHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 318 EFAALDFSRLKLSigggMAVQ------RAVADKWQNITKTRLLEG-YGLTEASplvaCC----------PYDLAGYNGSI 380
Cdd:PRK06178 318 RFAEYDLSSLRQV----RVVSfvkklnPDYRQRWRALTGSVLAEAaWGMTETH----TCdtftagfqddDFDLLSQPVFV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 381 GLPAPSTQIQV-RGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMI 459
Cdd:PRK06178 390 GLPVPGTEFKIcDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEML 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 460 LVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKlVEFRDELP 538
Cdd:PRK06178 469 KVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKpGADLTAAALQAWCRENMAVYKVPE-IRIVDALP 547
|
570
....*....|....*.
gi 655376187 539 KTNVGKILRRELRDEA 554
Cdd:PRK06178 548 MTATGKVRKQDLQALA 563
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
38-556 |
3.42e-95 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 299.08 E-value: 3.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK06839 17 DRIAIITEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDQTPVKNVI-ITGLGDLLSAPkrtlvnfvvkyIKRLVPKyslphaismrralragkka 196
Cdd:PRK06839 97 KDSGTTVLFVEKTFQNMALSMQKVSYVQRVIsITSLKEIEDRK-----------IDNFVEK------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 197 qyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQaNGAYAPLLNDgkEFVVTALPLYHIFALTVNCLLFLHKG 276
Cdd:PRK06839 147 -------NESASFIICYTSGTTGKPKGAVLTQENMFWNALN-NTFAIDLTMH--DRSIVLLPLFHIGGIGLFAFPTLFAG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANnLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGG----MAVQRAVADKwqnitKTR 352
Cdd:PRK06839 217 GV-IIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGapcpEELMREFIDR-----GFL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLV-ACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdK 431
Cdd:PRK06839 291 FGQGFGMTETSPTVfMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-Q 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLT 510
Cdd:PRK06839 370 DGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSsSVLI 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 511 EKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKS 556
Cdd:PRK06839 450 EKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKS 495
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-554 |
2.06e-92 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 293.99 E-value: 2.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFV--NMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:PRK12583 22 DAFDATVARFPDREALVvrHQALRYTWRQLADAVDRLARGLLA-LGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKRTLVNfVVKYIKRLVPKYSLPHAI 184
Cdd:PRK12583 101 NPAYRASELEYALGQSGVRWVICADAFKTSDYHAMLQELLPGLAEGQPGALACERLPELRG-VVSLAPAPPPGFLAWHEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 SMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVAN---VLQANGayaplLNDGKEFVVtALPLYH 261
Cdd:PRK12583 180 QARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNgyfVAESLG-----LTEHDRLCV-PVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 262 IFALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGG----MAV 337
Cdd:PRK12583 254 CFGMVLANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGapcpIEV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 QRAVADKwqnITKTRLLEGYGLTEASPLV--ACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVM 415
Cdd:PRK12583 334 MRRVMDE---MHMAEVQIAYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 416 LGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSG 495
Cdd:PRK12583 411 KGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYG 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 496 ELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:PRK12583 491 EEIVAWVRLHpGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREIS 550
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
27-556 |
2.72e-92 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 293.64 E-value: 2.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPA--FVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:PRK08315 20 QLLDRTAARYPDREAlvYRDQGLRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVV-----SNFASTLEQVV----DQTPvknviitglGDLLSAPKRTLVNfvVKYI--KR 173
Cdd:PRK08315 99 NPAYRLSELEYALNQSGCKALIAAdgfkdSDYVAMLYELApelaTCEP---------GQLQSARLPELRR--VIFLgdEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 174 LVPKYSLPHAISMRRALRAGKKAQyVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNvlqaNGAY-APLLNDGKE- 251
Cdd:PRK08315 168 HPGMLNFDELLALGRAVDDAELAA-RQATLDPDDPINIQYTSGTTGFPKGATLTHRNIL-N----NGYFiGEAMKLTEEd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 252 FVVTALPLYHIFALTVNCLLFLHKGANnllITNPrdIPGF--------VAELKktpFTALTGVNTLFNALVNSEEFAALD 323
Cdd:PRK08315 242 RLCIPVPLYHCFGMVLGNLACVTHGAT---MVYP--GEGFdplatlaaVEEER---CTALYGVPTMFIAELDHPDFARFD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 324 FSRLKLSIgggMA-------VQRAVADKW--QNITKtrlleGYGLTEASPlVACC-----PYDLAgyNGSIGLPAPSTQI 389
Cdd:PRK08315 314 LSSLRTGI---MAgspcpieVMKRVIDKMhmSEVTI-----AYGMTETSP-VSTQtrtddPLEKR--VTTVGRALPHLEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 390 Q-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFP 468
Cdd:PRK08315 383 KiVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 469 NEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILR 547
Cdd:PRK08315 463 REIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRpGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
....*....
gi 655376187 548 RELRDEAKS 556
Cdd:PRK08315 543 FKMREMMIE 551
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
23-554 |
1.13e-89 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 288.78 E-value: 1.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQPA---FVNMGA-----TLTYRKLEER-SRAfaAYLQNDLKLQKGDRVAIMMPNLLQYPIALFG 93
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPAlsfLLDADPldrpeTWTYAELLADvTRT--ANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 94 VLRAGmVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNF-----ASTLEQVVDQTP-VKNVIITGLGDLLSAPKRTLVNFV 167
Cdd:PRK07529 103 GEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiWQKVAEVLAALPeLRTVVEVDLARYLPGPKRLAVPLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 168 VKYIKRLVPKYSLPHAISMRRALRAGkkaqyvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANgayAPLLN 247
Cdd:PRK07529 182 RRKAHARILDFDAELARQPGDRLFSG-------RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGA---LLLGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 248 DGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITnP---RDiPGFVAELKKT----PFTALTGVNTLFNALVNSEeFA 320
Cdd:PRK07529 252 GPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAT-PqgyRG-PGVIANFWKIveryRINFLSGVPTVYAALLQVP-VD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 321 ALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQV--RGDDGQV 398
Cdd:PRK07529 329 GHDISSLRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGRY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 399 L---PQGETGELFAKGPQVMLGYwQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV 475
Cdd:PRK07529 409 LrdcAVDEVGVLCIAGPNVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 476 ALHPKVVEVAAVGVPHEVSGELVKIFV-VAKDKSLTEKELIKHCRHHLTG-YKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK07529 488 LRHPAVALAAAVGRPDAHAGELPVAYVqLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
.
gi 655376187 554 A 554
Cdd:PRK07529 568 A 568
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
18-488 |
1.05e-88 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 285.46 E-value: 1.05e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 18 DASRYASLLEMLESAVNTYADQPAFVNMGA----TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFG 93
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 94 VLRAGMVVVnvnPLY---TPRELKHQLVDSGAKaIVVVSNF--ASTLEQVVDQTP-VKNVIITGLGDLLSAPKrtlvnfv 167
Cdd:COG1022 85 ILAAGAVTV---PIYptsSAEEVAYILNDSGAK-VLFVEDQeqLDKLLEVRDELPsLRHIVVLDPRGLRDDPR------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 168 VKYIKRLVP---KYSLPHAISMRRALragkkaqyvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAp 244
Cdd:COG1022 154 LLSLDELLAlgrEVADPAELEARRAA------------VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 245 lLNDGKEFVVTaLPLYHIFALTVnCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTA--------LTGVNT-------- 308
Cdd:COG1022 221 -LGPGDRTLSF-LPLAHVFERTV-SYYALAAGATVAFAESPDTLAEDLREVKPTFMLAvprvwekvYAGIQAkaeeaggl 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 309 ---LFNALVNseefAALDFSRLKL---SIGGGMAVQRAVAD-----KWQNITKTRL------------------------ 353
Cdd:COG1022 298 krkLFRWALA----VGRRYARARLagkSPSLLLRLKHALADklvfsKLREALGGRLrfavsggaalgpelarffralgip 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 -LEGYGLTEASPLVACCPYDlaGYN-GSIGLPAPSTQIQVrgddgqvlpqGETGELFAKGPQVMLGYWQRPEETAKVIDK 431
Cdd:COG1022 374 vLEGYGLTETSPVITVNRPG--DNRiGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMI-LVSGFNVFPNEVEEVVALHPKVVEVAAVG 488
Cdd:COG1022 442 DGWLHTGDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-551 |
2.96e-88 |
|
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: 278.79 E-value: 2.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVvs 129
Cdd:cd05934 5 TYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 nfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvksdDIA 209
Cdd:cd05934 82 -----------------------------------------------------------------------------DPA 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 210 FLQYTGGTTGVSKGAMLSHgnivANVLQANGAYAPLLNDGKEFV-VTALPLYHIFALTVNCLLFLHKGANNLLItnPRDI 288
Cdd:cd05934 85 SILYTSGTTGPPKGVVITH----ANLTFAGYYSARRFGLGEDDVyLTVLPLFHINAQAVSVLAALSVGATLVLL--PRFS 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 289 P-GFVAELKKTPFTALTGVNTLFNALVNSEEFAalDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVA 367
Cdd:cd05934 159 AsRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP--DDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVI 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 368 CcPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAK---GPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMD 444
Cdd:cd05934 237 G-PRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRD 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 445 EKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLT 523
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPgETLDPEELFAFCEGQLA 394
|
490 500
....*....|....*....|....*...
gi 655376187 524 GYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-551 |
1.88e-87 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 279.95 E-value: 1.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKAIVVVSN-FASTLEQVVDQTP-VKNVIITGLG----DLLSA----PKRTLVNFVVkyikrlvp 176
Cdd:PRK06188 95 LGSLDDHAYVLEDAGISTLIVDPApFVERALALLARVPsLKHVLTLGPVpdgvDLLAAaakfGPAPLVAAAL-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 177 kyslphaismrralragkkaqyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVAnvlQANGAYAPL-LNDGKEFVVT 255
Cdd:PRK06188 167 ----------------------------PPDIAGLAYTGGTTGKPKGVMGTHRSIAT---MAQIQLAEWeWPADPRFLMC 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 256 AlPLYHIFALTVncLLFLHKGANNLLIT--NPRDIPGFVAELKKTpFTALtgVNTLFNALVNSEEFAALDFSRLKLSIGG 333
Cdd:PRK06188 216 T-PLSHAGGAFF--LPTLLRGGTVIVLAkfDPAEVLRAIEEQRIT-ATFL--VPTMIYALLDHPDLRTRDLSSLETVYYG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 334 GMAvqravadkwqnITKTRLLEG-----------YGLTEAsPLVAC-------CPYDlAGYNGSIGLPAPSTQIQVRGDD 395
Cdd:PRK06188 290 ASP-----------MSPVRLAEAierfgpifaqyYGQTEA-PMVITylrkrdhDPDD-PKRLTSCGRPTPGLRVALLDED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 396 GQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV 475
Cdd:PRK06188 357 GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVL 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 476 ALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK06188 436 AEHPAVAQVAVIGVPDEKWGEAVTAVVVLRpGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
35-551 |
7.74e-86 |
|
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: 275.02 E-value: 7.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 35 TYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELK 114
Cdd:cd05959 16 GRGDKTAFIDDAGSLTYAELEAEARRVAGALRA-LGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 115 HQLVDSGAKAIVVVSNFASTLEQVV--DQTPVKNVIITGlgdllsapkrtlvnfvvkyikrlvPKYSLPHAISMRRALRA 192
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAALtkSEHTLVVLIVSG------------------------GAGPEAGALLLAELVAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 193 GkkAQYVKPVVKS-DDIAFLQYTGGTTGVSKGAMLSHGNI-VANVLQANGAYAPLLNDgkeFVVTALPLYHIFALTvNCL 270
Cdd:cd05959 151 E--AEQLKPAATHaDDPAFWLYSSGSTGRPKGVVHLHADIyWTAELYARNVLGIREDD---VCFSAAKLFFAYGLG-NSL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 LF-LHKGANNLLITNpRDIPGFVAELKKT--PfTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN 347
Cdd:cd05959 225 TFpLSVGATTVLMPE-RPTPAAVFKRIRRyrP-TVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITKTRLLEGYGLTEA-----SPLVACCPYdlagynGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRP 422
Cdd:cd05959 303 RFGLDILDGIGSTEMlhiflSNRPGRVRY------GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 423 EETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV 502
Cdd:cd05959 377 DKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFV 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 655376187 503 V----AKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05959 456 VlrpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-552 |
4.18e-82 |
|
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: 263.38 E-value: 4.18e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVvvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd05941 81 TDSEPSLVL----------------------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksdDIAFLQYTGGTTGVSKGAMLSHGNIVANV--LQANGAYAPllndgKEFVVTALPLYHIFAL--TVNCLLFl 273
Cdd:cd05941 90 ---------DPALILYTSGTTGRPKGVVLTHANLAANVraLVDAWRWTE-----DDVLLHVLPLHHVHGLvnALLCPLF- 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 hkgANNLLITNPRDIPGFVAELKKTP-FTALTGVNTLFNALVNSEEFAALD--------FSRLKLSIGGGMAVQRAVADK 344
Cdd:cd05941 155 ---AGASVEFLPKFDPKEVAISRLMPsITVFMGVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVPTLEE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 345 WQNITKTRLLEGYGLTEASpLVACCPYDLAGYNGSIGLPAPSTQIQVRGDD-GQVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:cd05941 232 WEAITGHTLLERYGMTEIG-MALSNPLDGERRPGTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVS-GFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV 502
Cdd:cd05941 311 ATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSgGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVV 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 655376187 503 VAKD--KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05941 391 VLRAgaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-551 |
3.52e-81 |
|
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: 257.98 E-value: 3.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANvlqanGAYAPLLNDGKEFVVTAL--PLYHIFALTVNCLLFLHKGANNLLIT 283
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNN-----GYFIGERLGLTEQDRLCIpvPLFHCFGSVLGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 284 NPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN-ITKTRLLEGYGLTEA 362
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEvMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVACC----PYDLAgYNgSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLAT 437
Cdd:cd05917 157 SPVSTQTrtddSIEKR-VN-TVGRIMPHTEAKiVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 438 GDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIK 516
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEgAELTEEDIKA 314
|
330 340 350
....*....|....*....|....*....|....*
gi 655376187 517 HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05917 315 YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
49-552 |
9.83e-81 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 259.19 E-value: 9.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVv 128
Cdd:cd05972 1 WSFRELKRESAKAANVLA-KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 snfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvKSDDI 208
Cdd:cd05972 79 ---------------------------------------------------------------------------DAEDP 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVANVLQAngAYAPLLNDGKEFVVTALP------LYHIFA-LTVNCLLFLHKGannll 281
Cdd:cd05972 84 ALIYFTSGTTGLPKGVLHTHSYPLGHIPTA--AYWLGLRPDDIHWNIADPgwakgaWSSFFGpWLLGATVFVYEG----- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 itnprdiPGFVAE-----LKKTPFTALTGVNTLFNALVnSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEG 356
Cdd:cd05972 157 -------PRFDAErilelLERYGVTSFCGPPTAYRMLI-KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDG 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTEASPLVACCPyDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAK--GPQVMLGYWQRPEETAKVIdKDGW 434
Cdd:cd05972 229 YGQTETGLTVGNFP-DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEEGDIAIKlpPPGLFLGYVGDPEKTEASI-RGDY 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 435 LATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-----KSL 509
Cdd:cd05972 307 YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSgyepsEEL 386
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 655376187 510 TEkELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05972 387 AE-ELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
36-551 |
4.31e-78 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 255.68 E-value: 4.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 36 YADQPAFVN--MGATLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPREL 113
Cdd:PLN02246 36 FSDRPCLIDgaTGRVYTYADVELLSRRVAAGL-HKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 114 KHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGlgdllsaPKRTLVNFvvkyikrlvpkyslphaismrRALRAG 193
Cdd:PLN02246 115 AKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDD-------PPEGCLHF---------------------SELTQA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 194 KKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVV-TALPLYHIFALtvNCLLF 272
Cdd:PLN02246 167 DENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVIlCVLPMFHIYSL--NSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 273 --LHKGANnLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGG----GMAVQRAVADKWQ 346
Cdd:PLN02246 245 cgLRVGAA-ILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGaaplGKELEDAFRAKLP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NitkTRLLEGYGLTEASPLVACC------PYDLAgyNGSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYW 419
Cdd:PLN02246 324 N---AVLGQGYGMTEAGPVLAMClafakePFPVK--SGSCGTVVRNAELKiVDPETGASLPRNQPGEICIRGPQIMKGYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 420 QRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVK 499
Cdd:PLN02246 399 NDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPV 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 655376187 500 IFVV-AKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PLN02246 479 AFVVrSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
46-556 |
8.21e-77 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 251.33 E-value: 8.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMM----PNLLQYpialFGVLRAGMVVVNVNPLYTPRELKHQLVDSG 121
Cdd:PRK07514 26 GLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVekspEALALY----LATLRAGAVFLPLNTAYTLAELDYFIGDAE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 122 AKAIVVVSNFASTLEQVVDQTPVKNViiTGLGDLLSApkrtlvnfvvkyikrlvpkySLphaisMRRAlrAGKKAQYVKP 201
Cdd:PRK07514 101 PALVVCDPANFAWLSKIAAAAGAPHV--ETLDADGTG--------------------SL-----LEAA--AAAPDDFETV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 202 VVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvlqangayAPLLND-----GKEFVVTALPLYHIFALTV--NCLLFlh 274
Cdd:PRK07514 152 PRGADDLAAILYTSGTTGRSKGAMLSHGNLLSN--------ALTLVDywrftPDDVLIHALPIFHTHGLFVatNVALL-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 275 KGANnlLITNPRDIPGFVAELKKTPfTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLL 354
Cdd:PRK07514 222 AGAS--MIFLPKFDPDAVLALMPRA-TVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 355 EGYGLTEASPLVACcPYDLAGYNGSIGLPAPSTQIQVRG-DDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDG 433
Cdd:PRK07514 299 ERYGMTETNMNTSN-PYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 434 WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEK 512
Cdd:PRK07514 378 FFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKpGAALDEA 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 655376187 513 ELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKS 556
Cdd:PRK07514 458 AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYAD 501
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
46-552 |
1.92e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 250.21 E-value: 1.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNFASTLEQVVDQTPvknviitglgdlLSAPKRTLVNFVVKYIKRLvpkyslphaismrRALRAGKKAQYVKPVVKS 205
Cdd:PRK08276 88 IVSAALADTAAELAAELP------------AGVPLLLVVAGPVPGFRSY-------------EEALAAQPDTPIADETAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDiafLQYTGGTTGVSKGAM--LSHGNI--VANVLQANGAYAPLLNDGKEFVVTAlPLYH----IFALTVncllflHKGA 277
Cdd:PRK08276 143 AD---MLYSSGTTGRPKGIKrpLPGLDPdeAPGMMLALLGFGMYGGPDSVYLSPA-PLYHtaplRFGMSA------LALG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVN-SEEF-AALDFSRLKLSIGGG----MAVQRAVADKWQNItkt 351
Cdd:PRK08276 213 GTVVVMEKFDAEEALALIERYRVTHSQLVPTMFVRMLKlPEEVrARYDVSSLRVAIHAAapcpVEVKRAMIDWWGPI--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 rLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPStQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDK 431
Cdd:PRK08276 290 -IHEYYASSEGGGVTVITSEDWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV-----VAKD 506
Cdd:PRK08276 368 HGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadgADAG 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 507 KSLTEkELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK08276 448 DALAA-ELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRD 492
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
19-553 |
2.22e-76 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 251.11 E-value: 2.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 19 ASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAG 98
Cdd:PRK07470 3 SRRVMNLAHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 99 MVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTP-VKNVIITGLGdllsapkrtlvnfvvkyikRLVPK 177
Cdd:PRK07470 82 AVWVPTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPdLTHVVAIGGA-------------------RAGLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 178 YSlphAISMRRALRAGKKAQyvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGN---IVANVLqangayAPLLNDGKEF-- 252
Cdd:PRK07470 143 YE---ALVARHLGARVANAA-----VDHDDPCWFFFTSGTTGRPKAAVLTHGQmafVITNHL------ADLMPGTTEQda 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 253 -VVTAlPLYHifALTVNCLLFLHKGANNLLITNPR-DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLS 330
Cdd:PRK07470 209 sLVVA-PLSH--GAGIHQLCQVARGAATVLLPSERfDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 331 IGGGMAVQRAvaDKWQNITK--TRLLEGYGLTEASPLVACCPYDL-------AGYNGSIGLPAPSTQIQVRGDDGQVLPQ 401
Cdd:PRK07470 286 IYAGAPMYRA--DQKRALAKlgKVLVQYFGLGEVTGNITVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 402 GETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKV 481
Cdd:PRK07470 364 GETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAV 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 482 VEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK07470 443 SEVAVLGVPDPVWGEVGVAVCVARDgAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
60-551 |
5.23e-75 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 245.43 E-value: 5.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 60 AFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAG----MVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTL 135
Cdd:cd05922 4 SAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 136 EQVVDQTPVKNVIITGlgdllsapkrtlvnfvvkyikrlvpkyslpHAISMRRALRAGKkaqyvkpVVKSDDIAFLQYTG 215
Cdd:cd05922 84 RDALPASPDPGTVLDA------------------------------DGIRAARASAPAH-------EVSHEDLALLLYTS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 216 GTTGVSKGAMLSHGNIVANvlqANGAYAPLLNDGKEFVVTALPLYHIFALTVnCLLFLHKGANnlLITNPRDIP--GFVA 293
Cdd:cd05922 127 GSTGSPKLVRLSHQNLLAN---ARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGAT--LVLTNDGVLddAFWE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 294 ELKKTPFTALTGVNTLFNALvnseefAALDFSRLKL-------SIGGGM--AVQRAVADKWQNitkTRLLEGYGLTEASP 364
Cdd:cd05922 201 DLREHGATGLAGVPSTYAML------TRLGFDPAKLpslryltQAGGRLpqETIARLRELLPG---AQVYVMYGQTEATR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 365 LVACCPYDLAGYN-GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYM 443
Cdd:cd05922 272 RMTYLPPERILEKpGSIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 444 DEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPhEVSGELVKIFVVAKDKsLTEKELIKHCRHHLT 523
Cdd:cd05922 352 DEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLP-DPLGEKLALFVTAPDK-IDPKDVLRSLAERLP 429
|
490 500
....*....|....*....|....*...
gi 655376187 524 GYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05922 430 PYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-552 |
1.42e-73 |
|
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: 243.31 E-value: 1.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS 129
Cdd:cd12119 27 TYAEVAERARRLANALR-RLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 NFASTLEQVVDQTPVKNVIITGLGDLLSAPKRTlvNFVVKYikrlvpkyslphaismrRALRAGKKAQYVKPVVKSDDIA 209
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDDAAMPEPAG--VGVLAY-----------------EELLAAESPEYDWPDFDENTAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 210 FLQYTGGTTGVSKGAMLSHGnivANVLQANGAyapLLNDG-----KEFVVTALPLYHIFA--LTVNCLLFlhkGANnLLI 282
Cdd:cd12119 167 AICYTSGTTGNPKGVVYSHR---SLVLHAMAA---LLTDGlglseSDVVLPVVPMFHVNAwgLPYAAAMV---GAK-LVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNPRDIPGFVAELKKT---PFTAltGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITkTRLLEGYGL 359
Cdd:cd12119 237 PGPYLDPASLAELIERegvTFAA--GVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERG-VRVIHAWGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 360 TEASPLVACC--PYDLAG--------YNGSIGLPAPSTQIQVRGDDGQVLPQ-GET-GELFAKGPQVMLGYWQRPEETAK 427
Cdd:cd12119 314 TETSPLGTVArpPSEHSNlsedeqlaLRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 428 vIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD- 506
Cdd:cd12119 394 -LTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEg 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 507 KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd12119 473 ATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-551 |
2.65e-73 |
|
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: 240.36 E-value: 2.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVV 127
Cdd:cd05903 1 RLTYSELDTRADRLAAGL-AALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 VSNFASTleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvKPVVKSDD 207
Cdd:cd05903 80 PERFRQF-----------------------------------------------------------------DPAAMPDA 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTGVSKGAMLSHGNIVANVLQangaYAPLLNDGKEFVV-TALPLYHI--FALTVNCLLFLHKGANNLLITN 284
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQ----YAERLGLGPGDVFlVASPMAHQtgFVYGFTLPLLLGAPVVLQDIWD 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 285 PRDIpgfVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASP 364
Cdd:cd05903 171 PDKA---LALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 365 LVACCPYDLAGYN-GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEeTAKVIDKDGWLATGDIGYM 443
Cdd:cd05903 248 AVTSITPAPEDRRlYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPD-LTADAAPEGWFRTGDLARL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 444 DEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHC-RHH 521
Cdd:cd05903 327 DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSgALLTFDELVAYLdRQG 406
|
490 500 510
....*....|....*....|....*....|
gi 655376187 522 LTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05903 407 VAKQYWPERLVHVDDLPRTPSGKVQKFRLR 436
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
3-555 |
3.79e-73 |
|
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: 242.36 E-value: 3.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 3 QPWinslPADVpaeidASRY--------ASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKG 74
Cdd:COG1021 6 TPW----PEEF-----AARYreagywrgETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLL-ALGLRPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 75 DRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS-----NFASTLEQVVDQTP-VKNVI 148
Cdd:COG1021 76 DRVVVQLPNVAEFVIVFFALFRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVPsLRHVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 149 ITG-------LGDLLSAPkrtlvnfvvkyikrlvpkyslphaismrralragkkAQYVKPVVKSDDIAFLQYTGGTTGVS 221
Cdd:COG1021 156 VVGdageftsLDALLAAP------------------------------------ADLSEPRPDPDDVAFFQLSGGTTGLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 222 KGAMLSHGNIVANVLQANGAYAplLNDGKEFVVtALPLYHIFALTVNCLL-FLHKGANNLLITNPRDIPGF--VAELKKT 298
Cdd:COG1021 200 KLIPRTHDDYLYSVRASAEICG--LDADTVYLA-ALPAAHNFPLSSPGVLgVLYAGGTVVLAPDPSPDTAFplIERERVT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 299 pFTALtgVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKwqnITKT---RLLEGYGLTEAspLVACC----PY 371
Cdd:COG1021 277 -VTAL--VPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARR---VRPAlgcTLQQVFGMAEG--LVNYTrlddPE 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 372 DLAgyNGSIGLP-APSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFY 450
Cdd:COG1021 349 EVI--LTTQGRPiSPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLV 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 451 IVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCR-HHLTGYKVPK 529
Cdd:COG1021 427 VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLReRGLAAFKLPD 506
|
570 580
....*....|....*....|....*.
gi 655376187 530 LVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:COG1021 507 RLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
38-553 |
1.99e-71 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 236.78 E-value: 1.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAA-LGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFAStlEQVVDQtPVKnviitgLGDLLSAPKRtlvnfvvkyIKRLVPKYSLphaismrralragkkaq 197
Cdd:PRK03640 96 DDAEVKCLITDDDFEA--KLIPGI-SVK------FAELMNGPKE---------EAEIQEEFDL----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANvlqangAYAPLLNDG---KEFVVTALPLYHIFALTV------- 267
Cdd:PRK03640 141 --------DEVATIMYTSGTTGKPKGVIQTYGNHWWS------AVGSALNLGlteDDCWLAAVPIFHISGLSIlmrsviy 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 268 NCLLFLH-----KGANNLLITnpRDIpgfvaelkktpfTALTGVNTLFNALVnseefAALDFSRLKLSI-----GGGMA- 336
Cdd:PRK03640 207 GMRVVLVekfdaEKINKLLQT--GGV------------TIISVVSTMLQRLL-----ERLGEGTYPSSFrcmllGGGPAp 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 337 ---VQRAVAdkwQNITktrLLEGYGLTE-ASPLVACCPYDLAGYNGSIGLPAPSTQIQVRgDDGQVLPQGETGELFAKGP 412
Cdd:PRK03640 268 kplLEQCKE---KGIP---VYQSYGMTEtASQIVTLSPEDALTKLGSAGKPLFPCELKIE-KDGVVVPPFEEGEIVVKGP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 413 QVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHE 492
Cdd:PRK03640 341 NVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDD 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 493 VSGELVKIFVVaKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK03640 420 KWGQVPVAFVV-KSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
35-552 |
2.70e-71 |
|
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: 237.91 E-value: 2.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 35 TYADQPAFVnmGATLTYRKLEERSRAFAAYLQNDLKlqKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYTPRELK 114
Cdd:cd05931 13 TFLDDEGGR--EETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAV---PLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 115 HQ------LVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKRtlvnfvvkyikrlvpkyslphaismrr 188
Cdd:cd05931 86 HAerlaaiLADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSA--------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 189 alragkkAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGkefVVTALPLYHIFALTVN 268
Cdd:cd05931 139 -------ADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDV---VVSWLPLYHDMGLIGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 CLLFLHKGANNLLITnPRDipgFVAE----LK-----KTPFTAltGVNtlFnAL------VNSEEFAALDFSRLKLSIGG 333
Cdd:cd05931 209 LLTPLYSGGPSVLMS-PAA---FLRRplrwLRlisryRATISA--APN--F-AYdlcvrrVRDEDLEGLDLSSWRVALNG 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 334 GMAVQRAVADKWQ------NITKTRLLEGYGLTEASPLVACCP---------YDLAGYNG----------------SIGL 382
Cdd:cd05931 280 AEPVRPATLRRFAeafapfGFRPEAFRPSYGLAEATLFVSGGPpgtgpvvlrVDRDALAGravavaaddpaarelvSCGR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 383 PAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKV------IDKDGWLATGDIGYMDEkGFFYIVDRK 455
Cdd:cd05931 360 PLPDQEVRiVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAETfgalaaTDEGGWLRTGDLGFLHD-GELYITGRL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 456 KDMILVSGFNVFPNEVEEVVALHPKVVE---VAAVGVPHEVSGELVKIFVVAKDK-SLTEKELIKHCR------HHLTGY 525
Cdd:cd05931 439 KDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGAdPADLAAIAAAIRaavareHGVAPA 518
|
570 580
....*....|....*....|....*..
gi 655376187 526 KVpKLVEfRDELPKTNVGKILRRELRD 552
Cdd:cd05931 519 DV-VLVR-PGSIPRTSSGKIQRRACRA 543
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
23-553 |
2.72e-71 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 238.11 E-value: 2.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQPAFV-NMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVV 101
Cdd:PRK06087 23 ASLADYWQQTARAMPDKIAVVdNHGASYTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 102 VNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTleqvvdqTPVKnvIITGLGDLLSAPKRTLVnfvvkyIKRLVPKYSlp 181
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQAKMFFAPTLFKQT-------RPVD--LILPLQNQLPQLQQIVG------VDKLAPATS-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 182 hAISMRRALRAGKKAQYvKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVAnvlqANGAYAPLLNDGKEFVV-TALPLY 260
Cdd:PRK06087 165 -SLSLSQIIADYEPLTT-AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILA----SERAYCARLNLTWQDVFmMPAPLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 261 HIFAltvncllFLHKgannllITNPRDIPGFVAELKK-TPFTALTGVN----------TLF-NALVNSEEFAALDFSRLK 328
Cdd:PRK06087 239 HATG-------FLHG------VTAPFLIGARSVLLDIfTPDACLALLEqqrctcmlgaTPFiYDLLNLLEKQPADLSALR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 329 LSIGGGMAV-QRAVADKWQNITKtrLLEGYGLTEASPLVACCPYDLAGYNGSI-GLPAPSTQIQVRGDDGQVLPQGETGE 406
Cdd:PRK06087 306 FFLCGGTTIpKKVARECQQRGIK--LLSVYGSTESSPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 407 LFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAA 486
Cdd:PRK06087 384 EASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 487 VGVPHEVSGELVKIFVVAKD--KSLTEKELIKH-CRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK06087 464 VAMPDERLGERSCAYVVLKAphHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
23-553 |
5.81e-71 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 237.18 E-value: 5.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQPAFVN--MGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMV 100
Cdd:PLN02330 28 LTLPDFVLQDAELYADKVAFVEavTGKAVTYGEVVRDTRRFAKALRS-LGLRKGQVVVVVLPNVAEYGIVALGIMAAGGV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 101 VVNVNPLYTPRELKHQLVDSGAKAIVV-VSNFAStleqvvdqtpVKN----VIITGlgdllsapkrtlvnfvvkyikrlv 175
Cdd:PLN02330 107 FSGANPTALESEIKKQAEAAGAKLIVTnDTNYGK----------VKGlglpVIVLG------------------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 176 pKYSLPHAISMRRALRAGKKA--QYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAngayapLLNDGKEFV 253
Cdd:PLN02330 153 -EEKIEGAVNWKELLEAADRAgdTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSS------LFSVGPEMI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 254 --VTAL---PLYHIFALTVNCLLFLhKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLK 328
Cdd:PLN02330 226 gqVVTLgliPFFHIYGITGICCATL-RNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 329 L-SIGGGMA-----VQRAVADKWQNItktRLLEGYGLTEAS--PLVACCP---YDLAGYNgSIGLPAPSTQIQ-VRGDDG 396
Cdd:PLN02330 305 LqAIMTAAAplapeLLTAFEAKFPGV---QVQEAYGLTEHSciTLTHGDPekgHGIAKKN-SVGFILPNLEVKfIDPDTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 397 QVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PLN02330 381 RSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILL 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 477 LHPKVVEVAAVGVPHEVSGEL-VKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PLN02330 461 THPSVEDAAVVPLPDEEAGEIpAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
38-553 |
3.53e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 233.62 E-value: 3.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK06145 17 DRAALVYRDQEISYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDQtpvknvIITGlgdllsapkrtlvnfvvkyikrlvpkyslPHAISMRRALRAGKKAQ 197
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPK------IVID-----------------------------AAAQADSRRLAQGGLEI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 YVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApLLNDGKEFVVTalPLYHIFALTVNCLLFLHKGA 277
Cdd:PRK06145 141 PPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALG-LTASERLLVVG--PLYHVGAFDLPGIAVLWVGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NnLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAV-QRAVADKWQNITKTRLLEG 356
Cdd:PRK06145 218 T-LRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRARYIDA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTEAsplvacCPYDL---AGYN----GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI 429
Cdd:PRK06145 297 YGLTET------CSGDTlmeAGREiekiGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 dKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGE-LVKIFVVAKDKS 508
Cdd:PRK06145 371 -YGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGErITAVVVLNPGAT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 655376187 509 LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:PRK06145 450 LTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
207-547 |
1.35e-69 |
|
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: 227.00 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVAnVLQANGAYAPLLNDGKEFVVTalPLYHIFALTVNCLLFLHKGANnLLITNPR 286
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLR-AAAAWADCADLTEDDRYLIIN--PFFHTFGYKAGIVACLLTGAT-VVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN-ITKTRLLEGYGLTEASPL 365
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSeLGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 366 VACCPYDLA-GYNGSIGLPAPSTQIQVrGDDGQVLpqgetgelfAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMD 444
Cdd:cd17638 157 TMCRPGDDAeTVATTCGRACPGFEVRI-ADDGEVL---------VRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 445 EKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLT 523
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPgVTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 655376187 524 GYKVPKLVEFRDELPKTNVGKILR 547
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
46-552 |
2.75e-69 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 233.20 E-value: 2.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVD-SGAKA 124
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDcSVGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 125 IVVVSNfastleqvVDQTPVKNVIITGLGDllsapkrtlvNFVVKYIKRLVPKYslphaismrRALRAGKKAQYVKPVVK 204
Cdd:PLN02574 144 FTSPEN--------VEKLSPLGVPVIGVPE----------NYDFDSKRIEFPKF---------YELIKEDFDFVPKPVIK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 SDDIAFLQYTGGTTGVSKGAMLSHGNIVANV-----LQANGAYAPllndGKEFV-VTALPLYHIFALTVNCLLFLHKGAN 278
Cdd:PLN02574 197 QDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelfvrFEASQYEYP----GSDNVyLAALPMFHIYGLSLFVVGLLSLGST 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 279 nLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEE-FAALDFSRLKL-SIGGGMAVQRAVADKWQNITKTRLLEG 356
Cdd:PLN02574 273 -IVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQvSCGAAPLSGKFIQDFVQTLPHVDFIQG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTEASPLvaccpyDLAGYN-------GSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKV 428
Cdd:PLN02574 352 YGMTESTAV------GTRGFNteklskySSVGLLAPNMQAKvVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQST 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 429 IDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKS 508
Cdd:PLN02574 426 IDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGS 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 655376187 509 -LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PLN02574 506 tLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKR 550
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
33-552 |
7.30e-69 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 230.73 E-value: 7.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 33 VNTYADQPAFV--NMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTP 110
Cdd:PRK13391 7 AQTTPDKPAVImaSTGEVVTYRELDERSNRLAHLFR-SLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 111 RELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPvknviitglgdllsapkRTLVNFVVKYIKRLVPKYSLPHAIsmrral 190
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALLKQCP-----------------GVRHRLVLDGDGELEGFVGYAEAV------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 191 rAGKKAQYVKPVVKSDDiafLQYTGGTTGVSKG--AMLSHGNIVanvlQANGAYAPLLN-----DGKEFVVTAlPLYHIf 263
Cdd:PRK13391 143 -AGLPATPIADESLGTD---MLYSSGTTGRPKGikRPLPEQPPD----TPLPLTAFLQRlwgfrSDMVYLSPA-PLYHS- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 264 ALTVNCLLFLHKGANNLLITNpRDIPGFVAELKKTPFTALTGVNTLFNALVN--SEEFAALDFSRLKLSIGGG----MAV 337
Cdd:PRK13391 213 APQRAVMLVIRLGGTVIVMEH-FDAEQYLALIEEYGVTHTQLVPTMFSRMLKlpEEVRDKYDLSSLEVAIHAAapcpPQV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 QRAVADKWQNItktrLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTqIQVRGDDGQVLPQGETGELFAKGPQvMLG 417
Cdd:PRK13391 292 KEQMIDWWGPI----IHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGR-PFE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YWQRPEETAKVIDKDG-WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGE 496
Cdd:PRK13391 366 YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGE 445
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 497 LVKIFV-----VAKDKSLTEkELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK13391 446 EVKAVVqpvdgVDPGPALAA-ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-551 |
1.31e-68 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 227.73 E-value: 1.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 39 QPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLV 118
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRN-LGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 119 DSGAkaivvvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikRLVpkyslphaismrralragkkaqy 198
Cdd:cd05919 80 DCEA--------------------------------------------------RLV----------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 199 vkpVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVanvLQANGAYAPLLNDGKEFVVTALP-LYHIFALTvNCLLF-LHKG 276
Cdd:cd05919 87 ---VTSADDIAYLLYSSGTTGPPKGVMHAHRDPL---LFADAMAREALGLTPGDRVFSSAkMFFGYGLG-NSLWFpLAVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEG 356
Cdd:cd05919 160 ASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDG 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTEASPLVACCPYDLAGYnGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLA 436
Cdd:cd05919 240 IGATEVGHIFLSNRPGAWRL-GSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-NGGWYR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 437 TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIK 516
Cdd:cd05919 318 TGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLAR 397
|
490 500 510
....*....|....*....|....*....|....*....
gi 655376187 517 ----HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05919 398 dihrHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
38-551 |
1.32e-68 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 230.82 E-value: 1.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK07786 32 DAPALRFLGNTTTWRELDDRVAALAGAL-SRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGdllsAPKRTLVNFvvkyiKRLVPKYSLPHAismrralragkkaq 197
Cdd:PRK07786 111 SDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGG----SSDDSVLGY-----EDLLAEAGPAHA-------------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkPV-VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVvtALPLYHIFALTvNCLLFLHKG 276
Cdd:PRK07786 168 ---PVdIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFV--GVPLFHIAGIG-SMLPGLLLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANNLLI-TNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMA---VQRAVADKWqniTKTR 352
Cdd:PRK07786 242 APTVIYpLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPAsdtLLRQMAATF---PEAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPlVACCpydLAGYN-----GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK 427
Cdd:PRK07786 319 ILAAFGQTEMSP-VTCM---LLGEDairklGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 428 VIDkDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGElVKIFVVA--- 504
Cdd:PRK07786 395 AFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGE-VPVAVAAvrn 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 655376187 505 KDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK07786 473 DDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
46-554 |
1.86e-67 |
|
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: 226.44 E-value: 1.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNDLKlqKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05909 5 GTSLTYRKLLTGAIALARKLAKMTK--EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNFASTLEQVVDQTPVKNVIITGLGDLlsapkRTLVNFVVKYIKRLvpKYSLPHAISMRRALRAGkkaqyvkpvVKS 205
Cdd:cd05909 83 LTSKQFIEKLKLHHLFDVEYDARIVYLEDL-----RAKISKADKCKAFL--AGKFPPKWLLRIFGVAP---------VQP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkeFVVTALPLYHIFALTVNCLLFLHKGANNLLITNP 285
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPED---VVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 RDIPGFVAELKKTPFTALTGVNTLFNALVNSEEfaALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPL 365
Cdd:cd05909 224 LDYKKIPELIYDKKATILLGTPTFLRGYARAAH--PEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 366 VACCPYDLAGYNGSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMD 444
Cdd:cd05909 302 ISVNTPQSPNKEGTVGRPLPGMEVKiVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKID 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 445 EKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALH-PKVVEVAAVGVPHEVSGElvKIFVVAKDKSLTEKELIKHCRHH-L 522
Cdd:cd05909 381 GEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE--KIVLLTTTTDTDPSSLNDILKNAgI 458
|
490 500 510
....*....|....*....|....*....|..
gi 655376187 523 TGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:cd05909 459 SNLAKPSYIHQVEEIPLLGTGKPDYVTLKALA 490
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
22-552 |
2.50e-67 |
|
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: 226.03 E-value: 2.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 22 YASL--LEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGM 99
Cdd:cd12118 1 YVPLtpLSFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALA-ALGISRGDTVAVLAPNTPAMYELHFGVPMAGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 100 VVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTleqvvdqtpvknviitglgDLLSAPKRTlvnfvvkyikrlvpkys 179
Cdd:cd12118 80 VLNALNTRLDAEEIAFILRHSEAKVLFVDREFEYE-------------------DLLAEGDPD----------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 180 lphaismrralragkkAQYVKPVVKSDDIAfLQYTGGTTGVSKGAMLSH--------GNIVANVLQANGAYapllndgke 251
Cdd:cd12118 124 ----------------FEWIPPADEWDPIA-LNYTSGTTGRPKGVVYHHrgaylnalANILEWEMKQHPVY--------- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 252 fvVTALPLYH---------IFAL--TVNCLlflhkgannllitnpRDI--PGFVAELKKTPFTALTGVNTLFNALVNSEE 318
Cdd:cd12118 178 --LWTLPMFHcngwcfpwtVAAVggTNVCL---------------RKVdaKAIYDLIEKHKVTHFCGAPTVLNMLANAPP 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 319 FAALDFSRLKLSIGGGMAVQRAVADKWQNItKTRLLEGYGLTEASPLVACCPY----------DLAGYNGSIGLPAPS-T 387
Cdd:cd12118 241 SDARPLPHRVHVMTAGAPPPAAVLAKMEEL-GFDVTHVYGLTETYGPATVCAWkpewdelpteERARLKARQGVRYVGlE 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 388 QIQVRGDDGQ--VLPQGET-GELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGF 464
Cdd:cd12118 320 EVDVLDPETMkpVPRDGKTiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGE 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 465 NVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRdELPKTNVG 543
Cdd:cd12118 399 NISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEgAKVTEEEIIAFCREHLAGFMVPKTVVFG-ELPKTSTG 477
|
....*....
gi 655376187 544 KILRRELRD 552
Cdd:cd12118 478 KIQKFVLRD 486
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
48-488 |
4.03e-67 |
|
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: 224.40 E-value: 4.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLY---TPRELKHQLVDSGAKA 124
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPV---PIYptsSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 125 IVVvsnfastleqvvdqtpvknviitglgdllSAPkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvk 204
Cdd:cd05907 81 LFV-----------------------------EDP--------------------------------------------- 86
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 sDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPllnDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITN 284
Cdd:cd05907 87 -DDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA---TEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASS 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 285 PRDIPGFVAELKKTPFTALTGV-NTLFNALVNSEE-------FAALDFSRLKLSIGGGMAVQRAVADKWQ--NITktrLL 354
Cdd:cd05907 163 AETLLDDLSEVRPTVFLAVPRVwEKVYAAIKVKAVpglkrklFDLAVGGRLRFAASGGAPLPAELLHFFRalGIP---VY 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 355 EGYGLTEASPLVACCPYDlAGYNGSIGLPAPSTQIQVrgddgqvlpqGETGELFAKGPQVMLGYWQRPEETAKVIDKDGW 434
Cdd:cd05907 240 EGYGLTETSAVVTLNPPG-DNRIGTVGKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 435 LATGDIGYMDEKGFFYIVDRKKDMILVS-GFNVFPNEVEEVVALHPKVVEVAAVG 488
Cdd:cd05907 309 LHTGDLGEIDEDGFLHITGRKKDLIITSgGKNISPEPIENALKASPLISQAVVIG 363
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
48-551 |
5.53e-67 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 225.72 E-value: 5.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKL-EERSRAfaAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:PRK08008 37 RYSYLELnEEINRT--ANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNFASTLEQV--VDQTPVKNVIITGLGDllsapkrtlvnfvvkyikrlvPKYSLPHAISMRRALRAGKKAQyvKPVVK 204
Cdd:PRK08008 115 TSAQFYPMYRQIqqEDATPLRHICLTRVAL---------------------PADDGVSSFTQLKAQQPATLCY--APPLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 SDDIAFLQYTGGTTGVSKGAMLSHGNivanvLQANGAYAP----LLNDgkEFVVTALPLYHIfaltvNCLLflhkgannl 280
Cdd:PRK08008 172 TDDTAEILFTSGTTSRPKGVVITHYN-----LRFAGYYSAwqcaLRDD--DVYLTVMPAFHI-----DCQC--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 281 litnprdipgfvaelkktpfTALTGVNTLFNALVNSEEFAALDF----SRLKLSIGGGMA-------VQRAVADKWQ--- 346
Cdd:PRK08008 231 --------------------TAAMAAFSAGATFVLLEKYSARAFwgqvCKYRATITECIPmmirtlmVQPPSANDRQhcl 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 -------NIT-----------KTRLLEGYGLTEA-SPLVACCPYDLAGYNgSIGLPAPSTQIQVRGDDGQVLPQGETGEL 407
Cdd:PRK08008 291 revmfylNLSdqekdafeerfGVRLLTSYGMTETiVGIIGDRPGDKRRWP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 408 FAKG---PQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEV 484
Cdd:PRK08008 370 CIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDI 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 485 AAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK08008 450 VVVGIKDSIRDEAIKAFVVLNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
48-552 |
9.32e-67 |
|
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: 222.22 E-value: 9.32e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGakaivv 127
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAA-LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 vsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvVKSDD 207
Cdd:cd05912 74 ---------------------------------------------------------------------------VKLDD 78
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTGVSKGAMLSHGNIVANvlqangAYAPLLNDG---KEFVVTALPLYHIFALTV-------NCLLFLHKGA 277
Cdd:cd05912 79 IATIMYTSGTTGKPKGVQQTFGNHWWS------AIGSALNLGlteDDNWLCALPLFHISGLSIlmrsviyGMTVYLVDKF 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNLLITNprdipgfvaELKKTPFTALTGVNTLFNALVnsEEFAALDFSRLKLSI-GGGMAVQRAVAD-KWQNITktrLLE 355
Cdd:cd05912 153 DAEQVLH---------LINSGKVTIISVVPTMLQRLL--EILGEGYPNNLRCILlGGGPAPKPLLEQcKEKGIP---VYQ 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 356 GYGLTE-ASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGqvlPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGW 434
Cdd:cd05912 219 SYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGW 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 435 LATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAkDKSLTEKEL 514
Cdd:cd05912 295 FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVS-ERPISEEEL 373
|
490 500 510
....*....|....*....|....*....|....*...
gi 655376187 515 IKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05912 374 IAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
50-553 |
1.80e-65 |
|
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: 222.34 E-value: 1.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS 129
Cdd:cd05928 43 SFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 NFASTLEQVVDQTPvknviitglgDLlsapkrtlvnfvvkYIKRLVPKYSLPHAISMRRALR-AGKKAQYVKpvVKSDDI 208
Cdd:cd05928 123 ELAPEVDSVASECP----------SL--------------KTKLLVSEKSRDGWLNFKELLNeASTEHHCVE--TGSQEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVANvLQANGAYAPLLNDGKEF--------VVTALplYHIFA-LTVNCLLFLHKgann 279
Cdd:cd05928 177 MAIYFTSGTTGSPKMAEHSHSSLGLG-LKVNGRYWLDLTASDIMwntsdtgwIKSAW--SSLFEpWIQGACVFVHH---- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 280 llitNPR-DIPGFVAELKKTPFTALTGVNTLFNALVNsEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYG 358
Cdd:cd05928 250 ----LPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASpLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAK-GPQ----VMLGYWQRPEETAKVIDKDG 433
Cdd:cd05928 325 QTETG-LICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 434 WLaTGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV--AKDKSLTE 511
Cdd:cd05928 404 YL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlaPQFLSHDP 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 512 KELIKHCRHHLTG----YKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:cd05928 483 EQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
27-552 |
4.84e-65 |
|
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: 221.25 E-value: 4.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQP---AFVN--MGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVV 101
Cdd:cd17642 18 EQLHKAMKRYASVPgtiAFTDahTGVNYSYAEYLEMSVRLAEALKK-YGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 102 VNVNPLYTPRELKHQL-------VDSGAKAIVVVSNFASTLEQVVdqtpvKNVIITGLGDLLSapKRTLVNFVvkyikrl 174
Cdd:cd17642 97 APTNDIYNERELDHSLniskptiVFCSKKGLQKVLNVQKKLKIIK-----TIIILDSKEDYKG--YQCLYTFI------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 175 vpkyslphaismRRALRAGKKAQYVKPVV--KSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQA-NGAYAPLLNDGKE 251
Cdd:cd17642 163 ------------TQNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHArDPIFGNQIIPDTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 252 fVVTALPLYHIFALTVNcLLFLHKGANNLLITNpRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSI 331
Cdd:cd17642 231 -ILTVIPFHHGFGMFTT-LGYLICGFRVVLMYK-FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 332 GGGMAVQRAVAD---KWQNITKTRllEGYGLTEASPLVACCPyDLAGYNGSIGLPAPSTQIQVRG-DDGQVLPQGETGEL 407
Cdd:cd17642 308 SGGAPLSKEVGEavaKRFKLPGIR--QGYGLTETTSAILITP-EGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGEL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 408 FAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAV 487
Cdd:cd17642 385 CVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 488 GVPHEVSGELVKIFVVAK-DKSLTEKELIKHCRHHLTGYKvpKL---VEFRDELPKTNVGKILRRELRD 552
Cdd:cd17642 465 GIPDEDAGELPAAVVVLEaGKTMTEKEVMDYVASQVSTAK--RLrggVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-554 |
1.26e-63 |
|
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: 212.34 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 SDDIAFLQYTGGTTGVSKGAMLSHGNIVAN--VLQANGAYAPllndgKEFVVTALPLYHIFALTVNCLLFLHKGANNLLI 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNawMLALNSLFDP-----DDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 T-----NPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAalDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGY 357
Cdd:cd05944 76 GpagyrNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPVNA--DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 358 GLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQ-----GETGELFAKGPQVMLGYWQrpEETAKVID-K 431
Cdd:cd05944 154 GLTEATCLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRLLrdcapDEVGEICVAGPGVFGGYLY--TEGNKNAFvA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV-VAKDKSLT 510
Cdd:cd05944 232 DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVqLKPGAVVE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 655376187 511 EKELIKHCRHHLTGY-KVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:cd05944 312 EEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADA 356
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
24-557 |
1.29e-63 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 217.32 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVN 103
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 104 VNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQV-VDQTPVKNVIITGLGDLLSAPKRtlvnfvVKYIkrlvpkySLPh 182
Cdd:PRK06155 101 INTALRGPQLEHILRNSGARLLVVEAALLAALEAAdPGDLPLPAVWLLDAPASVSVPAG------WSTA-------PLP- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 183 aismrrALRAGKKAQYVKPvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVanVLQANGAYAPLLNDGkEFVVTALPLYHI 262
Cdd:PRK06155 167 ------PLDAPAPAAAVQP----GDTAAILYTSGTTGPSKGVCCPHAQFY--WWGRNSAEDLEIGAD-DVLYTTLPLFHT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 263 FALTVNCLLFLHkGANnlLITNPR-DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQraV 341
Cdd:PRK06155 234 NALNAFFQALLA-GAT--YVLEPRfSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAA--L 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 342 ADKWQNITKTRLLEGYGLTEA-SPLVACCPYDLAGYNGSIglpAPSTQIQVRGDDGQVLPQGETGELF--AKGP-QVMLG 417
Cdd:PRK06155 309 HAAFRERFGVDLLDGYGSTETnFVIAVTHGSQRPGSMGRL---APGFEARVVDEHDQELPDGEPGELLlrADEPfAFATG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:PRK06155 386 YFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDE 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 498 VKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:PRK06155 465 VMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA 525
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
24-550 |
1.71e-63 |
|
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: 215.84 E-value: 1.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNM--GATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVV 101
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADParGLRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 102 VNVNPLYTPRELKhQLVDSGAKAIVVVSNFAstleqvvdqtPVKNVIITGLGDLLSapkrtlvnfvvkyikrlvpkysLP 181
Cdd:cd05923 81 ALINPRLKAAELA-ELIERGEMTAAVIAVDA----------QVMDAIFQSGVRVLA----------------------LS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 182 HAISMRRALRAGKKAQYvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqANGAYAPLLNDGKEFVVTALPLYH 261
Cdd:cd05923 128 DLVGLGEPESAGPLIED--PPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVL-FMSTQAGLRHGRHNVVLGLMPLYH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 262 I---FALTVNCLLFlhkganNLLITNPRDI-PGFVAEL-KKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMA 336
Cdd:cd05923 205 VigfFAVLVAALAL------DGTYVVVEEFdPADALKLiEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 337 VQRAVADKWQNITKTRLLEGYGLTEASPLVaccpYDLAGYNGSIGLPAPSTQIQ---VRGDDGQVLPQGETGELFAK--G 411
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTEAMNSL----YMRDARTGTEMRPGFFSEVRivrIGGSPDEALANGEEGELIVAaaA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 412 PQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPH 491
Cdd:cd05923 355 DAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAD 433
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 492 EVSGELVKIFVVAKDKSLTEKELIKHCR-HHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05923 434 ERWGQSVTACVVPREGTLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
39-551 |
2.02e-63 |
|
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: 214.26 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 39 QPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELkhqlv 118
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 119 dsgakaivvvsnfastlEQVVDQTpvknviitglgdllsapKRTlvnfvvkyikrlvpkyslphaismrRALRAGKkaqy 198
Cdd:cd05958 76 -----------------AYILDKA-----------------RIT-------------------------VALCAHA---- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 199 vkpVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVA-------NVLQangayaplLNDGKEFVVTAlPLYHIFALTVNCLL 271
Cdd:cd05958 93 ---LTASDDICILAFTSGTTGAPKATMHFHRDPLAsadryavNVLR--------LREDDRFVGSP-PLAFTFGLGGVLLF 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 272 FLHKGANNLLI--TNPRDIPGFVAELKKTP-FTALTGvntlFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNI 348
Cdd:cd05958 161 PFGVGASGVLLeeATPDLLLSAIARYKPTVlFTAPTA----YRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEA 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 349 TKTRLLEGYGLTEASPLVACCPYDLAgYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQvmlGYWQRPEETAKV 428
Cdd:cd05958 237 TGIPIIDGIGSTEMFHIFISARPGDA-RPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPT---GCRYLADKRQRT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 429 IDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK--- 505
Cdd:cd05958 313 YVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgv 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 655376187 506 --DKSLTEkELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05958 393 ipGPVLAR-ELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
14-555 |
1.50e-62 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 214.92 E-value: 1.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 14 PAEIDASRYA------SLLEMLESAVNTYADQPAFVNMGA------TLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMM 81
Cdd:PRK13295 9 PPRRAASIAAghwhdrTINDDLDACVASCPDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGL-ARLGVGRGDVVSCQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 82 PNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNF-----ASTLEQVVDQTP-VKNVIITGlGD- 154
Cdd:PRK13295 88 PNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPaLRHVVVVG-GDg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 155 ------LLSAPKRTLVnfvvkyikrlvpkyslPHAISMRRALRAGkkaqyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSH 228
Cdd:PRK13295 167 adsfeaLLITPAWEQE----------------PDAPAILARLRPG-----------PDDVTQLIYTSGTTGEPKGVMHTA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 229 GNIVANVLqangAYAPLLNDGKEFVV-TALPLYHIFALTVNCLLFLHKGANNLLitnpRDI--PGFVAELKKTPFTALTG 305
Cdd:PRK13295 220 NTLMANIV----PYAERLGLGADDVIlMASPMAHQTGFMYGLMMPVMLGATAVL----QDIwdPARAAELIRTEGVTFTM 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 306 VNTLFNA-LVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYD---LAGynGSIG 381
Cdd:PRK13295 292 ASTPFLTdLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDpdeRAS--TTDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 382 LPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAkvIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILV 461
Cdd:PRK13295 370 CPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRSKDVIIR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 462 SGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLTEKELIKHCR-HHLTGYKVPKLVEFRDELPK 539
Cdd:PRK13295 448 GGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRpGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPR 527
|
570 580
....*....|....*....|
gi 655376187 540 TNVGKI----LRRELRDEAK 555
Cdd:PRK13295 528 TPSGKIqkfrLREMLRGEDA 547
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-552 |
4.60e-61 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 208.06 E-value: 4.60e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVvs 129
Cdd:cd05971 8 TFKELKTASNRFANVLK-EIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 nfastleqvvdqtpvknviitglgDLlsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvkSDDIA 209
Cdd:cd05971 85 ------------------------DG-------------------------------------------------SDDPA 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 210 FLQYTGGTTGVSKGAMLSH----GNIVanVLQANGAYAPllNDGKEFVVTALPLYhIFALTVNCLLFLHKGannllitnp 285
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHrvllGHLP--GVQFPFNLFP--RDGDLYWTPADWAW-IGGLLDVLLPSLYFG--------- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 rdIPgfVAELKKTPFT---ALT-----GVNTLF---NAL-VNSEEFAALDFSRLKL-SIGGGMAVQRAVADKWQNIT-KT 351
Cdd:cd05971 158 --VP--VLAHRMTKFDpkaALDlmsryGVTTAFlppTALkMMRQQGEQLKHAQVKLrAIATGGESLGEELLGWAREQfGV 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQ--VMLGYWQRPEETAKVI 429
Cdd:cd05971 234 EVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 dKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSL 509
Cdd:cd05971 314 -AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET 392
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 655376187 510 TEKELIKHCRHH----LTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05971 393 PSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
25-551 |
1.82e-60 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 207.15 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 25 LLEMLESAVNTYADQPAFVNMG-ATLTYRKLEERSRAFAAylqndlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVN 103
Cdd:PRK07787 1 LASLNPAAVAAAADIADAVRIGgRVLSRSDLAGAATAVAE------RVAGARRVAVLATPTLATVLAVVGALIAGVPVVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 104 VNPLYTPRELKHQLVDSGAKAIvvvsnfastleqvvdqtpvknviitgLGDLLSAPKrtlvnfvvkyikrlvpkySLPHa 183
Cdd:PRK07787 75 VPPDSGVAERRHILADSGAQAW--------------------------LGPAPDDPA------------------GLPH- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 184 ISMRRALRAGkkaqYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkeFVVTALPLYHIF 263
Cdd:PRK07787 110 VPVRLHARSW----HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADD---VLVHGLPLFHVH 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 264 ALTVNCLLFLHKGanNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFA-ALDFSRLKLSigGGMAVQRAVA 342
Cdd:PRK07787 183 GLVLGVLGPLRIG--NRFVHTGRPTPEAYAQALSEGGTLYFGVPTVWSRIAADPEAArALRGARLLVS--GSAALPVPVF 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 343 DKWQNITKTRLLEGYGLTEAspLVACCPY-DLAGYNGSIGLPAPSTQIQVRGDDGQVLPQ-GET-GELFAKGPQVMLGYW 419
Cdd:PRK07787 259 DRLAALTGHRPVERYGMTET--LITLSTRaDGERRPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 420 QRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKK-DMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELV 498
Cdd:PRK07787 337 NRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRI 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 655376187 499 KIFVVAKDKSlTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK07787 417 VAYVVGADDV-AADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
213-547 |
1.79e-59 |
|
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: 200.57 E-value: 1.79e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 213 YTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGKEFVVtALPLYHIFALTVNcLLFLHKGANNLLIT--NPRDIPG 290
Cdd:cd17637 7 HTAAVAGRPRGAVLSHGNLIAANLQLIHAMG--LTEADVYLN-MLPLFHIAGLNLA-LATFHAGGANVVMEkfDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 291 FVAELKKTPFTALTGVntLFNaLVNSEEFAALDFSRLKLSIGGGMAvqrAVADKWQNITKTRLLEGYGLTEASPLVACCP 370
Cdd:cd17637 83 LIEEEKVTLMGSFPPI--LSN-LLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETSGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 371 YDLAgyNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFY 450
Cdd:cd17637 157 YRER--PGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLW 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 451 IVDRK--KDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKV 527
Cdd:cd17637 234 YAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPgATLTADELIEFVGSRIARYKK 313
|
330 340
....*....|....*....|
gi 655376187 528 PKLVEFRDELPKTNVGKILR 547
Cdd:cd17637 314 PRYVVFVEALPKTADGSIDR 333
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
18-552 |
2.51e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 205.93 E-value: 2.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 18 DASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRA 97
Cdd:PRK07788 44 DIRRYGPFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLA-LGVRAGDGVAVLARNHRGFVLALYAAGKV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 98 GMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGL--GDLLSAPKRTLVNFVVKYIKRLV 175
Cdd:PRK07788 123 GARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPddDEPSGSTDETLDDLIAGSSTAPL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 176 PKYSlphaismrralragkkaqyvkpvvKSDDIAFLqyTGGTTGVSKGAMLSH-------GNIVANV-LQANGAYaplln 247
Cdd:PRK07788 203 PKPP------------------------KPGGIVIL--TSGTTGTPKGAPRPEpsplaplAGLLSRVpFRAGETT----- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 248 dgkefVVTAlPLYH-------IFALTVNCLLFLH---KGANNLlitnpRDIPGFVAelkktpfTALTGVNTLFNALVNSE 317
Cdd:PRK07788 252 -----LLPA-PMFHatgwahlTLAMALGSTVVLRrrfDPEATL-----EDIAKHKA-------TALVVVPVMLSRILDLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 318 E--FAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDD 395
Cdd:PRK07788 314 PevLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVKILDEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 396 GQVLPQGETGELFAKGPQVMLGYwqrpeeTA---KVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVE 472
Cdd:PRK07788 394 GNEVPRGVVGRIFVGNGFPFEGY------TDgrdKQI-IDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 473 EVVALHPKVVEVAAVGVPHEVSGELVKIFVV-AKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK07788 467 DLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVkAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
.
gi 655376187 552 D 552
Cdd:PRK07788 547 E 547
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
49-551 |
5.72e-59 |
|
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: 202.35 E-value: 5.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYT---PRELKHQLVDSGAKAI 125
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVIC---PLFSafgPEAIRDRLENSEAKVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VvvsnfasTLEQVVDQTPVKnviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvks 205
Cdd:cd05969 77 I-------TTEELYERTDPE------------------------------------------------------------ 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 dDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqaNGAYAPLLNDGKEFVVTALP------LYHIFALTVNcllflhkGANN 279
Cdd:cd05969 90 -DPTLLHYTSGTTGTPKGVLHVHDAMIFYYF--TGKYVLDLHPDDIYWCTADPgwvtgtVYGIWAPWLN-------GVTN 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 280 LLIT---NPRDIPGFVAELKKTP-FTALTGVNTLFNAlvNSEEFAALDFSRLKLSIGGGMAVQRAVAdKW-QNITKTRLL 354
Cdd:cd05969 160 VVYEgrfDAESWYGIIERVKVTVwYTAPTAIRMLMKE--GDELARKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIH 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 355 EGYGLTE-ASPLVACCPYDLAGyNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKG--PQVMLGYWQRPEETAKVIdK 431
Cdd:cd05969 237 DTWWQTEtGSIMIANYPCMPIK-PGSMGKPLPGVKAAVVDENGNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSF-I 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSLT 510
Cdd:cd05969 315 DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKeGFEPS 394
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 655376187 511 EK---ELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05969 395 DElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
49-552 |
7.45e-59 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 203.78 E-value: 7.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVv 128
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAA-LGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 snFASTLEQVVDQTPvKNVIITglgdLLSAPKRTLVNFVVKYIKRLVPkyslPHAISMRRALRAGkkAQYVKPVVKSDdi 208
Cdd:PRK12406 90 --HADLLHGLASALP-AGVTVL----SVPTPPEIAAAYRISPALLTPP----AGAIDWEGWLAQQ--EPYDGPPVPQP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGamLSHGNIVANVLQANGAYAPLLNDGKEFVVTAL--PLYH-------IFALTVncllflhkGANn 279
Cdd:PRK12406 155 QSMIYTSGTTGHPKG--VRRAAPTPEQAAAAEQMRALIYGLKPGIRALLtgPLYHsapnaygLRAGRL--------GGV- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 280 lLITNPR-DIPGFVAELKKTPFTALTGVNTLFNALVN--SEEFAALDFSRLKLSIGGGMA----VQRAVADKWQNItktr 352
Cdd:PRK12406 224 -LVLQPRfDPEELLQLIERHRITHMHMVPTMFIRLLKlpEEVRAKYDVSSLRHVIHAAAPcpadVKRAMIEWWGPV---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVML-GYWQRPEETAKvIDK 431
Cdd:PRK12406 299 IYEYYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-IDR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGE-LVKIFVVAKDKSLT 510
Cdd:PRK12406 378 GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEaLMAVVEPQPGATLD 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655376187 511 EKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK12406 458 EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
201-552 |
7.65e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 203.50 E-value: 7.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 201 PVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVA-----NVLQANGAYAPLLNDGkefvvtalPLYHIFALTVNCLLFLHK 275
Cdd:PRK09088 130 PSIPPERVSLILFTSGTSGQPKGVMLSERNLQQtahnfGVLGRVDAHSSFLCDA--------PMFHIIGLITSVRPVLAV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANnLLITNprdipGFvaELKKT------PFTALT---GVNTLFNALVNSEEFAALDFSRLKLSIGGGmAVQRAVADKWQ 346
Cdd:PRK09088 202 GGS-ILVSN-----GF--EPKRTlgrlgdPALGIThyfCVPQMAQAFRAQPGFDAAALRHLTALFTGG-APHAAEDILGW 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NITKTRLLEGYGLTEASPlVACCPYD---LAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:PRK09088 273 LDDGIPMVDGFGMSEAGT-VFGMSVDcdvIRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV 503
Cdd:PRK09088 352 ATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIV 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 655376187 504 AKDKSLTEKELIK-HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK09088 432 PADGAPLDLERIRsHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
38-552 |
2.16e-58 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 203.45 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK13382 58 DRPGLIDELGTLTWRELDERSDALAAALQA-LPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDQTPVKNVIItglgDLLSAPKRTLVNfvvkyikrlvpkyslphaismrrALRAGKKAQ 197
Cdd:PRK13382 137 TREGVDTVIYDEEFSATVDRALADCPQATRIV----AWTDEDHDLTVE-----------------------VLIAAHAGQ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 YVKPVVKSDDIAFLqyTGGTTGVSKGAMLShGNIVANVLQANGAYAPLlnDGKEFVVTALPLYH-------IFALTVNCL 270
Cdd:PRK13382 190 RPEPTGRKGRVILL--TSGTTGTPKGARRS-GPGGIGTLKAILDRTPW--RAEEPTVIVAPMFHawgfsqlVLAASLACT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 LflhkgannllITNPRDIPGFVAEL-KKTPFTALTGVNTLFNALVN--SEEFAALDFSRLKLSIGGGMAVQRAVADKWQN 347
Cdd:PRK13382 265 I----------VTRRRFDPEATLDLiDRHRATGLAVVPVMFDRIMDlpAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYwqRPEETAK 427
Cdd:PRK13382 335 QFGDVIYNNYNATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 428 VIDkdGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDK 507
Cdd:PRK13382 413 FHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 508 -SLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK13382 491 aSATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
211-552 |
5.29e-58 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 200.68 E-value: 5.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 211 LQYTGGTTGVSKG--AMLSHGNIVANVLqangaYAPLLNDGKEFVVTAL---PLYHIFALTVNCLLflHKGANNLLITNP 285
Cdd:cd05929 130 MLYSGGTTGRPKGikRGLPGGPPDNDTL-----MAAALGFGPGADSVYLspaPLYHAAPFRWSMTA--LFMGGTLVLMEK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 RDIPGFVAELKKTPFTALTGVNTLFNAL--VNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEAS 363
Cdd:cd05929 203 FDPEEFLRLIERYRVTFAQFVPTMFVRLlkLPEAVRNAYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 364 PLVACCPYDLAGYNGSIGLPAPStQIQVRGDDGQVLPQGETGEL-FAKGPQVMlgYWQRPEETAKVIDKDGWLATGDIGY 442
Cdd:cd05929 283 GLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVyFANGPGFE--YTNDPEKTAAARNEGGWSTLGDVGY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 443 MDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV----VAKDKSLTEKELIKHC 518
Cdd:cd05929 360 LDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVqpapGADAGTALAEELIAFL 439
|
330 340 350
....*....|....*....|....*....|....
gi 655376187 519 RHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05929 440 RDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
37-550 |
5.10e-57 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 197.37 E-value: 5.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 37 ADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYtPRE-LKH 115
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRE-RGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY-PAErLAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 116 QLVDSGAKAIVVvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkk 195
Cdd:cd05930 79 ILEDSGAKLVLT-------------------------------------------------------------------- 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 196 aqyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNVLQANGAYAPLLNDGKEFVVTALP----LYHIFALTVN--C 269
Cdd:cd05930 91 --------DPDDLAYVIYTSGSTGKPKGVMVEHRGLV-NLLLWMQEAYPLTPGDRVLQFTSFSfdvsVWEIFGALLAgaT 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 270 LLFLHKGAnnllITNPRDIPGFVAELKktpFTALTGVNTLFNALVNSEEFAalDFSRLKLSIGGGMAVQRAVADKW-QNI 348
Cdd:cd05930 162 LVVLPEEV----RKDPEALADLLAEEG---ITVLHLTPSLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWrELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 349 TKTRLLEGYGLTEASplVAC----CPYDLAGYNG-SIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:cd05930 233 PGARLVNLYGPTEAT--VDAtyyrVPPDDEEDGRvPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPE 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:cd05930 311 LTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKR 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 655376187 498 VKIFVVAKDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05930 391 LVAYVVPDEGGeLDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
39-557 |
3.23e-56 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 204.00 E-value: 3.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 39 QPAFVN-MGATLTYRKLEERSRAFAAYLQNDLKLQKgdRVAIMMPNLLQYPIALFGVLRAGMVVVNVNplYTPRE--LKH 115
Cdd:PRK08633 631 RLAVADsTGGELSYGKALTGALALARLLKRELKDEE--NVGILLPPSVAGALANLALLLAGKVPVNLN--YTASEaaLKS 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 116 QLVDSGAKAIVvvsnfasTLEQVVDQTPVKnviitglGDLLSAPkrTLVNFVvkYIKRLVPKyslPHAISMRRALRAGK- 194
Cdd:PRK08633 707 AIEQAQIKTVI-------TSRKFLEKLKNK-------GFDLELP--ENVKVI--YLEDLKAK---ISKVDKLTALLAARl 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 195 ------KAQYVKPVvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkeFVVTALPLYHIFALTVN 268
Cdd:PRK08633 766 lparllKRLYGPTF-KPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD---VILSSLPFFHSFGLTVT 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 CLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNI 348
Cdd:PRK08633 842 LWLPLLEGIKVVYHPDPTDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEK 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 349 TKTRLLEGYGLTEASPLVAC-CPYDLAGYN--------GSIGLPAPSTQIQ-VRGDDGQVLPQGETGELFAKGPQVMLGY 418
Cdd:PRK08633 922 FGIRILEGYGATETSPVASVnLPDVLAADFkrqtgskeGSVGMPLPGVAVRiVDPETFEELPPGEDGLILIGGPQVMKGY 1001
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 419 WQRPEETAKVI---DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA--LHPKVVEVAAVGVPHEV 493
Cdd:PRK08633 1002 LGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGGEEVVFAVTAVPDEK 1081
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 494 SGElvKIFVVAKDKSLTEKELikhcRHHLTGYKVPKLVEFR-----DELPKTNVGKILRRELRDEAKSA 557
Cdd:PRK08633 1082 KGE--KLVVLHTCGAEDVEEL----KRAIKESGLPNLWKPSryfkvEALPLLGSGKLDLKGLKELALAL 1144
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
35-550 |
3.36e-56 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 195.16 E-value: 3.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 35 TYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPlYTPrelk 114
Cdd:cd05945 3 ANPDRPAVVEGGRTLTYRELKERADALAAALA-SLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDA-SSP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 115 hqlvdsgakaivvvsnfASTLEQVVDQTPVKNVIITGlgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragk 194
Cdd:cd05945 77 -----------------AERIREILDAAKPALLIADG------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 195 kaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGKEFVVTA-----LPLYHIF-AL--- 265
Cdd:cd05945 97 -----------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP--LGPGDVFLNQApfsfdLSVMDLYpALasg 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 266 -TVNCLlflhkgaNNLLITNPRDipgFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADK 344
Cdd:cd05945 164 aTLVPV-------PRDATADPKQ---LFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 345 WQNIT-KTRLLEGYGLTEASplVACCPYD-----LAGYNG-SIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLG 417
Cdd:cd05945 234 LQQRFpDARIYNTYGPTEAT--VAVTYIEvtpevLDGYDRlPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YWQRPEETAKV---IDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVS 494
Cdd:cd05945 312 YLNNPEKTAAAffpDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 495 GELVKIFVVAKDKS--LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05945 392 VTELIAFVVPKPGAeaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
26-557 |
5.88e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 197.09 E-value: 5.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 26 LEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVN 105
Cdd:PRK08162 21 LSFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALAR-RGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 106 PLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDllsapkrtlvnfvvkyikrlvPKYSLPHAIS 185
Cdd:PRK08162 100 TRLDAASIAFMLRHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVDD---------------------PEYPGGRFIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 186 MR--RALRAGKKAQYV--KPVVKSDDIAfLQYTGGTTGVSKGAMLSH-G---NIVANVLQAN-GAYAPLLndgkefvvTA 256
Cdd:PRK08162 159 ALdyEAFLASGDPDFAwtLPADEWDAIA-LNYTSGTTGNPKGVVYHHrGaylNALSNILAWGmPKHPVYL--------WT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 257 LPLYHI----FALTVNcllfLHKGANNLLitnpRDI-PGFVAEL-KKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLS 330
Cdd:PRK08162 230 LPMFHCngwcFPWTVA----ARAGTNVCL----RKVdPKLIFDLiREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 331 IGGGMAVQRAVADKWQNItKTRLLEGYGLTEASPLVACC----------PYDLAGYNGSIGLPAPsTQIQVR---GDDGQ 397
Cdd:PRK08162 302 MVAGAAPPAAVIAKMEEI-GFDLTHVYGLTETYGPATVCawqpewdalpLDERAQLKARQGVRYP-LQEGVTvldPDTMQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 398 VLPQ-GET-GELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV 475
Cdd:PRK08162 380 PVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 476 ALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFrDELPKTNVGKILRRELRDEA 554
Cdd:PRK08162 459 YRHPAVLVAAVVAKPDPKWGEVPCAFVELKDgASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQA 537
|
...
gi 655376187 555 KSA 557
Cdd:PRK08162 538 KSL 540
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
46-547 |
8.38e-56 |
|
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: 194.58 E-value: 8.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvks 205
Cdd:cd05914 84 FVSDE--------------------------------------------------------------------------- 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVlqaNGAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITnp 285
Cdd:cd05914 89 DDVALINYTSGTTGNSKGVMLTYRNIVSNV---DGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLD-- 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 rDIPGFVAELKK------------------------TPFTALTGVNTLFNALVNSEEFAALDFS--------RLKLSIGG 333
Cdd:cd05914 164 -KIPSAKIIALAfaqvtptlgvpvplviekifkmdiIPKLTLKKFKFKLAKKINNRKIRKLAFKkvheafggNIKEFVIG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 334 GMAVQRAVADKWQNItKTRLLEGYGLTEASPLVACCPYDLAGYnGSIGLPAPSTQIQVRGDDgqvlPQGETGELFAKGPQ 413
Cdd:cd05914 243 GAKINPDVEEFLRTI-GFPYTIGYGMTETAPIISYSPPNRIRL-GSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 414 VMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILV-SGFNVFPNEVEEVVALHPKVVEvAAVGVPHE 492
Cdd:cd05914 317 VMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLE-SLVVVQEK 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 493 VSGELVKI---FVVAKDKSLTEK------ELIKHCRHHLTGY-KVPKLVEFRDELPKTNVGKILR 547
Cdd:cd05914 396 KLVALAYIdpdFLDVKALKQRNIidaikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
48-551 |
2.38e-55 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 195.88 E-value: 2.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVvnvNPLYT---PRELKHQLVDSGAKA 124
Cdd:PRK04319 73 KYTYKELKELSNKFANVLK-ELGVEKGDRVFIFMPRIPELYFALLGALKNGAIV---GPLFEafmEEAVRDRLEDSEAKV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 125 IVVVsnfASTLEQVV-DQTP-VKNVIITGLGDllsapkrtlvnfvvkyikRLVPKYslphaISMRRALRAGKKaQYVKPV 202
Cdd:PRK04319 149 LITT---PALLERKPaDDLPsLKHVLLVGEDV------------------EEGPGT-----LDFNALMEQASD-EFDIEW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 203 VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvlQANGAYAPLLNDGKEFVVTALP------LYHIFALtvncllFLHkG 276
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGVLHVHNAMLQH--YQTGKYVLDLHEDDVYWCTADPgwvtgtSYGIFAP------WLN-G 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANNLLIT---NPRDIPGFVAELKKTP-FTALTGVNTLFNAlvNSEEFAALDFSRLK--LSIGGGM---AVqravadKW-Q 346
Cdd:PRK04319 273 ATNVIDGgrfSPERWYRILEDYKVTVwYTAPTAIRMLMGA--GDDLVKKYDLSSLRhiLSVGEPLnpeVV------RWgM 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGEL-FAKG-PQVMLGYWQRPEE 424
Cdd:PRK04319 345 KVFGLPIHDNWWMTETGGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLaIKKGwPSMMRGIWNNPEK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 425 TAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVA 504
Cdd:PRK04319 425 YESYF-AGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVAL 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 655376187 505 K-----DKSLTEkELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK04319 504 RpgyepSEELKE-EIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
50-552 |
7.87e-55 |
|
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: 193.87 E-value: 7.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVs 129
Cdd:cd05970 49 TFAELADYSDKTANFFKA-MGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAI- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 nfastleqvvDQTPVKNVIITGLGDLLSAPKRTLVNFVV--------KYIKRLVPKYSLPHAISMrralragkkaqyvkp 201
Cdd:cd05970 127 ----------AEDNIPEEIEKAAPECPSKPKLVWVGDPVpegwidfrKLIKNASPDFERPTANSY--------------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 202 vVKSDDIAFLQYTGGTTGVSKgaMLSH------GNIVANVLQANgayapLLNDGKEFVVTAL--------PLYHIFALTV 267
Cdd:cd05970 182 -PCGEDILLVYFSSGTTGMPK--MVEHdftyplGHIVTAKYWQN-----VREGGLHLTVADTgwgkavwgKIYGQWIAGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 268 NCLLFLHKgannllitnpRDIPGFVAE-LKKTPFTALTGVNTLFNALVNsEEFAALDFSRLKLSIGGGMAVQRAVADKWQ 346
Cdd:cd05970 254 AVFVYDYD----------KFDPKALLEkLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NITKTRLLEGYGLTEASPLVACCPYdLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGEL---FAKGPQVML--GYWQR 421
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPW-MEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIvirTSKGKPVGLfgGYYKD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 422 PEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIF 501
Cdd:cd05970 402 AEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKAT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 502 VV-AKDKSLTE---KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05970 481 IVlAKGYEPSEelkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
28-544 |
3.29e-54 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 192.02 E-value: 3.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 28 MLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPL 107
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLI-AQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 108 YTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTP-VKNVIItgLGDLLSAPkrtlvnfvvkyikrlvpkySLPHAISM 186
Cdd:PRK07798 87 YVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPkLRTLVV--VEDGSGND-------------------LLPGAVDY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 RRALRAGkKAQYVKPVVKSDDIAFLqYTGGTTGVSKGAMLSHGNIVanVLQANG---AYAPLLNDGKEFVVTAL------ 257
Cdd:PRK07798 146 EDALAAG-SPERDFGERSPDDLYLL-YTGGTTGMPKGVMWRQEDIF--RVLLGGrdfATGEPIEDEEELAKRAAagpgmr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 258 -----PLYHIFAL--TVNCLLFlhkGANNLLITNPRdipgFVA-ELKKTpfTALTGVNTLF-----------NALVNSEE 318
Cdd:PRK07798 222 rfpapPLMHGAGQwaAFAALFS---GQTVVLLPDVR----FDAdEVWRT--IEREKVNVITivgdamarpllDALEARGP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 319 FaalDFSRLKLSIGGGMAVQRAVADKWQ----NITktrLLEGYGLTEasplvaccpydlAGYNGSI---------GLP-- 383
Cdd:PRK07798 293 Y---DLSSLFAIASGGALFSPSVKEALLellpNVV---LTDSIGSSE------------TGFGGSGtvakgavhtGGPrf 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 384 --APSTqiQVRGDDGQVLPQGETGE-LFAKGPQVMLGYWQRPEETAK---VIDKDGWLATGDIGYMDEKGFFYIVDRKKD 457
Cdd:PRK07798 355 tiGPRT--VVLDEDGNPVEPGSGEIgWIARRGHIPLGYYKDPEKTAEtfpTIDGVRYAIPGDRARVEADGTITLLGRGSV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 458 MILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSG-ELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDE 536
Cdd:PRK07798 433 CINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGqEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDE 512
|
....*...
gi 655376187 537 LPKTNVGK 544
Cdd:PRK07798 513 VQRSPAGK 520
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
50-487 |
1.07e-53 |
|
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: 187.47 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS 129
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 NFASTLEQVVDqtpvknVIITGLGDLLSAPKRTLVNFVVKyikrlvpkyslphaismrralragkkaqyvkPVVKSDDIA 209
Cdd:TIGR01733 81 ALASRLAGLVL------PVILLDPLELAALDDAPAPPPPD-------------------------------APSGPDDLA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 210 FLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkefVVTALPLYH-------IFAltvnCLLFlhkGANNLLI 282
Cdd:TIGR01733 124 YVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDD----RVLQFASLSfdasveeIFG----ALLA---GATLVVP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNP--RDIPGFVAELKKT-PFTALTGVNTLFNALVNSEEFAaldFSRLKLSIGGGMAVQRAVADKWQ-NITKTRLLEGYG 358
Cdd:TIGR01733 193 PEDeeRDDAALLAALIAEhPVTVLNLTPSLLALLAAALPPA---LASLRLVILGGEALTPALVDRWRaRGPGARLINLYG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASplVAC----CPYDLAGYNGS--IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI--- 429
Cdd:TIGR01733 270 PTETT--VWStatlVDPDDAPRESPvpIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFvpd 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 430 -----DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPkVVEVAAV 487
Cdd:TIGR01733 348 pfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHP-GVREAVV 409
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
47-488 |
1.50e-53 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 188.72 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 47 ATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvkSD 206
Cdd:cd17640 83 VEND--------------------------------------------------------------------------SD 88
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANgAYAPLlNDGKEFVvTALPLYHIFALTVNCLLFLhKGANNLLITnpr 286
Cdd:cd17640 89 DLATIIYTSGTTGNPKGVMLTHANLLHQIRSLS-DIVPP-QPGDRFL-SILPIWHSYERSAEYFIFA-CGCSQAYTS--- 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 dIPGFVAELKKTPFTALTGVNTLFNALVNS--EEFAALDFSR------------LKLSIGGGMAVQRAVaDKWQNITKTR 352
Cdd:cd17640 162 -IRTLKDDLKRVKPHYIVSVPRLWESLYSGiqKQVSKSSPIKqflflfflsggiFKFGISGGGALPPHV-DTFFEAIGIE 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVAC----CPYdlagyNGSIGLPAPSTQIQVRGDDGQ-VLPQGETGELFAKGPQVMLGYWQRPEETAK 427
Cdd:cd17640 240 VLNGYGLTETSPVVSArrlkCNV-----RGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSK 314
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 428 VIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVS-GFNVFPNEVEEVVALHPKVVEVAAVG 488
Cdd:cd17640 315 VLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
73-550 |
1.25e-52 |
|
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: 185.34 E-value: 1.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 73 KGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGakaivvvsnfastleqvvdqtpvKNVIITGl 152
Cdd:TIGR01923 23 SGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLD-----------------------VQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 153 gDLLSApkrtlvnfvvKYIKrlvpkyslphAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIV 232
Cdd:TIGR01923 79 -SLLEE----------KDFQ----------ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 233 ANV---LQANGAYapllnDGKEFVVtALPLYHIFALTV--NCL-----LFLHKGANNLLitnprdipgfvAELKKTPFTA 302
Cdd:TIGR01923 138 ASAvgsKENLGFT-----EDDNWLL-SLPLYHISGLSIlfRWLiegatLRIVDKFNQLL-----------EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 303 LTGVNTLFNALV---NSEEfaaldfsRLKLSIGGGMAVQRAVADKWQ--NITktrLLEGYGLTE-ASPLVACCPYDLAGy 376
Cdd:TIGR01923 201 ISLVPTQLNRLLdegGHNE-------NLRKILLGGSAIPAPLIEEAQqyGLP---IYLSYGMTEtCSQVTTATPEMLHA- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 377 NGSIGLPAPSTQIQVRGDDgqvlpQGETGELFAKGPQVMLGYWQrPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKK 456
Cdd:TIGR01923 270 RPDVGRPLAGREIKIKVDN-----KEGHGEIMVKGANLMKGYLY-QGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 457 DMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAkDKSLTEKELIKHCRHHLTGYKVPKLVEFRDE 536
Cdd:TIGR01923 344 DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVS-ESDISQAKLIAYLTEKLAKYKVPIAFEKLDE 422
|
490
....*....|....
gi 655376187 537 LPKTNVGKILRREL 550
Cdd:TIGR01923 423 LPYNASGKILRNQL 436
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
213-540 |
3.25e-52 |
|
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: 181.35 E-value: 3.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 213 YTGGTTGVSKGAMLSHGNIVAnvlqANGAYAPLLNDGKEFV-VTALPLYHIFALTVnCLLFLHKGANNLLItnPRDIPGF 291
Cdd:cd17636 7 YTAAFSGRPNGALLSHQALLA----QALVLAVLQAIDEGTVfLNSGPLFHIGTLMF-TLATFHAGGTNVFV--RRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 292 VAEL---KKTPFTALTGvnTLFNALVNSEEFAALDFSRLKlsigggmaVQRAVADKWQNITKT-----RLLEGYGLTEAS 363
Cdd:cd17636 80 VLELieaERCTHAFLLP--PTIDQIVELNADGLYDLSSLR--------SSPAAPEWNDMATVDtspwgRKPGGYGQTEVM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 364 PLVAccpydLAGYNGSI----GLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGD 439
Cdd:cd17636 150 GLAT-----FAALGGGAiggaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-RGGWHHTND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 440 IGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHC 518
Cdd:cd17636 224 LGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVTEAELIEHC 303
|
330 340
....*....|....*....|..
gi 655376187 519 RHHLTGYKVPKLVEFRDELPKT 540
Cdd:cd17636 304 RARIASYKKPKSVEFADALPRT 325
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
49-557 |
8.96e-52 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 185.77 E-value: 8.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTprelkhqlVDSGAKAIVVV 128
Cdd:PLN02860 33 RTGHEFVDGVLSLAAGL-LRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWS--------FEEAKSAMLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SnfASTLeqVVDQTPVKNVIITGLGDLLSAPKRTLVNFVVKyikRLVPKYSLPHAISMRRAlRAGKKAQyVKPVVKSDDI 208
Cdd:PLN02860 104 R--PVML--VTDETCSSWYEELQNDRLPSLMWQVFLESPSS---SVFIFLNSFLTTEMLKQ-RALGTTE-LDYAWAPDDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVANVLqANGAYAPLLNDgKEFVVTAlPLYHIFALTvNCLLFLHKGANNLLItnprdi 288
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSALIVQSL-AKIAIVGYGED-DVYLHTA-PLCHIGGLS-SALAMLMVGACHVLL------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 289 PGFVAEL-----KKTPFTALTGVNTLFNALVN---SEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLT 360
Cdd:PLN02860 245 PKFDAKAalqaiKQHNVTSMITVPAMMADLISltrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 361 EA---------------SPLVACCPYDlAGYNGS--------IGLPAPSTQIQVRGDDGQvlpqgETGELFAKGPQVMLG 417
Cdd:PLN02860 325 EAcssltfmtlhdptleSPKQTLQTVN-QTKSSSvhqpqgvcVGKPAPHVELKIGLDESS-----RVGRILTRGPHVMLG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:PLN02860 399 YWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEM 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 498 VKIFVVAKDK---------------SLTEKELIKHCR-HHLTGYKVPKL-VEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:PLN02860 479 VVACVRLRDGwiwsdnekenakknlTLSSETLRHHCReKNLSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
35-551 |
1.13e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 181.75 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 35 TYADQPAFV--NMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRE 112
Cdd:PRK13390 9 IAPDRPAVIvaETGEQVSYRQLDDDSAALARVLY-DAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 113 LKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVI---ITGLGDLLSApkrtlvnfvvkyikrlvpkyslphaismrrA 189
Cdd:PRK13390 88 ADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSFggeIDGFGSFEAA------------------------------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 190 LRAGKkaqyvkPVVKSDDIAFLQYTGGTTGVSKG--------AMLSHGNIVANVlqANGAYAPLLNDgkeFVVTALPLYH 261
Cdd:PRK13390 138 AGAGP------RLTEQPCGAVMLYSSGTTGFPKGiqpdlpgrDVDAPGDPIVAI--ARAFYDISESD---IYYSSAPIYH 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 262 ifALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALV--NSEEFAALDFSRLKLSIGGG----M 335
Cdd:PRK13390 207 --AAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLLklDADVRTRYDVSSLRAVIHAAapcpV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 336 AVQRAVADKWQNItktrLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTqIQVRGDDGQVLPQGETGELFAKGPQVM 415
Cdd:PRK13390 285 DVKHAMIDWLGPI----VYEYYSSTEAHGMTFIDSPDWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 416 LGYWQRPEETAKVIDKDG--WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEV 493
Cdd:PRK13390 360 FRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPE 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 494 SGELVK--IFVVAKDKSLTE--KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK13390 440 MGEQVKavIQLVEGIRGSDElaRELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
19-554 |
1.05e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 179.94 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 19 ASRYASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAG 98
Cdd:PRK06164 6 APRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLACARLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 99 MVVVNVNPLYTPRELKHQLVDSGAKAIVVVS-----NFASTLEQVVDQT--PVKNVIITGLG-DLLSAPKRtLVNFVVky 170
Cdd:PRK06164 85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWPgfkgiDFAAILAAVPPDAlpPLRAIAVVDDAaDATPAPAP-GARVQL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 171 ikrLVPKYSLPHAISMRRALRAgkkaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGk 250
Cdd:PRK06164 162 ---FALPDPAPPAAAGERAADP-------------DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYG--YDPG- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 251 EFVVTALPLYHIFALTvNCLLFLHKGANnlLITNPR-DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAAlDFSRLKL 329
Cdd:PRK06164 223 AVLLAALPFCGVFGFS-TLLGALAGGAP--LVCEPVfDAARTARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 330 SiggGMAvqrAVADKWQNITKTRLLEG------YGLTEASPLVACCPYDLAG---YNGSiGLPApSTQIQVRG---DDGQ 397
Cdd:PRK06164 299 F---GFA---SFAPALGELAALARARGvpltglYGSSEVQALVALQPATDPVsvrIEGG-GRPA-SPEARVRArdpQDGA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 398 VLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVAL 477
Cdd:PRK06164 371 LLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 478 HPKVVEVAAVGVPHEVSGELVKiFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKT---NVGKILRRELRDE 553
Cdd:PRK06164 451 LPGVAAAQVVGATRDGKTVPVA-FVIPTDgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLREM 529
|
.
gi 655376187 554 A 554
Cdd:PRK06164 530 A 530
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
27-550 |
2.30e-49 |
|
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: 177.78 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLR-AAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKAIVVvsnfASTLEQVVDQTPVKNVIItglgdllsapkrtlvnfvvkyikrlvpkyslphaism 186
Cdd:cd12117 80 ELPAERLAFMLADAGAKVLLT----DRSLAGRAGGLEVAVVID------------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 rRALRAGKkAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqaNGAYAPLlNDGKEFVVTAlPL------Y 260
Cdd:cd12117 119 -EALDAGP-AGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK--NTNYVTL-GPDDRVLQTS-PLafdastF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 261 HIFAltvnCLLflhKGANnlLITNPRDIPGFVAELKKtpFTALTGVNT------LFNALVNSEEFAaldFSRLK-LSIGG 333
Cdd:cd12117 193 EIWG----ALL---NGAR--LVLAPKGTLLDPDALGA--LIAEEGVTVlwltaaLFNQLADEDPEC---FAGLReLLTGG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 334 GMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYD-LAGYNGS--IGLPAPSTQIQVRGDDGQVLPQGETGELFAK 410
Cdd:cd12117 259 EVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTeLDEVAGSipIGRPIANTRVYVLDEDGRPVPPGVPGELYVG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 411 GPQVMLGYWQRPEETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEV 484
Cdd:cd12117 339 GDGLALGYLNRPALTAERFVADPFGPgerlyrTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREA 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 485 AAVGVPHEVSGELVKIFVVAkDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd12117 419 VVVVREDAGGDKRLVAYVVA-EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
13-548 |
6.74e-49 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 177.39 E-value: 6.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 13 VPAEIDASRYAS-----LLEMLESAVNTYADQPAFV--NMGATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLL 85
Cdd:PRK05852 1 MRFMGGAAPMASdfgprIADLVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 86 QYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFAStlEQVVDQTPVKNVIITGLGDLLSAPKRTLVN 165
Cdd:PRK05852 80 EFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPH--DRAEPTTRWWPLTVNVGGDSGPSGGTLSVH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 166 fvvkyikrLVPKYSLPHAISMRRALRagkkaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApl 245
Cdd:PRK05852 158 --------LDAATEPTPATSTPEGLR--------------PDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYR-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 246 LNDGkEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPR-DIPGFVAELKKTPFTALTGVNTLFNALVN--SEEFAAL 322
Cdd:PRK05852 214 LSPR-DATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVGATWYTAVPTIHQILLEraATEPSGR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 323 DFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYN----GSIGLPAPST--QIQVRGDDG 396
Cdd:PRK05852 293 KPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIEGIGQTenpvVSTGLVGRSTgaQIRIVGSDG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 397 QVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PRK05852 373 LPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLA 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 477 LHPKVVEVAAVGVPHEVSGELVKIFVVAKDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRR 548
Cdd:PRK05852 452 SHPNVMEAAVFGVPDQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRR 524
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
48-555 |
2.19e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 174.97 E-value: 2.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQNDLKLQKgdRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVV 127
Cdd:PRK07638 26 VLTYKDWFESVCKVANWLNEKESKNK--TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 VSNFASTLEQVvdQTPVKnviitglgdLLSAPKRTLVNfvvkYIKRLVPKYSLPHAismrralragkkaqyvkPVvksdd 207
Cdd:PRK07638 104 ERYKLNDLPDE--EGRVI---------EIDEWKRMIEK----YLPTYAPIENVQNA-----------------PF----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 iaFLQYTGGTTGVSKGAMLSHGNIVANvLQANGAYAPLLNDGKefVVTALPLYHIfaltvnclLFLHKGANNL-----LI 282
Cdd:PRK07638 147 --YMGFTSGSTGKPKAFLRAQQSWLHS-FDCNVHDFHMKREDS--VLIAGTLVHS--------LFLYGAISTLyvgqtVH 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNPRDIPGFVAE-LKKTPFTALTGVNTLFNALVNSEEFaaLDFSRLKLSIGGgmavqravadKWQNITKTR--------- 352
Cdd:PRK07638 214 LMRKFIPNQVLDkLETENISVMYTVPTMLESLYKENRV--IENKMKIISSGA----------KWEAEAKEKiknifpyak 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKvIDKD 432
Cdd:PRK07638 282 LYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE-LNAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 433 GWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGElvkIFVVAKDKSLTEK 512
Cdd:PRK07638 361 GWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGE---KPVAIIKGSATKQ 437
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 655376187 513 ELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK07638 438 QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSWIE 480
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
24-550 |
3.84e-48 |
|
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: 174.44 E-value: 3.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVN 103
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLR-GLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 104 VNPLYTPRELKHQLVDSGAKAIVVvsnfastleqvvdqtpvknviitglgdllsapKRTLVNFvvkyikrlvpkYSLPHA 183
Cdd:cd05920 95 ALPSHRRSELSAFCAHAEAVAYIV--------------------------------PDRHAGF-----------DHRALA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 184 ISMRRALRagkkaqyvkpvvksdDIAFLQYTGGTTGVSKGAMLSHGNIVANVlqanGAYAPLLNDGKEFV-VTALPLYHI 262
Cdd:cd05920 132 RELAESIP---------------EVALFLLSGGTTGTPKLIPRTHNDYAYNV----RASAEVCGLDQDTVyLAVLPAAHN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 263 FALTVNCLL-FLHKGANNLLITNPRdiPGFVAEL-KKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRA 340
Cdd:cd05920 193 FPLACPGVLgTLLAGGRVVLAPDPS--PDAAFPLiEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 341 VADKWQNITKTRLLEGYGLTEAspLVacC------PYDLAGYngSIGLPA-PSTQIQVRGDDGQVLPQGETGELFAKGPQ 413
Cdd:cd05920 271 LARRVPPVLGCTLQQVFGMAEG--LL--NytrlddPDEVIIH--TQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 414 VMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEV 493
Cdd:cd05920 345 TIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 494 SGELVKIFVVAKDKSLTEKELIKHCRHH-LTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd05920 425 LGERSCAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
27-551 |
1.28e-47 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 175.37 E-value: 1.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGA-----TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVV 101
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 102 VNVNPLYTPRELKHQLVDSGAKAIVVVSNFA---------STLEQVVDQTP-VKNVIIT-GLG-DLLSAPKRTLVNFVVK 169
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkEEADKACAQCPtVEKVVVVrHLGnDFTPAKGRDLSYDEEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 170 yikrlvpKYSLPHAISMrralragkkaqyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDG 249
Cdd:cd05968 224 -------ETAGDGAERT-----------------ESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 250 KEFVVTAL-----PLYHIFALTVNCLLFLHKGANNLliTNPRDIPGFVAELKKTPFtaltGVN-TLFNALV--NSEEFAA 321
Cdd:cd05968 280 LLTWFTDLgwmmgPWLIFGGLILGATMVLYDGAPDH--PKADRLWRMVEDHEITHL----GLSpTLIRALKprGDAPVNA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 322 LDFSRLKLSIGGGMAVQravADKWQNITKTRLLE-----GY-GLTEASPLVACC----PYDLAGYNGsiglPAPSTQIQV 391
Cdd:cd05968 354 HDLSSLRVLGSTGEPWN---PEPWNWLFETVGKGrnpiiNYsGGTEISGGILGNvlikPIKPSSFNG----PVPGMKADV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 392 RGDDGQVLPqGETGELFAKGPQVML--GYWQRPE---ETAKVIDKDGWLAtGDIGYMDEKGFFYIVDRKKDMILVSGFNV 466
Cdd:cd05968 427 LDESGKPAR-PEVGELVLLAPWPGMtrGFWRDEDrylETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRV 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 467 FPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD----KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNV 542
Cdd:cd05968 505 GPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPgvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRN 584
|
....*....
gi 655376187 543 GKILRRELR 551
Cdd:cd05968 585 AKVMRRVIR 593
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
207-552 |
1.24e-46 |
|
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: 165.97 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANvlqANGAYAPLLNDGKEFVVTALPLYHI--FALTVNCLLflhkGANNLLITN 284
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLAS---AAGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLL----AGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 285 PRDipGFVAELKKTPFTALTGVNT-LFNALVNSEEFAALDfsRLKLSIGGGMAVQRAVADKW--QNItktRLLEGYGLTE 361
Cdd:cd17630 74 RNQ--ALAEDLAPPGVTHVSLVPTqLQRLLDSGQGPAALK--SLRAVLLGGAPIPPELLERAadRGI---PLYTTYGMTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 362 ASPLVACCPYDLAGyngsiglpapstqiqvRGDDGQVLPQGE-----TGELFAKGPQVMLGYWQRPEEtaKVIDKDGWLA 436
Cdd:cd17630 147 TASQVATKRPDGFG----------------RGGVGVLLPGRElriveDGEIWVGGASLAMGYLRGQLV--PEFNEDGWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 437 TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAkDKSLTEKELIK 516
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-RGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*.
gi 655376187 517 HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
38-550 |
2.37e-46 |
|
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: 168.64 E-value: 2.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLR-AEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVvsnfastleqvvdqTPvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd17643 81 ADSGPSLLLT--------------DP------------------------------------------------------ 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVAnVLQANGayaPLLNDGKEFVVTalpLYHIFALTVNC----LLFL 273
Cdd:cd17643 93 --------DDLAYVIYTSGSTGRPKGVVVSHANVLA-LFAATQ---RWFGFNEDDVWT---LFHSYAFDFSVweiwGALL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 HKGanNLLITNP---RDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN--- 347
Cdd:cd17643 158 HGG--RLVVVPYevaRSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGrfg 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITKTRLLEGYGLTEASPLV---ACCPYDLAGYNGS-IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:cd17643 236 LDRPQLVNMYGITETTVHVtfrPLDAADLPAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAK--VIDKDG--------------WLATGDIGYMdekgffyivDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAV 487
Cdd:cd17643 316 LTAErfVANPFGgpgsrmyrtgdlarRLPDGELEYL---------GRADEQVKIRGFRIELGEIEAALATHPSVRD-AAV 385
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 488 GVPHEVSGE--LVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17643 386 IVREDEPGDtrLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
48-552 |
3.34e-46 |
|
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: 171.34 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKaIVV 127
Cdd:cd05967 82 TYTYAELLDEVSRLAGVLRK-LGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK-LIV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 VSNFASTLEQVVDQTPVKNVIITGLGdllSAPKRTLVnfvvkYIKRLVPKYSLPHAISMR-RALRagKKAQYVKPV-VKS 205
Cdd:cd05967 160 TASCGIEPGKVVPYKPLLDKALELSG---HKPHHVLV-----LNRPQVPADLTKPGRDLDwSELL--AKAEPVDCVpVAA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGamlshgnivanVLQANGAYAPLLN-------------------D-----GKEFVVTAlPLYH 261
Cdd:cd05967 230 TDPLYILYTSGTTGKPKG-----------VVRDNGGHAVALNwsmrniygikpgdvwwaasDvgwvvGHSYIVYG-PLLH 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 262 iFALTVncllfLHKGannllitNPRDIPG------FVAELK-KTPFTALTGVNTLFNALVNSEEFAALDFSRLK-LSIGG 333
Cdd:cd05967 298 -GATTV-----LYEG-------KPVGTPDpgafwrVIEKYQvNALFTAPTAIRAIRKEDPDGKYIKKYDLSSLRtLFLAG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 334 gmavQRAVAD--KW-QNITKTRLLEGYGLTEA-SPLVACCP--YDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGEL 407
Cdd:cd05967 365 ----ERLDPPtlEWaENTLGVPVIDHWWQTETgWPITANPVglEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 408 FAKGP---QVMLGYWQRPE--ETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVV 482
Cdd:cd05967 441 VIKLPlppGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVA 520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 483 EVAAVGVPHEVSGELVKIFVVAK------DKSLtEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:cd05967 521 ECAVVGVRDELKGQVPLGLVVLKegvkitAEEL-EKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
23-552 |
2.37e-45 |
|
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: 167.84 E-value: 2.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQ-PAFVNMGAT---LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAG 98
Cdd:cd05906 10 RTLLELLLRAAERGPTKgITYIDADGSeefQSYQDLLEDARRLAAGLRQ-LGLRPGDSVILQFDDNEDFIPAFWACVLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 99 MVVVNVNPLYTPRE-------LKH--QLVDSGakaiVVVSNFAST--LEQVVDQTPVKNVIITGLGDLLSAPkrtlvnfv 167
Cdd:cd05906 89 FVPAPLTVPPTYDEpnarlrkLRHiwQLLGSP----VVLTDAELVaeFAGLETLSGLPGIRVLSIEELLDTA-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 168 vkyikrlvpkyslphaismrralragkkAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvLQANGAYAPLLN 247
Cdd:cd05906 157 ----------------------------ADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR-SAGKIQHNGLTP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 248 DGKEFV------VTALPLYHIFALTVNC--------------LLFLHkgannlLITNPR-DI---PGFvaelkktpftAL 303
Cdd:cd05906 208 QDVFLNwvpldhVGGLVELHLRAVYLGCqqvhvpteeiladpLRWLD------LIDRYRvTItwaPNF----------AF 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 304 TgvntLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWqnitkTRLLE-----------GYGLTEASPLV----AC 368
Cdd:cd05906 272 A----LLNDLLEEIEDGTWDLSSLRYLVNAGEAVVAKTIRRL-----LRLLEpyglppdairpAFGMTETCSGViysrSF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 369 CPYDLAGYN--GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEk 446
Cdd:cd05906 343 PTYDHSQALefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDN- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 447 GFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVE--VAAVGV--PHEVSGELVKIFVVAKDKSLTEKELIKHCRHHL 522
Cdd:cd05906 422 GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVrdPGAETEELAIFFVPEYDLQDALSETLRAIRSVV 501
|
570 580 590
....*....|....*....|....*....|....
gi 655376187 523 T---GYKVPKLVEF-RDELPKTNVGKILRRELRD 552
Cdd:cd05906 502 SrevGVSPAYLIPLpKEEIPKTSLGKIQRSKLKA 535
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-551 |
1.19e-44 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 170.35 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNdlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYTPRELK--HQ------L 117
Cdd:PRK05691 38 GVVLSYRDLDLRARTIAAALQA--RASFGDRAVLLFPSGPDYVAAFFGCLYAGVIAV---PAYPPESARrhHQerllsiI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQvvdqtpvknviitgLGDLL--SAPKRTLVNfvvkyikrlvpkyslphaismrrALRAGKK 195
Cdd:PRK05691 113 ADAEPRLLLTVADLRDSLLQ--------------MEELAaaNAPELLCVD-----------------------TLDPALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 196 AQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgKEFVVTALPLYHIFALTVNCLLFLHK 275
Cdd:PRK05691 156 EAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP-DDVIVSWLPLYHDMGLIGGLLQPIFS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANNLLITnprdiPGFVAElkkTPFTALTGVNT--------------LFNALVNSEEFAALDFSRLKLSIGGGMAVQ--- 338
Cdd:PRK05691 235 GVPCVLMS-----PAYFLE---RPLRWLEAISEyggtisggpdfayrLCSERVSESALERLDLSRWRVAYSGSEPIRqds 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 339 -RAVADKWQ--NITKTRLLEGYGLTEASPLVAccpydlAGYNG---------------------------SIGLPAPSTQ 388
Cdd:PRK05691 307 lERFAEKFAacGFDPDSFFASYGLAEATLFVS------GGRRGqgipaleldaealarnraepgtgsvlmSCGRSQPGHA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 389 IQ-VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKV-IDKDG--WLATGDIGYMDEkGFFYIVDRKKDMILVSGF 464
Cdd:PRK05691 381 VLiVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLGFLRD-GELFVTGRLKDMLIVRGH 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 465 NVFPNEVEEVVALHPKVV---EVAAVGVPHEvsGElVKIFVVAK-----DKSLTEKELIKHCRHHLTG--YKVPKLVEFR 534
Cdd:PRK05691 460 NLYPQDIEKTVEREVEVVrkgRVAAFAVNHQ--GE-EGIGIAAEisrsvQKILPPQALIKSIRQAVAEacQEAPSVVLLL 536
|
570
....*....|....*....
gi 655376187 535 D--ELPKTNVGKILRRELR 551
Cdd:PRK05691 537 NpgALPKTSSGKLQRSACR 555
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-557 |
1.61e-44 |
|
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: 169.65 E-value: 1.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 7 NSLPADVPAEidasryASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQ 86
Cdd:COG1020 466 NATAAPYPAD------ATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 87 YPIALFGVLRAGMVVVNVNPLYtPRE-LKHQLVDSGAKAIVVVSNFASTLeqvvdqtpvknviitglgdllsapkrtlvn 165
Cdd:COG1020 539 MVVALLAVLKAGAAYVPLDPAY-PAErLAYMLEDAGARLVLTQSALAARL------------------------------ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 166 fvvkyikrlvPKYSLPhAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNVLQANGAYAPL 245
Cdd:COG1020 588 ----------PELGVP-VLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV-NLLAWMQRRYGL 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 246 lndGKEFVVTAL-PL------YHIF-ALTVncllflhkGANnLLITNP---RDIPGFVAELKKTPFTALTGVNTLFNALV 314
Cdd:COG1020 656 ---GPGDRVLQFaSLsfdasvWEIFgALLS--------GAT-LVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALL 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 315 nseEFAALDFSRLKLSIGGGMAVQRAVADKWQNITK-TRLLEGYGLTEASPLVACCPYDLAGYNG---SIGLPAPSTQIQ 390
Cdd:COG1020 724 ---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPgARLVNLYGPTETTVDSTYYEVTPPDADGgsvPIGRPIANTRVY 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 391 VRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK--VIDKDG-----WLATGDIGYMDEKGFFYIVDRKKDMILVSG 463
Cdd:COG1020 801 VLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAErfVADPFGfpgarLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 464 FNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHC-RHHLTGYKVPKLVEFRDELPKTNV 542
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLAlALLLPPYMVPAAVVLLLPLPLTGN 960
|
570
....*....|....*
gi 655376187 543 GKILRRELRDEAKSA 557
Cdd:COG1020 961 GKLDRLALPAPAAAA 975
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
213-547 |
2.40e-44 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 159.88 E-value: 2.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 213 YTGGTTGVSKGAMLSHGN-IVANVLQANGayapLLNDGKEFVVTALPLYHIFALTvNCLLFLHKGANNLLITNpRDIPGF 291
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSwIESFVCNEDL----FNISGEDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRK-FNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 292 VAELKKTPFTALTGVNTLFNALVNSEEfaalDFSRLKLSIGGGMAVQRAVADKWQNIT-KTRLLEGYGLTEASPLVACCP 370
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALARTLE----PESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 371 YDLAGYNgSIGLPAPSTQIQVRGDDGqvlpqGETGELFAKGPQVMLGYWqrpeeTAKVIDKDGWLATGDIGYMDEKGFFY 450
Cdd:cd17633 157 QESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIGYVDEEGYLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 451 IVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVkIFVVAKDKsLTEKELIKHCRHHLTGYKVPKL 530
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGDK-LTYKQLKRFLKQKLSRYEIPKK 303
|
330
....*....|....*..
gi 655376187 531 VEFRDELPKTNVGKILR 547
Cdd:cd17633 304 IIFVDSLPYTSSGKIAR 320
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
49-517 |
9.41e-44 |
|
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: 163.54 E-value: 9.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFA-AYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYtprelkHQLvdsGAKAIvv 127
Cdd:cd05927 6 ISYKEVAERADNIGsALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTV---PLY------DTL---GPEAI-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 vsnfastlEQVVDQTPVKNVIITGlgdllsapkrtlvNFVVkyikrlvpkyslphaISMRRALRAGKKAQYVKPVVKSDD 207
Cdd:cd05927 72 --------EYILNHAEISIVFCDA-------------GVKV---------------YSLEEFEKLGKKNKVPPPPPKPED 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFV-VTALPLYHIFALTVNCLLFLHKGANNLLITNPR 286
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVyISYLPLAHIFERVVEALFLYHGAKIGFYSGDIR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 DIPGFVAELKKTPFTA--------LTGV-----------NTLFNALVNSEE-------------FAALDFSRLKLSIG-- 332
Cdd:cd05927 196 LLLDDIKALKPTVFPGvprvlnriYDKIfnkvqakgplkRKLFNFALNYKLaelrsgvvraspfWDKLVFNKIKQALGgn 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 333 ------GGMAVQRAVADKWQNITKTRLLEGYGLTEASplVACC---PYDLAgyNGSIGLPAPSTQIQ----------VRG 393
Cdd:cd05927 276 vrlmltGSAPLSPEVLEFLRVALGCPVLEGYGQTECT--AGATltlPGDTS--VGHVGGPLPCAEVKlvdvpemnydAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 394 DDGqvlpqgeTGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMI-LVSGFNVFPNEVE 472
Cdd:cd05927 352 PNP-------RGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIE 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 473 EVVALHPKVVEVAAVGVPHEVSgeLVKIFVV--------AKDKSLTEK---ELIKH 517
Cdd:cd05927 425 NIYARSPFVAQIFVYGDSLKSF--LVAIVVPdpdvlkewAASKGGGTGsfeELCKN 478
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
4-551 |
9.98e-44 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 164.02 E-value: 9.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 4 PWINSLP---ADVPAEIDASRYASLLEmleSAVNTYAdqpAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIM 80
Cdd:PRK09192 8 PTTSSLPrryADFPTLVEALDYAALGE---AGMNFYD---RRGQLEEALPYQTLRARAEAGARRLLA-LGLKPGDRVALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVnvnPLYTP-----RE-----LKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIIT 150
Cdd:PRK09192 81 AETDGDFVEAFFACQYAGLVPV---PLPLPmgfggREsyiaqLRGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 151 GLGDLLSAPKRTLvnfvvkyikrlvpkyslphaismrralragkkaqyvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGN 230
Cdd:PRK09192 158 AWFKALPEADVAL-------------------------------------PRPTPDDIAYLQYSSGSTRFPRGVIITHRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 231 IVANvLQANGAYAPLLNDGKEfVVTALPLYHIFALtVNCllFLHKGANNL-------------------LIT-NPRDI-- 288
Cdd:PRK09192 201 LMAN-LRAISHDGLKVRPGDR-CVSWLPFYHDMGL-VGF--LLTPVATQLsvdylptrdfarrplqwldLISrNRGTIsy 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 289 -PGFVAELkktpfTALTgvntlfnalVNSEEFAALDFSRLKLS-IGGGMA---VQRAVADKWQ--NITKTRLLEGYGLTE 361
Cdd:PRK09192 276 sPPFGYEL-----CARR---------VNSKDLAELDLSCWRVAgIGADMIrpdVLHQFAEAFApaGFDDKAFMPSYGLAE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 362 A------SPL------------------VACCPYDLAGYNGSI---GLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQV 414
Cdd:PRK09192 342 AtlavsfSPLgsgivveevdrdrleyqgKAVAPGAETRRVRTFvncGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSL 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 415 MLGYWqRPEETAKVIDKDGWLATGDIGYMDEkGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVV--EVAAVGVPHE 492
Cdd:PRK09192 422 MSGYF-RDEESQDVLAADGWLDTGDLGYLLD-GYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQE 499
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 493 vSGELVKIFVVAKDKSLTEKELIKHCRHHL--TGYKVPKLVEF--RDELPKTNVGKILRRELR 551
Cdd:PRK09192 500 -NGEKIVLLVQCRISDEERRGQLIHALAALvrSEFGVEAAVELvpPHSLPRTSSGKLSRAKAK 561
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
50-555 |
1.91e-43 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 162.61 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQND-LKLqkGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVV 128
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDgIKL--GDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SNFASTLEQVVDQTP-VKNVIItgLGDllsapkrtlvnfvvkyiKRLVPKYSLPHAISMRRALrAGKKAQYVKPVVKSDD 207
Cdd:PRK06018 119 LTFVPILEKIADKLPsVERYVV--LTD-----------------AAHMPQTTLKNAVAYEEWI-AEADGDFAWKTFDENT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApLLNDGKEFVVTALPLYHIFA--LTVNCLLflhKGANnLLITNP 285
Cdd:PRK06018 179 AAGMCYTSGTTGDPKGVLYSHRSNVLHALMANNGDA-LGTSAADTMLPVVPLFHANSwgIAFSAPS---MGTK-LVMPGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 RDIPGFVAEL---KKTPFTAltGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNItKTRLLEGYGLTEA 362
Cdd:PRK06018 254 KLDGASVYELldtEKVTFTA--GVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVACC----PYDLAGYNGSI------GLPAPSTQIQVRGDDGQVLP-QGET-GELFAKGPQVMLGYWQrpeETAKVID 430
Cdd:PRK06018 331 SPLGTLAalkpPFSKLPGDARLdvlqkqGYPPFGVEMKITDDAGKELPwDGKTfGRLKVRGPAVAAAYYR---VDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 431 KDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK-DKSL 509
Cdd:PRK06018 408 DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKpGETA 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 510 TEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK06018 488 TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFK 533
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
38-550 |
3.23e-43 |
|
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: 160.53 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYtPRE-LKHQ 116
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLR-ARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY-PADrLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 117 LVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPkrtlvnfvvkyikrlvpkyslphaismrralragkka 196
Cdd:cd12116 80 LEDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTP------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 197 qyvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNVLQANGAyAPLLNDGKEFVVTALPLYHIFALTVncLLFLHKG 276
Cdd:cd12116 123 ------VSPDDLAYVIYTSGSTGRPKGVVVSHRNLV-NFLHSMRE-RLGLGPGDRLLAVTTYAFDISLLEL--LLPLLAG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 AnnLLITNPRDI---PGFVAELKKTP-FTALTGVNTLFNALVNSEEFAAldfSRLKLsIGGGMAVQRAVADKWQNiTKTR 352
Cdd:cd12116 193 A--RVVIAPRETqrdPEALARLIEAHsITVMQATPATWRMLLDAGWQGR---AGLTA-LCGGEALPPDLAARLLS-RVGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKD 432
Cdd:cd12116 266 LWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 433 GWLA-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKiFVVAK 505
Cdd:cd12116 346 PFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVA-YVVLK 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 506 D-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd12116 425 AgAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
38-550 |
6.08e-43 |
|
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: 160.13 E-value: 6.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17646 13 DAPAVVDEGRTLTYRELDERANRLAHLLR-ARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKaivvvsnfastleqvvdqtpvknVIITGlGDLLSAPKRTLVNFVVKYIKRLVPKYSLPhaismrralragkkaq 197
Cdd:cd17646 92 ADAGPA-----------------------VVLTT-ADLAARLPAGGDVALLGDEALAAPPATPP---------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYaPLlnDGKEFVVTALPLYhiFALTVNCLLF-LHKG 276
Cdd:cd17646 132 --LVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEY-PL--GPGDRVLQKTPLS--FDVSVWELFWpLVAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANnLLITNP---RDIPGFVAELKKTPFTALTGVNTLFNALVnsEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRL 353
Cdd:cd17646 205 AR-LVVARPgghRDPAYLAALIREHGVTTCHFVPSMLRVFL--AEPAAGSCASLRRVFCSGEALPPELAARFLALPGAEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 LEGYGLTEASPLVACCPYDLAGYNGS--IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK--VI 429
Cdd:cd17646 282 HNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAErfVP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 DKDG----WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGE-LVKIFVVA 504
Cdd:cd17646 362 DPFGpgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArLVGYVVPA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 655376187 505 KDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17646 442 AGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
50-555 |
8.85e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 160.64 E-value: 8.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS 129
Cdd:PRK07008 41 TYRDCERRAKQLAQAL-AALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 NFASTLEQVVDQTPvknviitglgdllsapkrTLVNFVVKYIKRLVPKYSLPhaISMRRALRAGKKAQYVKPVVKSDDIA 209
Cdd:PRK07008 120 TFLPLVDALAPQCP------------------NVKGWVAMTDAAHLPAGSTP--LLCYETLVGAQDGDYDWPRFDENQAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 210 FLQYTGGTTGVSKGAMLSHGNIVANvlqangAYAPLLNDG-----KEFVVTALPLYHIFA--LTVNCLLflhKGANnLLI 282
Cdd:PRK07008 180 SLCYTSGTTGNPKGALYSHRSTVLH------AYGAALPDAmglsaRDAVLPVVPMFHVNAwgLPYSAPL---TGAK-LVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNPrDIPG-FVAEL---KKTPFTAltGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYG 358
Cdd:PRK07008 250 PGP-DLDGkSLYELieaERVTFSA--GVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASPLVACCPYDlagyNGSIGLPaPSTQIQVR---------------GDDGQVLP-QGET-GELFAKGPQVMLGYWQR 421
Cdd:PRK07008 327 MTEMSPLGTLCKLK----WKHSQLP-LDEQRKLLekqgrviygvdmkivGDDGRELPwDGKAfGDLQVRGPWVIDRYFRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 422 peETAKVIDkdGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIF 501
Cdd:PRK07008 402 --DASPLVD--GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLV 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 655376187 502 VVAKDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK07008 478 VVKRPGAeVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
207-547 |
9.10e-43 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 155.88 E-value: 9.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVVtaLPLYHIFALTVNCLLFLHKGANNLLITNpR 286
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLP--LPATHIGGLWWILTCLIHGGLCVTGGEN-T 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGmavQRAVADKWQNIT---KTRLLEGYGLTEAS 363
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGG---SRAIAADVRFIEatgLTNTAQVYGLSETG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 364 PlVACCPYDLAGYN-GSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGY 442
Cdd:cd17635 156 T-ALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 443 MDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVA---KDKSLTeKELIKHCR 519
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAsaeLDENAI-RALKHTIR 312
|
330 340
....*....|....*....|....*...
gi 655376187 520 HHLTGYKVPKLVEFRDELPKTNVGKILR 547
Cdd:cd17635 313 RELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
27-546 |
3.07e-41 |
|
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: 156.97 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGA------TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMV 100
Cdd:cd17634 57 NALDRHLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 101 VVNVNPLYTPRELKHQLVDSGAKAIVVVSNFAS-----TLEQVVDQ------TPVKNVIITglgdllsapKRTLVnfvvk 169
Cdd:cd17634 136 HSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRagrsvPLKKNVDDalnpnvTSVEHVIVL---------KRTGS----- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 170 yikrlvPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGnivANVLQANGAYAPLLNDG 249
Cdd:cd17634 202 ------DIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTG---GYLVYAATTMKYVFDYG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 250 K-EFVVTALPL-------YHIFA-LTVNCLLFLHKGANNllitNPrDIPGFVAELKKTPFTALTGVNTLFNALV--NSEE 318
Cdd:cd17634 273 PgDIYWCTADVgwvtghsYLLYGpLACGATTLLYEGVPN----WP-TPARMWQVVDKHGVNILYTAPTAIRALMaaGDDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 319 FAALDFSRLKLSIGGGMAVQ-RAVADKWQNITKTR--LLEGYGLTEASPlvACCPyDLAG----YNGSIGLPAPSTQIQV 391
Cdd:cd17634 348 IEGTDRSSLRILGSVGEPINpEAYEWYWKKIGKEKcpVVDTWWQTETGG--FMIT-PLPGaielKAGSATRPVFGVQPAV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 392 RGDDGQVLPQGETGELF--AKGPQVMLGYWQRPEETAKVIDK--DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVF 467
Cdd:cd17634 425 VDNEGHPQPGGTEGNLVitDPWPGQTRTLFGDHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLG 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 468 PNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK----DKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVG 543
Cdd:cd17634 505 TAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvePSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSG 584
|
...
gi 655376187 544 KIL 546
Cdd:cd17634 585 KIM 587
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
6-555 |
2.34e-40 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 154.23 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 6 INSLPADvpaeidASRYASL--LEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPN 83
Cdd:PLN02479 7 IDDLPKN------AANYTALtpLWFLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASAL-AKRSIGPGSTVAVIAPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 84 LLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDqtpvknvIITGlgDLLSAPKRTL 163
Cdd:PLN02479 80 IPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVMVDQEFFTLAEEALK-------ILAE--KKKSSFKPPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 164 VnfVVKYIKRLVPKySLPHA-----ISMRRALRAGKKAQYVKPVVKS-DDIAfLQYTGGTTGVSKGAMLSHGNivANVLQ 237
Cdd:PLN02479 151 L--IVIGDPTCDPK-SLQYAlgkgaIEYEKFLETGDPEFAWKPPADEwQSIA-LGYTSGTTASPKGVVLHHRG--AYLMA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 238 ANGAYAPLLNDGKEFVVTaLPLYHIFALTVNCLLFLHKGANNLLitnpRDIP--GFVAELKKTPFTALTGVNTLFNALVN 315
Cdd:PLN02479 225 LSNALIWGMNEGAVYLWT-LPMFHCNGWCFTWTLAALCGTNICL----RQVTakAIYSAIANYGVTHFCAAPVVLNTIVN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 316 S-EEFAALDFSRLKLSIGGGMA----VQRAVADKWQNITKTrllegYGLTEA-SPLVACC---------PYDLAGYNGS- 379
Cdd:PLN02479 300 ApKSETILPLPRVVHVMTAGAApppsVLFAMSEKGFRVTHT-----YGLSETyGPSTVCAwkpewdslpPEEQARLNARq 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 380 ----IGLPA-----PSTQIQVRGDdgqvlpqGET-GELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFF 449
Cdd:PLN02479 375 gvryIGLEGldvvdTKTMKPVPAD-------GKTmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYI 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 450 YIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK------DKSLTEKELIKHCRHHLT 523
Cdd:PLN02479 447 EIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKpgvdksDEAALAEDIMKFCRERLP 526
|
570 580 590
....*....|....*....|....*....|..
gi 655376187 524 GYKVPKLVEFrDELPKTNVGKILRRELRDEAK 555
Cdd:PLN02479 527 AYWVPKSVVF-GPLPKTATGKIQKHVLRAKAK 557
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
29-554 |
5.66e-40 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 153.49 E-value: 5.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 29 LESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLY 108
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAA-ARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 109 TPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPkRTLVNFvvkyikrlvpkyslphaisMRR 188
Cdd:PRK08279 122 RGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGDTLDDP-EGYEDL-------------------AAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 189 ALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGnivaNVLQANGAYAPLLNDGKEFVV-TALPLYHIFALTV 267
Cdd:PRK08279 182 AAGAPTTNPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHM----RWLKAMGGFGGLLRLTPDDVLyCCLPLYHNTGGTV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 268 nCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEfAALDFS-RLKLSIGGGMavQRAVADKWQ 346
Cdd:PRK08279 258 -AWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCRYLLNQPP-KPTDRDhRLRLMIGNGL--RPDIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NITKT-RLLEGYGLTEA----------------SPLVACCPYDLAGYNGSIGLPapstqiqVRGDDG--QVLPQGETGEL 407
Cdd:PRK08279 334 QRFGIpRILEFYAASEGnvgfinvfnfdgtvgrVPLWLAHPYAIVKYDVDTGEP-------VRDADGrcIKVKPGEVGLL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 408 FAK----GPqvMLGYWQrPEETAKVI------DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVAL 477
Cdd:PRK08279 407 IGRitdrGP--FDGYTD-PEASEKKIlrdvfkKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 478 HPKVVEVAAVGVphEVSGE-----LVKIfVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:PRK08279 484 FPGVEEAVVYGV--EVPGTdgragMAAI-VLADGAEFDLAALAAHLYERLPAYAVPLFVRLVPELETTGTFKYRKVDLRK 560
|
..
gi 655376187 553 EA 554
Cdd:PRK08279 561 EG 562
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-551 |
1.23e-39 |
|
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: 149.98 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYT---PRELKHQLVDSGAKai 125
Cdd:cd05973 1 LTFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQ---PLFTafgPKAIEHRLRTSGAR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNFAStleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismRRALragkkaqyvkpvvkS 205
Cdd:cd05973 75 LVVTDAAN-----------------------------------------------------RHKL--------------D 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVAnvLQANGAYAPLLNDGKEFVVTALP-----LYhiFALTVNCLLflhkGANNL 280
Cdd:cd05973 88 SDPFVMMFTSGTTGLPKGVPVPLRALAA--FGAYLRDAVDLRPEDSFWNAADPgwaygLY--YAITGPLAL----GHPTI 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 281 LITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNS-EEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGL 359
Cdd:cd05973 160 LLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAgAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 360 TEASpLVACCPYDLAG--YNGSIGLPAPSTQIQVRGDDGQVLPQGETGEL---FAKGPQVML-GYWQRPEETAKvidkDG 433
Cdd:cd05973 240 TELG-MVLANHHALEHpvHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLaidIANSPLMWFrGYQLPDTPAID----GG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 434 WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD----KSL 509
Cdd:cd05973 315 YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGghegTPA 394
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 655376187 510 TEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05973 395 LADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLR 436
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-555 |
1.95e-39 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 151.94 E-value: 1.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 33 VNTYADQPAF------VNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd05966 63 LKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLK-SLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKAIVVVSNF-----ASTLEQVVDQ-----TPVKNVII---TGlGDLLSAPKRTLvnfvvkYIKR 173
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGGyrggkVIPLKEIVDEalekcPSVEKVLVvkrTG-GEVPMTEGRDL------WWHD 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 174 LVPKYSlphaismrralragkkaQYVKPV-VKSDDIAFLQYTGGTTGVSKGAMLSHGnivANVLQAN------------- 239
Cdd:cd05966 215 LMAKQS-----------------PECEPEwMDSEDPLFILYTSGSTGKPKGVVHTTG---GYLLYAAttfkyvfdyhpdd 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 240 ----------------GAYAPLLNDGKEFVVTALPLYhifaltvncllflhkgannlliTNPRDIPGFVAELKKTPF-TA 302
Cdd:cd05966 275 iywctadigwitghsyIVYGPLANGATTVMFEGTPTY----------------------PDPGRYWDIVEKHKVTIFyTA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 303 LTGVNTLFNAlvNSEEFAALDFSRLKL--SIGGGMAVQravADKW--QNITKTR--LLEGYGLTEA-----SPLVACCPY 371
Cdd:cd05966 333 PTAIRALMKF--GDEWVKKHDLSSLRVlgSVGEPINPE---AWMWyyEVIGKERcpIVDTWWQTETggimiTPLPGATPL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 372 DlagyNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKG--PQVMLGYW---QRPEETA-KVIDkdGWLATGDIGYMDE 445
Cdd:cd05966 408 K----PGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRpwPGMARTIYgdhERYEDTYfSKFP--GYYFTGDGARRDE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 446 KGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD----KSLTEKELIKHCRHH 521
Cdd:cd05966 482 DGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDgeepSDELRKELRKHVRKE 561
|
570 580 590
....*....|....*....|....*....|....
gi 655376187 522 LTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:cd05966 562 IGPIATPDKIQFVPGLPKTRSGKIMRRILRKIAA 595
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
26-556 |
2.90e-39 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 151.33 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 26 LEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVN 105
Cdd:PLN03102 17 ITFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLIS-LNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPIN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 106 PLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVV------DQTPVKNVIITGLGDLLSAPKRTLVNFVVkYIKRLVPKYS 179
Cdd:PLN03102 96 TRLDATSIAAILRHAKPKILFVDRSFEPLAREVLhllsseDSNLNLPVIFIHEIDFPKRPSSEELDYEC-LIQRGEPTPS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 180 LphAISMRRalragkkaqyvkpVVKSDDIAFLQYTGGTTGVSKGAMLSHgnivanvlqaNGAYAPLLND--GKEF----- 252
Cdd:PLN03102 175 L--VARMFR-------------IQDEHDPISLNYTSGTTADPKGVVISH----------RGAYLSTLSAiiGWEMgtcpv 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 253 VVTALPLYHIFALTVNCLLFLHKGANNLL--ITNPRdipgFVAELKKTPFTALTGVNTLFNALvnseefaaLDFSRLKLS 330
Cdd:PLN03102 230 YLWTLPMFHCNGWTFTWGTAARGGTSVCMrhVTAPE----IYKNIEMHNVTHMCCVPTVFNIL--------LKGNSLDLS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 331 --------IGGGMAVQRAVADKWQNItKTRLLEGYGLTEASPLVACCPY-------------DLAGYNG--SIGLpapsT 387
Cdd:PLN03102 298 prsgpvhvLTGGSPPPAALVKKVQRL-GFQVMHAYGLTEATGPVLFCEWqdewnrlpenqqmELKARQGvsILGL----A 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 388 QIQVRGDDGQ--VLPQGET-GELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGF 464
Cdd:PLN03102 373 DVDVKNKETQesVPRDGKTmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 465 NVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAK----------DKSLT-EKELIKHCRHHLTGYKVPKLVEF 533
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEkgettkedrvDKLVTrERDLIEYCRENLPHFMCPRKVVF 531
|
570 580
....*....|....*....|...
gi 655376187 534 RDELPKTNVGKILRRELRDEAKS 556
Cdd:PLN03102 532 LQELPKNGNGKILKPKLRDIAKG 554
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
48-556 |
3.99e-39 |
|
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: 149.23 E-value: 3.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYtPRELKHQLV-DSGAKaIV 126
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLR-SLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH-PLQRLQEILqDTGAK-VV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvKSD 206
Cdd:cd05918 101 LTS--------------------------------------------------------------------------SPS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVLqangAYAPLLNDGKE----------FVVTalpLYHIF-ALTVNCLLFLhk 275
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHRALSTSAL----AHGRALGLTSEsrvlqfasytFDVS---ILEIFtTLAAGGCLCI-- 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 gANNLLITNprDIPGFVAELKktpftaltgVNTLFnaLVNSeeFAAL----DFSRLKLSIGGGMAVQRAVADKWQNitKT 351
Cdd:cd05918 178 -PSEEDRLN--DLAGFINRLR---------VTWAF--LTPS--VARLldpeDVPSLRTLVLGGEALTQSDVDTWAD--RV 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVR-GDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKV-I 429
Cdd:cd05918 240 RLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGATCWVVDpDNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAfI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 DKDGWLA------------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:cd05918 320 EDPAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSS 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 498 VKI---FVVAKDKSLTE------------------KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAKS 556
Cdd:cd05918 400 SPQlvaFVVLDGSSSGSgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
27-550 |
6.65e-39 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 148.63 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKAIVVVSNFastleqvvdqtpVKNVIITGLGDLLSapkrtlvnfvvkyikrlvpkyslphaism 186
Cdd:cd17655 80 DYPEERIQYILEDSGADILLTQSHL------------QPPIAFIGLIDLLD----------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 RRALRAGKKAQyVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYapLLNDGKEFVVTAlPLYhiFALT 266
Cdd:cd17655 119 EDTIYHEESEN-LEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVI--YQGEHLRVALFA-SIS--FDAS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 267 VNClLFLHKGANNLLITNPR----DIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLklsIGGGMAVQRAVA 342
Cdd:cd17655 193 VTE-IFASLLSGNTLYIVRKetvlDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKHL---IVGGEALSTELA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 343 DKW--QNITKTRLLEGYGLTEAsplVACC---PYDLAGYNG---SIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQV 414
Cdd:cd17655 269 KKIieLFGTNPTITNAYGPTET---TVDAsiyQYEPETDQQvsvPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 415 MLGYWQRPEETA-KVID----------KDG----WLATGDIGYMdekgffyivDRKKDMILVSGFNVFPNEVEEVVALHP 479
Cdd:cd17655 346 ARGYLNRPELTAeKFVDdpfvpgermyRTGdlarWLPDGNIEFL---------GRIDHQVKIRGYRIELGEIEARLLQHP 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 480 KVVEvAAVGVPHEVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17655 417 DIKE-AVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
30-551 |
1.24e-38 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 149.55 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 30 ESAVNTYADQPAfvnmgATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYT 109
Cdd:PRK05620 25 DTTVTTWGGAEQ-----EQTTFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 110 PRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTP-VKNVIITGLGDLLSAPKRTLVNFVVkyikrlvpkYSLphaismrR 188
Cdd:PRK05620 100 NDQIVHIINHAEDEVIVADPRLAEQLGEILKECPcVRAVVFIGPSDADSAAAHMPEGIKV---------YSY-------E 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 189 ALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVVtALPLYHIFALTVN 268
Cdd:PRK05620 164 ALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTDSLAVTHGESFLC-CVPIYHVLSWGVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 CLLFLhKGAnNLLITNPRDIPGFVAELKKT--PFTAlTGVNTLFNALV-----NSEEfaaldfsRLKLS--IGGGMAVQR 339
Cdd:PRK05620 243 LAAFM-SGT-PLVFPGPDLSAPTLAKIIATamPRVA-HGVPTLWIQLMvhylkNPPE-------RMSLQeiYVGGSAVPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 340 AVADKWQNITKTRLLEGYGLTEASPL--VACCPYDLAG-----YNGSIGLPAPSTQIQVRgDDGQVLPQGE--TGELFAK 410
Cdd:PRK05620 313 ILIKAWEERYGVDVVHVWGMTETSPVgtVARPPSGVSGearwaYRVSQGRFPASLEYRIV-NDGQVMESTDrnEGEIQVR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 411 GPQVMLGYWQRP----------------EETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEV 474
Cdd:PRK05620 392 GNWVTASYYHSPteegggaastfrgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 475 VALHPKVVEVAAVGVPHEVSGEL-VKIFVVAKDKSLTE---KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK05620 472 IMAAPEVVECAVIGYPDDKWGERpLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
.
gi 655376187 551 R 551
Cdd:PRK05620 552 R 552
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
206-556 |
7.57e-38 |
|
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: 146.09 E-value: 7.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApllNDGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNP 285
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTE---WKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 RDIPGFVAELKKTPFTALTGVNT------LFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKW------QNITKTRL 353
Cdd:cd05908 183 LFIRRPILWLKKASEHKATIVSSpnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFldhmskYGLKRNAI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 LEGYGLTEAS--------------------------PLVACCPYDLAGYNG-SIGLPAPSTQIQVRGDDGQVLPQGETGE 406
Cdd:cd05908 263 LPVYGLAEASvgaslpkaqspfktitlgrrhvthgePEPEVDKKDSECLTFvEVGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 407 LFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMdEKGFFYIVDRKKDMILVSGFNVFPNEVEEV-VALHPKVV-EV 484
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIaEELEGVELgRV 421
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 485 AAVGV-PHEVSGELVKIFVVAKDKSLTEKELIKHCRHHL---TGYKVPKLVEFRdELPKTNVGKILRRELRDEAKS 556
Cdd:cd05908 422 VACGVnNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLnkrGGWQINEVLPIR-RIPKTTSGKVKRYELAQRYQS 496
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
23-505 |
1.31e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 146.63 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQPAFVNM-------GA--TLTYRKLEERSRAFAAYLQndLKLQKGDRVAIMMPNLLQYPIALFG 93
Cdd:PRK05850 1 SSVPSLLRERASLQPDDAAFTFIdyeqdpaGVaeTLTWSQLYRRTLNVAEELR--RHGSTGDRAVILAPQGLEYIVAFLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 94 VLRAGMVVVnvnPLYTPRelkhqlvdsgakaivvvsnFASTLEQVV----DQTPVknVIITglgdlLSApkrtLVNFVVK 169
Cdd:PRK05850 79 ALQAGLIAV---PLSVPQ-------------------GGAHDERVSavlrDTSPS--VVLT-----TSA----VVDDVTE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 170 YIKRLvPKYSLPHAISMRrALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYapLLNDG 249
Cdd:PRK05850 126 YVAPQ-PGQSAPPVIEVD-LLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDY--FGDTG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 250 KE-----FVVTALPLYH-------IFA---------LTvNCLLFLHKGAN--NLLITNPRDI---PGFVAEL--KKTpft 301
Cdd:PRK05850 202 GVpppdtTVVSWLPFYHdmglvlgVCApilggcpavLT-SPVAFLQRPARwmQLLASNPHAFsaaPNFAFELavRKT--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 302 altgvntlfnalvNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQ------NITKTRLLEGYGLTEASPLVAC------- 368
Cdd:PRK05850 278 -------------SDDDMAGLDLGGVLGIISGSERVHPATLKRFAdrfapfNLRETAIRPSYGLAEATVYVATrepgqpp 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 369 -----------------CPYD----LAGYngsiGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEET-- 425
Cdd:PRK05850 345 esvrfdyeklsaghakrCETGggtpLVSY----GSPRSPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETer 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 426 ---AKVIDK-----DG-WLATGDIGYMDEkGFFYIVDRKKDMILVSGFNVFPNEVEEVVAlhpkvvE-----VAAVGVPH 491
Cdd:PRK05850 421 tfgATLVDPspgtpEGpWLRTGDLGFISE-GELFIVGRIKDLLIVDGRNHYPDDIEATIQ------EitggrVAAISVPD 493
|
570
....*....|....
gi 655376187 492 EVSGELVKIFVVAK 505
Cdd:PRK05850 494 DGTEKLVAIIELKK 507
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-550 |
3.25e-37 |
|
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: 143.95 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDqtpvknvIITGLGDLLSAPkrtlvnfvvkyikrlvpkyslphaismrralragkkAQ 197
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFD-------VLILDLDALAAP------------------------------------AP 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 YVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApllnDGKEFVVTA-------LPLYHIFALtvncl 270
Cdd:cd12114 118 PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFA----VGPDDRVLAlsslsfdLSVYDIFGA----- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 lfLHKGANNLLITNPRDI-PGFVAELKKT-PFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNI 348
Cdd:cd12114 189 --LSAGATLVLPDEARRRdPAHWAELIERhGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLLSGDWIPLDLPARLRAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 349 TK-TRLLEGYGLTEAS------PLVACCPYDlagynGSI--GLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYW 419
Cdd:cd12114 267 APdARLISLGGATEASiwsiyhPIDEVPPDW-----RSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYL 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 420 QRPEETAK--VIDKDG--WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSG 495
Cdd:cd12114 342 GDPELTAArfVTHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGK 421
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 496 ELVKiFVVAKDK--SLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd12114 422 RLAA-FVVPDNDgtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
46-545 |
1.81e-36 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 145.11 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNDLKLqkGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNplYTprelkhqlvdSGAKAI 125
Cdd:PRK06814 656 NGPLTYRKLLTGAFVLGRKLKKNTPP--GENVGVMLPNANGAAVTFFALQSAGRVPAMIN--FS----------AGIANI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVvsnfASTLEQVvdqtpvkNVIIT--------GLGDLLSApkrtlVNFVVK--YIKRLVPKYSLPHAIsmrRALRAGKK 195
Cdd:PRK06814 722 LS----ACKAAQV-------KTVLTsrafiekaRLGPLIEA-----LEFGIRiiYLEDVRAQIGLADKI---KGLLAGRF 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 196 AQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAnGAYAPLLNDGKEFvvTALPLYHIFALTVNCLLFLHK 275
Cdd:PRK06814 783 PLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQV-AARIDFSPEDKVF--NALPVFHSFGLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANNLLITNP---RDIPGFVAElkkTPFTALTGVNTLFNALVNSEefAALDFSRLKLSIGGGMAVQRAVADKWQNITKTR 352
Cdd:PRK06814 860 GVKVFLYPSPlhyRIIPELIYD---TNATILFGTDTFLNGYARYA--HPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIR 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 353 LLEGYGLTEASPLVAC-CP-YDLAGYNGSIgLPApstqIQVRGDDGQVLPQGetGELFAKGPQVMLGYWQrpEETAKVID 430
Cdd:PRK06814 935 ILEGYGVTETAPVIALnTPmHNKAGTVGRL-LPG----IEYRLEPVPGIDEG--GRLFVRGPNVMLGYLR--AENPGVLE 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 431 --KDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGElvKIFVVAKDKS 508
Cdd:PRK06814 1006 ppADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGE--RIILLTTASD 1083
|
490 500 510
....*....|....*....|....*....|....*...
gi 655376187 509 LTEKELIKHCRHH-LTGYKVPKLVEFRDELPKTNVGKI 545
Cdd:PRK06814 1084 ATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKI 1121
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
29-551 |
2.74e-36 |
|
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: 141.33 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 29 LESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLY 108
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRA-RGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 109 TPRELKHQLVDSGAKaiVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKRtlvnfvvkyikrlvpkyslphaismrr 188
Cdd:cd17651 80 PAERLAFMLADAGPV--LVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPD--------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 189 alragkkaqyvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNiVANVLQANGAYAPLlNDGKEFVVTALPLYHIFALTVn 268
Cdd:cd17651 131 ------------PALDADDLAYVIYTSGSTGRPKGVVMPHRS-LANLVAWQARASSL-GPGARTLQFAGLGFDVSVQEI- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 cLLFLHKGANNLLITNP--RDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLK-LSIGG-----GMAVQRA 340
Cdd:cd17651 196 -FSTLCAGATLVLPPEEvrTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRyLLTGGeqlvlTEDLREF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 341 VADkwqnITKTRLLEGYGLTEASplVACC---PYDLAGYNG--SIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVM 415
Cdd:cd17651 275 CAG----LPGLRLHNHYGPTETH--VVTAlslPGDPAAWPAppPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 416 LGYWQRPEETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGV 489
Cdd:cd17651 349 RGYLNRPELTAERFVPDPFVPgarmyrTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVRE-AVVLA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655376187 490 PHEVSGE--LVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd17651 428 REDRPGEkrLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
27-552 |
2.84e-36 |
|
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: 140.14 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLL-QLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKAIVVVSNfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaism 186
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLTTDS-------------------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 rralragkkaqyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIvANVLQANGAyapllndgkefvvtalplyhifalt 266
Cdd:cd17653 104 ------------------PDDLAYIIFTSGSTGIPKGVMVPHRGV-LNYVSQPPA------------------------- 139
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 267 vncLLFLHKGANNLLITNPrdipGFVAelkktpftaltGVNTLFNALVN---------SEEFAAL--------------- 322
Cdd:cd17653 140 ---RLDVGPGSRVAQVLSI----AFDA-----------CIGEIFSTLCNggtlvladpSDPFAHVartvdalmstpsils 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 323 -----DFSRLKLSIGGGMAVQRAVADKWQNitKTRLLEGYGLTEASplvACCPYD--LAGYNGSIGLPAPSTQIQVRGDD 395
Cdd:cd17653 202 tlspqDFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECT---ISSTMTelLPGQPVTIGKPIPNSTCYILDAD 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 396 GQVLPQGETGELFAKGPQVMLGYWQRPEETAK----VIDKDGWL--ATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPN 469
Cdd:cd17653 277 LQPVPEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRmyRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLE 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 470 EVEEVVALHPKVVEVAAVGVpheVSGELVKiFVVAkdKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRE 549
Cdd:cd17653 357 EIEEVVLQSQPEVTQAAAIV---VNGRLVA-FVTP--ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKA 430
|
...
gi 655376187 550 LRD 552
Cdd:cd17653 431 LRE 433
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
49-524 |
6.44e-36 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 140.68 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIvvv 128
Cdd:cd05932 7 FTWGEVADKARRLAAALRA-LGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 snFASTLEQVVDQTPvknviitGLGDLLsapkrtlvnfvvkyIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVVKSDDI 208
Cdd:cd05932 83 --FVGKLDDWKAMAP-------GVPEGL--------------ISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVanvLQANGAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGannLLITNPRDI 288
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSFA---WAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGG---VLVAFAESL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 289 PGFVAELKKTPFTALTGVN---TLF----------------------NALVNSEEFAALDFSRLKLSIGGGMAVQRAVAD 343
Cdd:cd05932 214 DTFVEDVQRARPTLFFSVPrlwTKFqqgvqdkipqqklnlllkipvvNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 344 KWQNItKTRLLEGYGLTEASPLVACCpYDLAGYNGSIGLPAPSTQIQvrgddgqvlpQGETGELFAKGPQVMLGYWQRPE 423
Cdd:cd05932 294 WYRSL-GLNILEAYGMTENFAYSHLN-YPGRDKIGTVGNAGPGVEVR----------ISEDGEILVRSPALMMGYYKDPE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVS-GFNVFPNEVEEVVALHPKV--VEVAAVGVPHEVSGELVKI 500
Cdd:cd05932 362 ATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVemVCVIGSGLPAPLALVVLSE 441
|
490 500
....*....|....*....|....
gi 655376187 501 FVVAKDKSLTEKELIKHCRHHLTG 524
Cdd:cd05932 442 EARLRADAFARAELEASLRAHLAR 465
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
200-550 |
2.30e-35 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 139.37 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 200 KPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVA--NVLQANGAYAPLLNDGkEFVVTALPLYHIFAL--TVNCLLflHK 275
Cdd:PRK05857 163 NADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAvpDILQKEGLNWVTWVVG-ETTYSPLPATHIGGLwwILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GannLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGmavQRAVADKWQNITKT--RL 353
Cdd:PRK05857 240 G---LCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGG---SRAIAADVRFIEATgvRT 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 LEGYGLTEASPLVACCPYDLAGYN----GSIGLPAPSTQIQVRGDDG------QVLPQGETGELFAKGPQVMLGYWQRPE 423
Cdd:PRK05857 314 AQVYGLSETGCTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV 503
Cdd:PRK05857 394 RTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 655376187 504 AK---DKSLTEK---ELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK05857 473 ASaelDESAARAlkhTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
49-490 |
4.28e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 139.86 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVnvnPLYTPRELKHQ------LVDSGA 122
Cdd:PRK07769 56 LTWSQFGARNRAVGARLQQ--VTKPGDRVAILAPQNLDYLIAFFGALYAGRIAV---PLFDPAEPGHVgrlhavLDDCTP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 123 KAIVVVSNFASTLEQVVDQTPvknviitglgdllsAPKRTlvnfvvkyikRLVPKYSLPHAISmrralragkkAQYVKPV 202
Cdd:PRK07769 131 SAILTTTDSAEGVRKFFRARP--------------AKERP----------RVIAVDAVPDEVG----------ATWVPPE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 203 VKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGKEfVVTALPLYHIFAL-TVnclLFLHKGANNLL 281
Cdd:PRK07769 177 ANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALE--GQEGDR-GVSWLPFFHDMGLiTV---LLPALLGHYIT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 ITNPRDI---PG-FVAELKKTPftalTGVNTLFNALVN-SEEFAA-----------LDFSRLKLSIGGGMAVQRAVADKW 345
Cdd:PRK07769 251 FMSPAAFvrrPGrWIRELARKP----GGTGGTFSAAPNfAFEHAAarglpkdgeppLDLSNVKGLLNGSEPVSPASMRKF 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 346 QN------ITKTRLLEGYGLTEASPLVACCPYDL-------------AGYNGSIGLPAPSTQIQVR-------------- 392
Cdd:PRK07769 327 NEafapygLPPTAIKPSYGMAEATLFVSTTPMDEeptviyvdrdelnAGRFVEVPADAPNAVAQVSagkvgvsewavivd 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI-----------------DKDGWLATGDIG-YMDekGFFYIVDR 454
Cdd:PRK07769 407 PETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRTGDYGvYFD--GELYITGR 484
|
490 500 510
....*....|....*....|....*....|....*....
gi 655376187 455 KKDMILVSGFNVFPNEVEEVVALHPKVVE---VAAVGVP 490
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYTAQEATKALRtgyVAAFSVP 523
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
25-550 |
4.64e-35 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 137.06 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 25 LLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRA-AGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphai 184
Cdd:cd12115 80 DPAYPPERLRFILEDAQARLVLT--------------------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 smrralragkkaqyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPllnDGKEFVVTA------LP 258
Cdd:cd12115 103 -------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSA---EELAGVLAStsicfdLS 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 259 LYHIFA-LTVNCLLFLhkgANNLLitnprDIPGFVAELKktpftaLTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAV 337
Cdd:cd12115 161 VFELFGpLATGGKVVL---ADNVL-----ALPDLPAAAE------VTLINTVPSAAAELLRHDALPASVRVVNLAGEPLP 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 QRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNG-SIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVML 416
Cdd:cd12115 227 RDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEvSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVAR 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 417 GYWQRPEETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvaAVGVP 490
Cdd:cd12115 307 GYLGRPGLTAERFLPDPFGPgarlyrTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVRE--AVVVA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 491 HEVSG---ELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd12115 385 IGDAAgerRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
48-488 |
5.13e-35 |
|
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: 138.71 E-value: 5.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLlqyPIALFGVLRAGMVVVNVNPLYT---PRELKHQLVDSGAKA 124
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNR---PEWVWAELAAQAIGALSLGIYQdsmAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 125 IVvvsnfASTLEQVVDQTPVknviitglgdllsAPKRTLVNFVVKYIKRLVPKYSLPHAISMRRALRAGKKAQYVKPVV- 203
Cdd:cd17641 87 VI-----AEDEEQVDKLLEI-------------ADRIPSVRYVIYCDPRGMRKYDDPRLISFEDVVALGRALDRRDPGLy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 204 -------KSDDIAFLQYTGGTTGVSKGAMLSHGNIV---ANVLQANG--------AYAPLLNDGKEFVVTALPLYHIFal 265
Cdd:cd17641 149 erevaagKGEDVAVLCTTSGTTGKPKLAMLSHGNFLghcAAYLAADPlgpgdeyvSVLPLPWIGEQMYSVGQALVCGF-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 266 TVNC-------LLFLHKGANNLLITNPRDIPGFVAELK-----KTPF--------------------------TALTGVN 307
Cdd:cd17641 227 IVNFpeepetmMEDLREIGPTFVLLPPRVWEGIAADVRarmmdATPFkrfmfelgmklglraldrgkrgrpvsLWLRLAS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 308 TLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNItKTRLLEGYGLTEASPLVACCPYDLAGYNgSIGLPAPST 387
Cdd:cd17641 307 WLADALLFRPLRDRLGFSRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDPD-TVGVPFPGT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 388 QIQVrgddgqvlpqGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVF 467
Cdd:cd17641 385 EVRI----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRF 454
|
490 500
....*....|....*....|..
gi 655376187 468 -PNEVEEVVALHPKVVEVAAVG 488
Cdd:cd17641 455 sPQFIENKLKFSPYIAEAVVLG 476
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
204-459 |
1.24e-34 |
|
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: 136.96 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 204 KSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgKEFVVTALPLYHIFALTVNCLLFLHKG------A 277
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGP-DDRYLAYLPLAHIFELAAENVCLYRGGtigygsP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNLLITNPRDIPGFVAELKKTPFTA------------LTGVN-------TLFNALVNSEEFA-----------ALDFSRL 327
Cdd:cd17639 165 RTLTDKSKRGCKGDLTEFKPTLMVGvpaiwdtirkgvLAKLNpmgglkrTLFWTAYQSKLKAlkegpgtplldELVFKKV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 328 KLSIGG-------GMAVQRAVADKWQNITKTRLLEGYGLTEAsplvaCC------PYDLagYNGSIGLPAPSTQIQ-VRG 393
Cdd:cd17639 245 RAALGGrlrymlsGGAPLSADTQEFLNIVLCPVIQGYGLTET-----CAggtvqdPGDL--ETGRVGPPLPCCEIKlVDW 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 394 DDGQVL-----PQGEtgeLFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMI 459
Cdd:cd17639 318 EEGGYStdkppPRGE---ILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
38-551 |
1.92e-33 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 132.49 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRA-LGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAivvvsnfastleqvvdqtpvknviitglgdLLSAPKRTLvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd17649 81 EDSGAGL------------------------------LLTHHPRQL---------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksddiAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAY------------------------APLLNdGKEFV 253
Cdd:cd17649 97 -----------AYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYgltpgdrelqfasfnfdgaheqllPPLIC-GACVV 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 254 VTALPLYhifaLTVN--CLLFLHKGANNLLITnprdiPGFVAELkktpftaltgvntlfnalvnSEEFAALDFSR---LK 328
Cdd:cd17649 165 LRPDELW----ASADelAEMVRELGVTVLDLP-----PAYLQQL--------------------AEEADRTGDGRppsLR 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 329 LSIGGGMAVQRAVADKWQNITKtRLLEGYGLTEA--SPLVACCPYDL--AGYNGSIGLPAPSTQIQVRGDDGQVLPQGET 404
Cdd:cd17649 216 LYIFGGEALSPELLRRWLKAPV-RLFNAYGPTEAtvTPLVWKCEAGAarAGASMPIGRPLGGRSAYILDADLNPVPVGVT 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 405 GELFAKGPQVMLGYWQRPEETAK--VIDKDG-----WLATGDIG-YMDEkGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:cd17649 295 GELYIGGEGLARGYLGRPELTAErfVPDPFGapgsrLYRTGDLArWRDD-GVIEYLGRVDHQVKIRGFRIELGEIEAALL 373
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 477 LHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTE--KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd17649 374 EHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPElrAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
23-493 |
2.08e-33 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 134.84 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 23 ASLLEMLESAVNTYADQPAF---VNMGAT------LTYRKL-EERSRAFAAYLQndLKLQKGDRVAIMMPNLLQYPIALF 92
Cdd:PLN02736 44 GTLHDNFVYAVETFRDYKYLgtrIRVDGTvgeykwMTYGEAgTARTAIGSGLVQ--HGIPKGACVGLYFINRPEWLIVDH 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 93 GVLRAGMVVVnvnPLYtprelkhqlvDS-GAKAIVVVSNFASTleQVVDQTPVK-NVIITGLGDLLSApkRTLVnfVVKY 170
Cdd:PLN02736 122 ACSAYSYVSV---PLY----------DTlGPDAVKFIVNHAEV--AAIFCVPQTlNTLLSCLSEIPSV--RLIV--VVGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 171 IKRLVPkySLPHA-----ISMRRALRAGKKAQ--YVKPvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVlqANGAYA 243
Cdd:PLN02736 183 ADEPLP--SLPSGtgveiVTYSKLLAQGRSSPqpFRPP--KPEDVATICYTSGTTGTPKGVVLTHGNLIANV--AGSSLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 244 PLLNDGKEFVvTALPLYHIFAlTVNCLLFLHKGA-------NNLLITNprDIpgfvAELKKTPFTAL------------T 304
Cdd:PLN02736 257 TKFYPSDVHI-SYLPLAHIYE-RVNQIVMLHYGVavgfyqgDNLKLMD--DL----AALRPTIFCSVprlynriydgitN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 305 GVNT-------LFNALVNSEEFAALD------------FSRLKLSIGGGM--------AVQRAVADKWQNITKTRLLEGY 357
Cdd:PLN02736 329 AVKEsgglkerLFNAAYNAKKQALENgknpspmwdrlvFNKIKAKLGGRVrfmssgasPLSPDVMEFLRICFGGRVLEGY 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 358 GLTEASPLVACC-PYDLAgyNGSIGLPAPSTQIQVRG-------DDGQVLPQGEtgeLFAKGPQVMLGYWQRPEETAKVI 429
Cdd:PLN02736 409 GMTETSCVISGMdEGDNL--SGHVGSPNPACEVKLVDvpemnytSEDQPYPRGE---ICVRGPIIFKGYYKDEVQTREVI 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655376187 430 DKDGWLATGDIGYMDEKGFFYIVDRKKDMI-LVSGFNVFPNEVEEVVALHPKVVE------------VAAVGVPHEV 493
Cdd:PLN02736 484 DEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFVAQcfvygdslnsslVAVVVVDPEV 560
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
27-550 |
3.23e-33 |
|
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: 131.91 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLR-GKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDSGAKaivvvsnfastleqvvdqtpvknVIITglgdllsapkrtlvnfvvkyikrlvpkyslphaism 186
Cdd:cd17645 81 DYPGERIAYMLADSSAK-----------------------ILLT------------------------------------ 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 rralragkkaqyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEfvvtalpLYHIFALT 266
Cdd:cd17645 102 -----------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSL-------VYASFSFD 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 267 VNCL-LFLHKGANNLLITNPRDIPGFVAELKKtpFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKW 345
Cdd:cd17645 158 ASAWeIFPHLTAGAALHVVPSERRLDLDALND--YFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGY 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 346 QnitktrLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEET 425
Cdd:cd17645 236 K------LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 426 AKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVK 499
Cdd:cd17645 310 AEKFIVHPFVPgermyrTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 655376187 500 IFVVAKdKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17645 390 AYVTAP-EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
211-550 |
6.90e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 130.16 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 211 LQYTGGTTGVSKGAMLSHGNIVANVlqanGAYAPLLN-DGKEFVVTALPLYHIFALTVNCLLFLHKGANNLLITNPRdiP 289
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTEIDREI----EAYNEALNcEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKN--P 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 290 GFV-AELKKTPFTALTGVNTLFNALVN--SEEFAaldFSRLKLSiggGMAVQRAVADKWQNITkTRLLEGYGLTEASpLV 366
Cdd:PRK08308 180 KFAlNILRNTPQHILYAVPLMLHILGRllPGTFQ---FHAVMTS---GTPLPEAWFYKLRERT-TYMMQQYGCSEAG-CV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 367 ACCPyDLAgYNGSIGLPAPSTQIQVRGDDGQvlpqgetgelfakgpqvmlgywqrPEETaKVIDKDGWLATGDIGYMDEK 446
Cdd:PRK08308 252 SICP-DMK-SHLDLGNPLPHVSVSAGSDENA------------------------PEEI-VVKMGDKEIFTKDLGYKSER 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 447 GFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAkDKSLTEKELIKHCRHHLTGYK 526
Cdd:PRK08308 305 GTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS-HEEIDPVQLREWCIQHLAPYQ 383
|
330 340
....*....|....*....|....
gi 655376187 527 VPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK08308 384 VPHEIESVTEIPKNANGKVSRKLL 407
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
38-551 |
1.74e-32 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 131.27 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLLQYPIALFGVLRAGmvVVNVNPLYTPRelKHQL 117
Cdd:PRK10946 38 DAIAVICGERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQ--RSEL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 ---VDSGAKAIVVVSN----FAST--LEQVVDQTPVKNVII----TGLGDLLSAPKRTLVNFVvkyikrlvpkySLPHAi 184
Cdd:PRK10946 113 nayASQIEPALLIADRqhalFSDDdfLNTLVAEHSSLRVVLllndDGEHSLDDAINHPAEDFT-----------ATPSP- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 smrralragkkaqyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQAN-----GAYAPLLNdgkefvvtALPL 259
Cdd:PRK10946 181 --------------------ADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVeicgfTPQTRYLC--------ALPA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 260 YHIFALTV-NCLLFLHKGANNLLITNPRDIPGF-VAELKKTPFTALT--GVNTLFNALVNSEEFAALdfSRLKLSIGGGM 335
Cdd:PRK10946 233 AHNYPMSSpGALGVFLAGGTVVLAPDPSATLCFpLIEKHQVNVTALVppAVSLWLQAIAEGGSRAQL--ASLKLLQVGGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 336 AVQRAVADKWQNITKTRLLEGYGLTEAsplvaccpydLAGYN----------GSIGLP-APSTQIQVRGDDGQVLPQGET 404
Cdd:PRK10946 311 RLSETLARRIPAELGCQLQQVFGMAEG----------LVNYTrlddsderifTTQGRPmSPDDEVWVADADGNPLPQGEV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 405 GELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEV 484
Cdd:PRK10946 381 GRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 485 AAVGVPHEVSGELVKIFVVAKDkSLTEKELIKHCRHH-LTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK10946 461 ALVSMEDELMGEKSCAFLVVKE-PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
24-553 |
1.82e-32 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 131.79 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPA--FVNMGAT-------LTYRKLEERSRAFAAYLQNdlKLQKGDRVAIMMPNLLQYPIALFGV 94
Cdd:PRK12476 35 TLISLIERNIANVGDTVAyrYLDHSHSaagcaveLTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 95 LRAGMVVVnvnPLYTPRELKHqlvdsgakaivvvsnfASTLEQVV-DQTPvkNVIITglgdlLSAPKRTLVNFVvkyikR 173
Cdd:PRK12476 113 IKAGTIAV---PLFAPELPGH----------------AERLDTALrDAEP--TVVLT-----TTAAAEAVEGFL-----R 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 174 LVPKYSLPHAISMRrALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLlnDGKEFV 253
Cdd:PRK12476 162 NLPRLRRPRVIAID-AIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLL--DRNTHG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 254 VTALPLYHIFALTVNCLLFLHKGANNLL-----ITNP-RDI----------------PGFVAELkktpfTALTGVntlfn 311
Cdd:PRK12476 239 VSWLPLYHDMGLSMIGFPAVYGGHSTLMsptafVRRPqRWIkalsegsrtgrvvtaaPNFAYEW-----AAQRGL----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 312 alvnSEEFAALDFSRLKLsIGGGMAVQRAVADKWQ------NITKTRLLEGYGLTEASPLVACCPYDL------------ 373
Cdd:PRK12476 309 ----PAEGDDIDLSNVVL-IIGSEPVSIDAVTTFNkafapyGLPRTAFKPSYGIAEATLFVATIAPDAepsvvyldreql 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 374 -AGY-------------NGSIGLPAPSTQ-IQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI--------- 429
Cdd:PRK12476 384 gAGRavrvaadapnavaHVSCGQVARSQWaVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrla 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 ---------DKDGWLATGDIG-YMDekGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVE---VAAVGVPHEVSGE 496
Cdd:PRK12476 464 egshadgaaDDGTWLRTGDLGvYLD--GELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAEDNER 541
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 497 LVkifVVAKDKSLTEK-------ELIKH--CRHHLTGYKVPKLVEfRDELPKTNVGKILRRELRDE 553
Cdd:PRK12476 542 LV---IVAERAAGTSRadpapaiDAIRAavSRRHGLAVADVRLVP-AGAIPRTTSGKLARRACRAQ 603
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
38-550 |
2.34e-32 |
|
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: 129.90 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLRE-KGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQvvdqtpvkNVIITglgdLLSAPKRTLVNfvvkyikrlvpkyslphaismrralragkkAQ 197
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSF--------NKSTI----LLEDPSISQED------------------------------TS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 YVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNVLQANGAYAPLLNDGKEFVVTALPL---YH-IFALtvncllfL 273
Cdd:cd17656 120 NIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFEREKTNINFSDKVLQFATCSFdvcYQeIFST-------L 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 HKGANNLLITNP--RDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMavQRAVADKWQNITKT 351
Cdd:cd17656 192 LSGGTLYIIREEtkRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHIITAGE--QLVITNEFKEMLHE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 R---LLEGYGLTEASPLVACC--PYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETA 426
Cdd:cd17656 270 HnvhLHNHYGPSETHVVTTYTinPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTA 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 427 KVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVPHEVSGE--LV 498
Cdd:cd17656 350 EKFFPDPFDPnermyrTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSE-AVVLDKADDKGEkyLC 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 655376187 499 KIFVVakDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17656 429 AYFVM--EQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
46-554 |
2.35e-31 |
|
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: 126.70 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05940 1 DEALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVvsnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvks 205
Cdd:cd05940 80 VV------------------------------------------------------------------------------ 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 dDIAFLQYTGGTTGVSKGAMLSHGNIVanvLQANGAYAPLLNDGKEFVVTALPLYHIFALTV---NCLLflhkGANNLLI 282
Cdd:cd05940 82 -DAALYIYTSGTTGLPKAAIISHRRAW---RGGAFFAGSGGALPSDVLYTCLPLYHSTALIVgwsACLA----SGATLVI 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAvqravADKWQNITK----TRLLEGYG 358
Cdd:cd05940 154 RKKFSASNFWDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLR-----PDIWEEFKErfgvPRIAEFYA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASplvaCCPYDLAGYNGSIGLpAPSTQIQV----------------RGDDGQV--LPQGETGELFAK--GPQVMLGY 418
Cdd:cd05940 229 ATEGN----SGFINFFGKPGAIGR-NPSLLRKVaplalvkydlesgepiRDAEGRCikVPRGEPGLLISRinPLEPFDGY 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 419 WQRPEETAKVI-----DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVP--- 490
Cdd:cd05940 304 TDPAATEKKILrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpg 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655376187 491 HEVSGELVKIfVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:cd05940 384 TDGRAGMAAI-VLQPNEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEG 446
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
46-553 |
2.70e-31 |
|
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: 127.41 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 VVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPK-RTLVNFVVKYIKRLVPKYslphaismrraLRAGkkaqyvkpvVK 204
Cdd:cd05938 83 VVAPELQEAVEEVLPALRADGVSVWYLSHTSNTEGvISLLDKVDAASDEPVPAS-----------LRAH---------VT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 SDDIAFLQYTGGTTGVSKGAMLSHGNIVA--NVLQANGAYApllndgKEFVVTALPLYHIFALTVNCLLFLHKGANNLLI 282
Cdd:cd05938 143 IKSPALYIYTSGTTGLPKAARISHLRVLQcsGFLSLCGVTA------DDVIYITLPLYHSSGFLLGIGGCIELGATCVLK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 tnprdiPGFVA-----ELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAvqravADKWQNITK----TRL 353
Cdd:cd05938 217 ------PKFSAsqfwdDCRKHNVTVIQYIGELLRYLCNQPQSPNDRDHKVRLAIGNGLR-----ADVWREFLRrfgpIRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 LEGYGLTEASplVACCPYdlAGYNGSIG-------LPAPSTQIQ--------VRGDDGQVLP--QGETGELFAKGPQV-- 414
Cdd:cd05938 286 REFYGSTEGN--IGFFNY--TGKIGAVGrvsylykLLFPFELIKfdvekeepVRDAQGFCIPvaKGEPGLLVAKITQQsp 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 415 MLGYWQRPEETAK-----VIDK-DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVG 488
Cdd:cd05938 362 FLGYAGDKEQTEKkllrdVFKKgDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 489 VPheVSGELVKI----FVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDE 553
Cdd:cd05938 442 VT--VPGHEGRIgmaaVKLKPGHEFDGKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
50-544 |
3.89e-31 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 128.29 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLQNdlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNplYTP--RELKHQLVDSGAKAIVv 127
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEK--YSVEGERIGLMLPNATISAAVIFGASLRRRIPAMMN--YTAgvKGLTSAITAAEIKTIF- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 vsnfasTLEQVVDQtpvknviitglGDLLSAPKR-TLVNFVvkYIKRLVPKYSLPHAISMRRALRAGKKAQYVKpvvKSD 206
Cdd:PRK08043 308 ------TSRQFLDK-----------GKLWHLPEQlTQVRWV--YLEDLKDDVTTADKLWIFAHLLMPRLAQVKQ---QPE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkEFVvTALPLYHIFALTVNCLLFLHKGANNLLITNP- 285
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPND--RFM-SALPLFHSFGLTVGLFTPLLTGAEVFLYPSPl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 286 --RDIPGFVAELKktpFTALTGVNTLfnaLVNSEEFA-ALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEA 362
Cdd:PRK08043 443 hyRIVPELVYDRN---CTVLFGTSTF---LGNYARFAnPYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTEC 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVAC-CPydLAGYNGSIGLPAPstqiqvrGDDGQVLP-----QGetGELFAKGPQVMLGYW--QRP-------EETAK 427
Cdd:PRK08043 517 APVVSInVP--MAAKPGTVGRILP-------GMDARLLSvpgieQG--GRLQLKGPNIMNGYLrvEKPgvlevptAENAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 428 VIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVakDK 507
Cdd:PRK08043 586 GEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLFTT--DS 663
|
490 500 510
....*....|....*....|....*....|....*...
gi 655376187 508 SLTEKELIKHCRHH-LTGYKVPKLVEFRDELPKTNVGK 544
Cdd:PRK08043 664 ELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
36-554 |
7.96e-31 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 127.46 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 36 YADQPAFVnMGATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKH 115
Cdd:PRK06060 19 WYDRPAFY-AADVVTHGQIHDGAARLGEVLRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 116 QLVDSGAkAIVVVSN-----FASTleQVVDQtpvknviitglGDLLSapkrtlvnfvvkyikrlvpkyslphaismrRAL 190
Cdd:PRK06060 97 AARNTEP-ALVVTSDalrdrFQPS--RVAEA-----------AELMS------------------------------EAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 191 RAGKkAQYvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLLNDgKEFVVTALPLYHIFALTVNCL 270
Cdd:PRK06060 133 RVAP-GGY--EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFV-DAMCRKALRLTP-EDTGLCSARMYFAYGLGNSVW 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 LFLHKGANnlLITNPRDIPGFVAELKKTPF--TALTGVNTLFNALVNSeeFAALDFSRLKLSIGGGMAVQRAVADKW-QN 347
Cdd:PRK06060 208 FPLATGGS--AVINSAPVTPEAAAILSARFgpSVLYGVPNFFARVIDS--CSPDSFRSLRCVVSAGEALELGLAERLmEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITKTRLLEGYGLTEASPLVACCPYDlAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEetaK 427
Cdd:PRK06060 284 FGGIPILDGIGSTEVGQTFVSNRVD-EWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---S 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 428 VIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDK 507
Cdd:PRK06060 360 PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSG 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 655376187 508 SLTEKELIKHCRH----HLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:PRK06060 440 ATIDGSVMRDLHRgllnRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQS 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-550 |
4.83e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.23 E-value: 4.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 12 DVPAEIDASRyaSLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLqndLKLQKGD--RVAIMMPNLLQYPI 89
Cdd:PRK12316 4542 RTDAGYPATR--CVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHAL---IARGVGPevLVGIAMERSAEMMV 4616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 90 ALFGVLRAGMVVVNVNPLYtPRE-LKHQLVDSGAKAIVvvsnfasTLEQVVDQTPVKNviitGLGDLLSAPKRTLVNFvv 168
Cdd:PRK12316 4617 GLLAVLKAGGAYVPLDPEY-PRErLAYMMEDSGAALLL-------TQSHLLQRLPIPD----GLASLALDRDEDWEGF-- 4682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 169 kyikrlvpkyslPHAISMRRAlragkkaqyvkpvvKSDDIAFLQYTGGTTGVSKGAMLSHGNIVaNVLQANGAYAPLLND 248
Cdd:PRK12316 4683 ------------PAHDPAVRL--------------HPDNLAYVIYTSGSTGRPKGVAVSHGSLV-NHLHATGERYELTPD 4735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 249 GKEFVVTALPlyhiFALTV-NCLLFLHKGANnLLITNPR--DIPGFVAELKKTPFTALTGVNTLFNALVNSEEfAALDFS 325
Cdd:PRK12316 4736 DRVLQFMSFS----FDGSHeGLYHPLINGAS-VVIRDDSlwDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAE-RDGEPP 4809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 326 RLKLSIGGGMAVQRAVADK-WQNITKTRLLEGYGLTEASPLV---ACCPYDLAGYNG-SIGLPAPSTQIQVRGDDGQVLP 400
Cdd:PRK12316 4810 SLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVllwKARDGDACGAAYmPIGTPLGNRSGYVLDGQLNPLP 4889
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 401 QGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLA-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEE 473
Cdd:PRK12316 4890 VGVAGELYLGGEGVARGYLERPALTAERFVPDPFGApggrlyrTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEA 4969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 474 VVALHPKVVEVAAVGVPHEVSGELVKiFVVAKDKSLTEK---------ELIKHCRHHLTGYKVPKLVEFRDELPKTNVGK 544
Cdd:PRK12316 4970 RLREHPAVREAVVIAQEGAVGKQLVG-YVVPQDPALADAdeaqaelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGK 5048
|
....*.
gi 655376187 545 ILRREL 550
Cdd:PRK12316 5049 LDRKAL 5054
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
48-475 |
6.92e-30 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 124.01 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFA-AYLQndLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKaIV 126
Cdd:cd05933 8 TLTYKEYYEACRQAAkAFLK--LGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEAN-IL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNfASTLE---QVVDQTP-VKNVIITglgdllsapkrtlvnfvvkyikRLVPKYSLPHAISMRRALRAG-----KKAQ 197
Cdd:cd05933 85 VVEN-QKQLQkilQIQDKLPhLKAIIQY----------------------KEPLKEKEPNLYSWDEFMELGrsipdEQLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 YVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLLN--DGKEFVVTALPLYHIFALTVN------- 268
Cdd:cd05933 142 AIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTA-KAASQHMDLRPatVGQESVVSYLPLSHIAAQILDiwlpikv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 269 --CLLFLHKGA-NNLLITNPRD--------IPgFVAE---------------LKKTPFTALTGV---------------- 306
Cdd:cd05933 221 ggQVYFAQPDAlKGTLVKTLREvrptafmgVP-RVWEkiqekmkavgaksgtLKRKIASWAKGVgletnlklmggespsp 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 307 --NTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQ--NItktRLLEGYGLTEAS-PLVACCPYdlaGYN-GSI 380
Cdd:cd05933 300 lfYRLAKKLVFKKVRKALGLDRCQKFFTGAAPISRETLEFFLslNI---PIMELYGMSETSgPHTISNPQ---AYRlLSC 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 381 G--LPAPSTQIQVRGDDGQvlpqgetGELFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDM 458
Cdd:cd05933 374 GkaLPGCKTKIHNPDADGI-------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKEL 446
|
490
....*....|....*...
gi 655376187 459 ILVS-GFNVFPNEVEEVV 475
Cdd:cd05933 447 IITAgGENVPPVPIEDAV 464
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
175-551 |
7.36e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 120.54 E-value: 7.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 175 VPKYSLPHAISMRRALRAGKkaqyvkPVvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvlqANGAYAPLLNDGKEFVv 254
Cdd:PRK07824 12 VPAQDERRAALLRDALRVGE------PI--DDDVALVVATSGTTGTPKGAMLTAAALTAS---ADATHDRLGGPGQWLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 255 tALPLYHIFALTVnCLLFLHKGANNLLIT-----NPRDIPGFVAELK-KTPFTALTGVNtLFNALVNSEEFAALdfSRLK 328
Cdd:PRK07824 80 -ALPAHHIAGLQV-LVRSVIAGSEPVELDvsagfDPTALPRAVAELGgGRRYTSLVPMQ-LAKALDDPAATAAL--AELD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 329 LSIGGGMAVQRAVADKWQ----NITKTrllegYGLTEASplvACCPYDlagyngsiGLPAPSTQIQVrgDDGQVlpqgET 404
Cdd:PRK07824 155 AVLVGGGPAPAPVLDAAAaagiNVVRT-----YGMSETS---GGCVYD--------GVPLDGVRVRV--EDGRI----AL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 405 GelfakGPQVMLGYWQRPEETAKVidKDGWLATGDIGYMDEkGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEV 484
Cdd:PRK07824 213 G-----GPTLAKGYRNPVDPDPFA--EPGWFRTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADC 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 485 AAVGVPHEVSGE-LVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK07824 285 AVFGLPDDRLGQrVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-550 |
9.47e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 125.27 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 11 ADVPAEI-----DASRYA--SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPN 83
Cdd:PRK12467 493 EERARELvrwnaPATEYApdCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLI-AAGVGPDVLVGIAVER 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 84 LLQYPIALFGVLRAGMVVVNVNPLYtPRE-LKHQLVDSGAKAIVVVSNFASTLEQVVDqtpVKNVIITGLGDLLSapkrt 162
Cdd:PRK12467 572 SIEMVVGLLAVLKAGGAYVPLDPEY-PQDrLAYMLDDSGVRLLLTQSHLLAQLPVPAG---LRSLCLDEPADLLC----- 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 163 lvnfvvkyikrlvpkyslphaismrralraGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIvANVLQANGAY 242
Cdd:PRK12467 643 ------------------------------GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL-ANYVCVIAER 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 243 APLLNDGKefvvtaLPLYHIFALTVNCLLF---LHKGAnNLLITNP---RDIPGFVAELKKTPFTALTGVNTLFNALVNS 316
Cdd:PRK12467 692 LQLAADDS------MLMVSTFAFDLGVTELfgaLASGA-TLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQA 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 317 EEfAALDFSRLKLSIgGGMAVQRAVADKW-QNITKTRLLEGYGLTEASPLVA---CCPYDLAGYNGSIGLPAPSTQIQVR 392
Cdd:PRK12467 765 SR-VALPRPQRALVC-GGEALQVDLLARVrALGPGARLINHYGPTETTVGVStyeLSDEERDFGNVPIGQPLANLGLYIL 842
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK--VIDKDG-----WLATGDIGYMDEKGFFYIVDRKKDMILVSGFN 465
Cdd:PRK12467 843 DHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAErfVPDPFGadggrLYRTGDLARYRADGVIEYLGRMDHQVKIRGFR 922
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 466 VFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEK-----ELIKHCRHHLTGYKVPKLVEFRDELPKT 540
Cdd:PRK12467 923 IELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAEHqatrdELKAQLRQVLPDYMVPAHLLLLDSLPLT 1002
|
570
....*....|
gi 655376187 541 NVGKILRREL 550
Cdd:PRK12467 1003 PNGKLDRKAL 1012
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
48-439 |
1.06e-29 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 123.45 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYT-----PRELKH--QLVDS 120
Cdd:PRK08180 69 RLTYAEALERVRAIAQALL-DRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSlvsqdFGKLRHvlELLTP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 121 G----------AKAIVVVsnFASTLEQVVDQTPVKNVIITGLGDLLSAPKRTLVNfvvkyikrlvpkyslphaismrRAL 190
Cdd:PRK08180 148 GlvfaddgaafARALAAV--VPADVEVVAVRGAVPGRAATPFAALLATPPTAAVD----------------------AAH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 191 RAgkkaqyvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYaPLLNDGKEFVVTALPLYHIFALTVNCL 270
Cdd:PRK08180 204 AA----------VGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF-PFLAEEPPVLVDWLPWNHTFGGNHNLG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 271 LFLHKGANnLLITNPRDIPGFVAE----LKKTPFTALTGVNTLFNALVNS----EEFAALDFSRLKLSIGGGMAVQRAVA 342
Cdd:PRK08180 273 IVLYNGGT-LYIDDGKPTPGGFDEtlrnLREISPTVYFNVPKGWEMLVPAlerdAALRRRFFSRLKLLFYAGAALSQDVW 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 343 DKWQNIT------KTRLLEGYGLTEASPLVACC--PYDLAGYngsIGLPAPSTQIQVrgddgqvLPQGETGELFAKGPQV 414
Cdd:PRK08180 352 DRLDRVAeatcgeRIRMMTGLGMTETAPSATFTtgPLSRAGN---IGLPAPGCEVKL-------VPVGGKLEVRVKGPNV 421
|
410 420
....*....|....*....|....*
gi 655376187 415 MLGYWQRPEETAKVIDKDGWLATGD 439
Cdd:PRK08180 422 TPGYWRAPELTAEAFDEEGYYRSGD 446
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-544 |
1.38e-29 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 119.79 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIaFLQYTGGTTGVSKGAMLSHGNIVanVLQANGA------YAPLLNDGKEFVVTAL-------PLYHifALTVNCLLF 272
Cdd:cd05924 4 DDL-YILYTGGTTGMPKGVMWRQEDIF--RMLMGGAdfgtgeFTPSEDAHKAAAAAAGtvmfpapPLMH--GTGSWTAFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 273 LHKGANNLLITNPRdipgFVAE-----LKKTPFTALTGVNT-----LFNALVNSEEFaalDFSRLKLSIGGGMAVQRAVA 342
Cdd:cd05924 79 GLLGGQTVVLPDDR----FDPEevwrtIEKHKVTSMTIVGDamarpLIDALRDAGPY---DLSSLFAISSGGALLSPEVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 343 DKWQNITKTR-LLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQiqVRGDDGQVLPQGETGE-LFAKGPQVMLGYWQ 420
Cdd:cd05924 152 QGLLELVPNItLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV--VLDDDGRVVPPGSGGVgWIARRGHIPLGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 421 RPEETAK---VIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:cd05924 230 DEAKTAEtfpEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 655376187 498 VKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGK 544
Cdd:cd05924 310 VVAVVQLREgAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
48-510 |
1.69e-29 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 122.31 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYpIAL-FGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:PRK09274 41 ELSFAELDARSDAIAHGL-NAAGIGRGMRAVLMVTPSLEF-FALtFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVsnfasTLEQVVDQtpvknviitglgdLLSAPKRTlvnfvvkyIKRLVP--KYSLPHAISMRRALRAGKKAQYVKPVVK 204
Cdd:PRK09274 119 GI-----PKAHLARR-------------LFGWGKPS--------VRRLVTvgGRLLWGGTTLATLLRDGAAAPFPMADLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 205 SDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkefvvTALPLYHIFALTVNCLlflhkGANNLL--- 281
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE------IDLPTFPLFALFGPAL-----GMTSVIpdm 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 -----IT-NPRDIpgfvaelkktpFTALT--GVNTLF------NALVNSEEFAALDFSRLKLSIGGGMAVQRAVadkWQN 347
Cdd:PRK09274 242 dptrpATvDPAKL-----------FAAIEryGVTNLFgspallERLGRYGEANGIKLPSLRRVISAGAPVPIAV---IER 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITK-----TRLLEGYGLTEASP---------LVACCPYDLAGYNGSIGLPAPSTQIQVRG---------DDGQVLPQGET 404
Cdd:PRK09274 308 FRAmlppdAEILTPYGATEALPissiesreiLFATRAATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 405 GELFAKGPQVMLGYWQRPEET--AKVIDKDG--WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPK 480
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPEATrlAKIPDGQGdvWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPG 467
|
490 500 510
....*....|....*....|....*....|
gi 655376187 481 VVEVAAVGVPheVSGELVKIFVVAKDKSLT 510
Cdd:PRK09274 468 VKRSALVGVG--VPGAQRPVLCVELEPGVA 495
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
38-550 |
1.85e-29 |
|
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: 120.82 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd17652 81 ADARPALLLTTP-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIvANVLQANGAYAPLLNDGK--EFvvtALPLYHIFALTVncLLFLHK 275
Cdd:cd17652 93 --------DNLAYVIYTSGSTGRPKGVVVTHRGL-ANLAAAQIAAFDVGPGSRvlQF---ASPSFDASVWEL--LMALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANNLLITNPRDIPG--FVAELKKTPFTALTGVNTLFNALvnsEEFAALDFSRLklsIGGGMAVQRAVADKWQNitKTRL 353
Cdd:cd17652 159 GATLVLAPAEELLPGepLADLLREHRITHVTLPPAALAAL---PPDDLPDLRTL---VVAGEACPAELVDRWAP--GRRM 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 354 LEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK--VIDK 431
Cdd:cd17652 231 INAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAErfVADP 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 432 DGWLA-----TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVPHEVSGE--LVKIFVVA 504
Cdd:cd17652 311 FGAPGsrmyrTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAE-AVVVVRDDRPGDkrLVAYVVPA 389
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 655376187 505 KDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17652 390 PGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
48-557 |
3.97e-29 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 121.38 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPR-----ELKHqLVDSGA 122
Cdd:cd05921 25 RVTYAEALRQVRAIAQGLL-DLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMsqdlaKLKH-LFELLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 123 KAIVVVSN---FASTLEQVV-DQTPVknVIITGLGdllsaPKRTLVNFvvkyikrlvpkyslphaiSMRRALRAGKKAQY 198
Cdd:cd05921 103 PGLVFAQDaapFARALAAIFpLGTPL--VVSRNAV-----AGRGAISF------------------AELAATPPTAAVDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 199 VKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYaPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGAN 278
Cdd:cd05921 158 AFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTY-PFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYNGGT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 279 nLLITNPRDIPGFVAE----LKK-TP---FTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNIT- 349
Cdd:cd05921 237 -LYIDDGKPMPGGFEEtlrnLREiSPtvyFNVPAGWEMLVAALEKDEALRRRFFKRLKLMFYAGAGLSQDVWDRLQALAv 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 350 -----KTRLLEGYGLTEASPLvACCPYDLAGYNGSIGLPAPSTQIQVrgddgqvLPQGETGELFAKGPQVMLGYWQRPEE 424
Cdd:cd05921 316 atvgeRIPMMAGLGATETAPT-ATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPEL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 425 TAKVIDKDGWLATGD-IGYMD----EKGFFYIVDRKKDMILVSG--FNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:cd05921 388 TAQAFDEEGFYCLGDaAKLADpddpAKGLVFDGRVAEDFKLASGtwVSVGPLRARAVAACAPLVHDAVVAGEDRAEVGAL 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 498 VKIFV-----VAKDKSLTEKELIKHcrhhltgykvPKLVE-FRDELPKTN------VGKILRRELRDEAKSA 557
Cdd:cd05921 468 VFPDLlacrrLVGLQEASDAEVLRH----------AKVRAaFRDRLAALNgeatgsSSRIARALLLDEPPSI 529
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
38-554 |
1.54e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.40 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKRTLVNFVVkyikrlvpkyslphaismrralragkkaq 197
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPFRV----------------------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVAnvlqANGAYAPLLNDGKEFVV-TALPLYHIFALTVNCLLFLHKG 276
Cdd:PRK07867 149 -----ADPDDLFMLIFTSGTSGDPKAVRCTHRKVAS----AGVMLAQRFGLGPDDVCyVSMPLFHSNAVMAGWAVALAAG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 277 ANnllITNPR--DIPGFVAELKKTPFTALTGV------------------NTLFNALVNseEFAALDFSRLKLSIGggma 336
Cdd:PRK07867 220 AS---IALRRkfSASGFLPDVRRYGATYANYVgkplsyvlatperpddadNPLRIVYGN--EGAPGDIARFARRFG---- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 337 vqravadkwqnitkTRLLEGYGLTEASPLVACCPydlAGYNGSIGLPAPSTQIqVRGDDGQVLPQGE------------T 404
Cdd:PRK07867 291 --------------CVVVDGFGSTEGGVAITRTP---DTPPGALGPLPPGVAI-VDPDTGTECPPAEdadgrllnadeaI 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 405 GELF-AKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVE 483
Cdd:PRK07867 353 GELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATE 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655376187 484 VAAVGVPHEVSGELVKIFVVAKDKSLTEKELIK---HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:PRK07867 432 VAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAeflAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEG 505
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-551 |
9.08e-28 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 116.76 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 50 TYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVS 129
Cdd:cd05915 26 TYAEVYQRARRLMGGL-RALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 130 NFASTLEQV------VDQTPVKNVIITGLGDLLSAPKrtlvnfvvkyikrlvPKYslphaismrralragkkaQYVKPVV 203
Cdd:cd05915 105 NLLPLVEAIrgelktVQHFVVMDEKAPEGYLAYEEAL---------------GEE------------------ADPVRVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 204 KSDDIAfLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLLNDGKEFVVTALPLYH------IFALTV--NCLLFLHK 275
Cdd:cd05915 152 ERAACG-MAYTTGTTGLPKGVVYSHRALVLHS-LAASLVDGTALSEKDVVLPVVPMFHvnawclPYAATLvgAKQVLPGP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANNLLITNprdipgfvaELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRaVADKWQNITKTRLLE 355
Cdd:cd05915 230 RLDPASLVE---------LFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPR-SLIARFERMGVEVRQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 356 GYGLTEASPLVACCPY----------DLAGYNGSIGLPAPSTQIQVRGDDGQVLPQ-GETGELFA-KGPQVMLGYWQRPE 423
Cdd:cd05915 300 GYGLTETSPVVVQNFVkshleslseeEKLTLKAKTGLPIPLVRLRVADEEGRPVPKdGKALGEVQlKGPWITGGYYGNEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 424 ETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV 503
Cdd:cd05915 380 ATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVV 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 655376187 504 AKDKSLTEKELIKHCRHHLTGYK-VPKLVEFRDELPKTNVGKILRRELR 551
Cdd:cd05915 460 PRGEKPTPEELNEHLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
201-549 |
1.34e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 116.63 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 201 PVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvlqANGAYAPLLND-GKEFVVTALPLYH----IFALTVNcllfLHK 275
Cdd:PRK07768 147 VETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN---AEAMFVAAEFDvETDVMVSWLPLFHdmgmVGFLTVP----MYF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GANNLLITnPRDI---PGFVAEL-KKTPFTALTGVNTLFNA----LVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQN 347
Cdd:PRK07768 220 GAELVKVT-PMDFlrdPLLWAELiSKYRGTMTAAPNFAYALlarrLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLD 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITK------TRLLEGYGLTEAS----------PLVAC--CPYDLAGYN-------------GSIGLPAPSTQIQVRGDDG 396
Cdd:PRK07768 299 AGArfglrpEAILPAYGMAEATlavsfspcgaGLVVDevDADLLAALRravpatkgntrrlATLGPPLPGLEVRVVDEDG 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 397 QVLPQGETGELFAKGPQVMLGYwQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PRK07768 379 QVLPPRGVGVIELRGESVTPGY-LTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAA 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 477 LHPKVVE--VAAVGVPHEVSGElvKIFVVAKDKSLTEKELIKHCRHHLTgYKVPKLVEFRDE---------LPKTNVGKi 545
Cdd:PRK07768 458 RVEGVRPgnAVAVRLDAGHSRE--GFAVAVESNAFEDPAEVRRIRHQVA-HEVVAEVGVRPRnvvvlgpgsIPKTPSGK- 533
|
....
gi 655376187 546 LRRE 549
Cdd:PRK07768 534 LRRA 537
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
24-553 |
1.78e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 115.76 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAI---MMPNLLqypIALFGVLRAGMV 100
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFID-SLKLPDKSPIIVfghMSPEML---ATFLGAVKAGHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 101 VVNVNpLYTPRELKHQLVDSGAKAIVVvsnfaSTLEQVVDQTPVKNVIITGLGDLLSAPkrtlvnfvvkyikrlvPKYSL 180
Cdd:PRK04813 79 YIPVD-VSSPAERIEMIIEVAKPSLII-----ATEELPLEILGIPVITLDELKDIFATG----------------NPYDF 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 181 PHAismrralragkkaqyvkpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGKEFVvtALPLY 260
Cdd:PRK04813 137 DHA-------------------VKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFA--LPEGPQFL--NQAPY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 261 HiFALTV----NCL-----LF-LHKGannlLITNPRDIpgFvAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLS 330
Cdd:PRK04813 194 S-FDLSVmdlyPTLasggtLVaLPKD----MTANFKQL--F-ETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHF 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 331 IGGGMAVQRAVADK-WQNITKTRLLEGYGLTEASplVACC-----PYDLAGYNG-SIGLPAPSTQIQVRGDDGQVLPQGE 403
Cdd:PRK04813 266 LFCGEELPHKTAKKlLERFPSATIYNTYGPTEAT--VAVTsieitDEMLDQYKRlPIGYAKPDSPLLIIDEEGTKLPDGE 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 404 TGELFAKGPQVMLGYWQRPEETAKV-IDKDGWLA--TGDIGYMDEkgffyivdrkkDMILVSG-------FNVFPNEVEE 473
Cdd:PRK04813 344 QGEIVISGPSVSKGYLNNPEKTAEAfFTFDGQPAyhTGDAGYLED-----------GLLFYQGridfqikLNGYRIELEE 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 474 VVALHPKVVEV-AAVGVP----HEVSgELVKiFVVAKDKSLT-EKELIKHCRHHLTG----YKVPKLVEFRDELPKTNVG 543
Cdd:PRK04813 413 IEQNLRQSSYVeSAVVVPynkdHKVQ-YLIA-YVVPKEEDFErEFELTKAIKKELKErlmeYMIPRKFIYRDSLPLTPNG 490
|
570
....*....|
gi 655376187 544 KILRRELRDE 553
Cdd:PRK04813 491 KIDRKALIEE 500
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
24-550 |
5.50e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 114.71 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNDlKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVN 103
Cdd:PRK13383 36 NPYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 104 VNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPVKNVIITGLGDLLSAPKrtlvnfvvkyikrlvpkyslpha 183
Cdd:PRK13383 115 ISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPA----------------------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 184 ismrralragkkaqyvkpVVKSDDIAFLqyTGGTTGVSKGAMLShgnivANVLQANGAYAPLLNDGK----EFVVTALPL 259
Cdd:PRK13383 172 ------------------VAAPGRIVLL--TSGTTGKPKGVPRA-----PQLRSAVGVWVTILDRTRlrtgSRISVAMPM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 260 YHifALTVNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVN--SEEFAALDFSRLKLSIGGGMAV 337
Cdd:PRK13383 227 FH--GLGLGMLMLTIALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILElpPRVRARNPLPQLRVVMSSGDRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 QRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLG 417
Cdd:PRK13383 305 DPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YwqrPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGEL 497
Cdd:PRK13383 385 Y---TDGGGKAV-VDGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHR 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 655376187 498 VKIFVVAKDKSLTEKELIK-HCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK13383 461 LAAFVVLHPGSGVDAAQLRdYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-550 |
1.52e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.44 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWINSLPA----------DVPaEIDASRYASLLEMLESAVNTYADQ-----------------PAFVNMGATLTYRK 53
Cdd:PRK12316 463 MARHWQNLLRGmvenpqarvdELP-MLDAEERGQLVEGWNATAAEYPLQrgvhrlfeeqvertpeaPALAFGEETLDYAE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 54 LEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIvvvsnfas 133
Cdd:PRK12316 542 LNRRANRLAHALI-ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL-------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 134 tLEQvvdqtpvknviiTGLGDLLSAPkRTLVNFVVKYIKRLVPKYSlphaismrralrAGKKAQYVKPvvksDDIAFLQY 213
Cdd:PRK12316 613 -LSQ------------SHLGRKLPLA-AGVQVLDLDRPAAWLEGYS------------EENPGTELNP----ENLAYVIY 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 214 TGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGkefVVTALPlyhiFALTVNCLLF---LHKGANnLLITNP---RD 287
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDT---VLQKTP----FSFDVSVWEFfwpLMSGAR-LVVAAPgdhRD 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 288 IPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLkLSIGG----GMAVQRAVADKWQnitkTRLLEGYGLTEAS 363
Cdd:PRK12316 735 PAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRR-IVCSGealpADAQEQVFAKLPQ----AGLYNLYGPTEAA 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 364 PLVACCPY-DLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAK------VIDKDGWLA 436
Cdd:PRK12316 810 IDVTHWTCvEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAErfvpspFVAGERMYR 889
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 437 TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVpheVSGELVKIFVVAKDKSLTEKELIK 516
Cdd:PRK12316 890 TGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVRE-AAVLA---VDGKQLVGYVVLESEGGDWREALK 965
|
570 580 590
....*....|....*....|....*....|....*
gi 655376187 517 -HCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK12316 966 aHLAASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
48-456 |
2.76e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 113.53 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVV 127
Cdd:PTZ00216 121 YITYAELWERIVNFGRGLA-ELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 VSNFASTLEQVVDQTPVKNVIITGLGDL---LSAPKRTLVNF--VVKYIKRLVPKYSLPHAISmrralragkkaqyvkpv 202
Cdd:PTZ00216 200 NGKNVPNLLRLMKSGGMPNTTIIYLDSLpasVDTEGCRLVAWtdVVAKGHSAGSHHPLNIPEN----------------- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 203 vkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqangAYAPLLND--GK----EFVVTALPLYHIFALTV-NclLFLHK 275
Cdd:PTZ00216 263 --NDDLALIMYTSGTTGDPKGVMHTHGSLTAGIL----ALEDRLNDliGPpeedETYCSYLPLAHIMEFGVtN--IFLAR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 276 GAnnlLIT--NPRDI---------------PGFVA-------ELKKTPFTALTGVNTL---------------------- 309
Cdd:PTZ00216 335 GA---LIGfgSPRTLtdtfarphgdltefrPVFLIgvprifdTIKKAVEAKLPPVGSLkrrvfdhayqsrlralkegkdt 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 310 --FNALVNSEEFAALDfSRLKLSIGGGMAVQRAVADkWQNITKTRLLEGYGLTEAsplVACCPYDLAG--YNGSIGLPAP 385
Cdd:PTZ00216 412 pyWNEKVFSAPRAVLG-GRVRAMLSGGGPLSAATQE-FVNVVFGMVIQGWGLTET---VCCGGIQRTGdlEPNAVGQLLK 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 386 STQIQVRGDDG-----QVLPQGEtgeLFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKK 456
Cdd:PTZ00216 487 GVEMKLLDTEEykhtdTPEPRGE---ILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVK 559
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
33-555 |
6.54e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 112.16 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 33 VNTYADQPAFVNMG------ATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMV--VVNV 104
Cdd:PRK00174 77 LKTRGDKVAIIWEGddpgdsRKITYRELHREVCRFANALKS-LGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsVVFG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NplYTPRELKHQLVDSGAKAIVVVSNF-----ASTLEQVVDQ-----TPVKNVII---TGlGDLLSAPKRTLvnfvvkYI 171
Cdd:PRK00174 156 G--FSAEALADRIIDAGAKLVITADEGvrggkPIPLKANVDEalancPSVEKVIVvrrTG-GDVDWVEGRDL------WW 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 172 KRLVPKYSlphaismrralragkkaQYVKPV-VKSDDIAFLQYTGGTTGVSKG-----------AMLSHGNI-------- 231
Cdd:PRK00174 227 HELVAGAS-----------------DECEPEpMDAEDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVfdykdgdv 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 232 ---VANVLQANG----AYAPLLNdGkefvvtalplyhifALTVncllfLHKGAnnllitnPR--------DIpgfVAELK 296
Cdd:PRK00174 290 ywcTADVGWVTGhsyiVYGPLAN-G--------------ATTL-----MFEGV-------PNypdpgrfwEV---IDKHK 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 297 KTPF-TALTGVNTLFNAlvNSEEFAALDFSRLKL------------------SIGGGmavQRAVADK-WQniTKTrlleg 356
Cdd:PRK00174 340 VTIFyTAPTAIRALMKE--GDEHPKKYDLSSLRLlgsvgepinpeawewyykVVGGE---RCPIVDTwWQ--TET----- 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 yGLTEASPL---VACCPydlagynGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKG--PQVMLGYW---QRPEETAKV 428
Cdd:PRK00174 408 -GGIMITPLpgaTPLKP-------GSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDpwPGMMRTIYgdhERFVKTYFS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 429 IDKDGWLaTGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKS 508
Cdd:PRK00174 480 TFKGMYF-TGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGE 558
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 655376187 509 LTE----KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEAK 555
Cdd:PRK00174 559 EPSdelrKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRRILRKIAE 609
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
38-550 |
6.79e-26 |
|
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: 110.63 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRG-LGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKAivvvsnfastleqvvdqtpvknviitglgdLLSAPkrtlvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd17650 81 EDSGAKL------------------------------LLTQP-------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIvanvlqANGAYAPllndGKEFVVTALPLYHIFALTVNCLLFLHKGA 277
Cdd:cd17650 93 --------EDLAYVIYTSGTTGKPKGVMVEHRNV------AHAAHAW----RREYELDSFPVRLLQMASFSFDVFAGDFA 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNL-----LITNPRDIPGFVAEL----KKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSI-GGGMAVQRAVADKWQN 347
Cdd:cd17650 155 RSLlnggtLVICPDEVKLDPAALydliLKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIvGSDGCKAQDFKTLAAR 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 I-TKTRLLEGYGLTEASplVACCPYDLA------GYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQ 420
Cdd:cd17650 235 FgQGMRIINSYGVTEAT--IDSTYYEEGrdplgdSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLN 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 421 RPEETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVPHEVS 494
Cdd:cd17650 313 RPELTAERFVENPFAPgermyrTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKG 391
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 495 GE--LVKiFVVAKDKsLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17650 392 GEarLCA-YVVAAAT-LNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-551 |
1.44e-25 |
|
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: 109.19 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQlVDSGAKAIVVV 128
Cdd:cd05974 1 VSFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDR-VDRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SNfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpVVKSDDI 208
Cdd:cd05974 79 DE-----------------------------------------------------------------------NTHADDP 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTgvSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVVTALPLYHIFALTvNCLLFLHKGANNLLITNPR-D 287
Cdd:cd05974 88 MLLYFTSGTT--SKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWNISSPGWAKHAWS-CFFAPWNAGATVFLFNYARfD 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 288 IPGFVAELKKTPFTALTGVNTLFNALVNsEEFAALDfSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVA 367
Cdd:cd05974 165 AKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFD-VKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 368 CCPydlaGYN---GSIGLPAPSTQIQVRGDDGQVLPQGE-TGELFAKGPQ-VMLGYWQRPEETAKVIdKDGWLATGDIGY 442
Cdd:cd05974 243 NSP----GQPvkaGSMGRPLPGYRVALLDPDGAPATEGEvALDLGDTRPVgLMKGYAGDPDKTAHAM-RGGYYRTGDIAM 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 443 MDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVV----AKDKSLTEKELIKHC 518
Cdd:cd05974 318 RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlragYEPSPETALEIFRFS 397
|
490 500 510
....*....|....*....|....*....|...
gi 655376187 519 RHHLTGYKVPKLVEFRdELPKTNVGKILRRELR 551
Cdd:cd05974 398 RERLAPYKRIRRLEFA-ELPKTISGKIRRVELR 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
38-550 |
2.55e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.59 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYtPRE-LKHQ 116
Cdd:PRK12316 2018 EAIAVVFGDQHLSYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY-PAErLAYM 2095
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 117 LVDSGAKAIVvvsnfasTLEQVVDQTPVKnviiTGLGDLLsapkrtlvnfvvkyikrLVPKYSLPHAISMRRALRAGkka 196
Cdd:PRK12316 2096 LEDSGAALLL-------TQRHLLERLPLP----AGVARLP-----------------LDRDAEWADYPDTAPAVQLA--- 2144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 197 qyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANvLQANGAYAPLLNDGKEFVVTAlplyhiFALTV---NCLLFL 273
Cdd:PRK12316 2145 --------GENLAYVIYTSGSTGLPKGVAVSHGALVAH-CQAAGERYELSPADCELQFMS------FSFDGaheQWFHPL 2209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 HKGANNLLITNPRDIPG-FVAELKKTPFTALTGVNTLFNALVnseEFAALDFSRLKLSIG--GGMAVQRAVADK-WQNIT 349
Cdd:PRK12316 2210 LNGARVLIRDDELWDPEqLYDEMERHGVTILDFPPVYLQQLA---EHAERDGRPPAVRVYcfGGEAVPAASLRLaWEALR 2286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 350 KTRLLEGYGLTEA--SPLV-ACCPYDLAGYNGS-IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEET 425
Cdd:PRK12316 2287 PVYLFNGYGPTEAvvTPLLwKCRPQDPCGAAYVpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLT 2366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 426 AKVIDKDGWLA-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVPHEVSGELV 498
Cdd:PRK12316 2367 AERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVRE-AVVVAQDGASGKQL 2445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 655376187 499 KIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK12316 2446 VAYVVPDDaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
38-550 |
6.66e-25 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 107.49 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 38 DQPAFVNMGATLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQL 117
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 118 VDSGAKaivvvsnfastleqvvdqtpvknVIITGlgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaq 197
Cdd:cd17648 82 EDTGAR-----------------------VVITN---------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 yvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYApLLNDGKEfVVTALPLYhIFALTVNCLLFLHKGA 277
Cdd:cd17648 93 -------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYF-GRDNGDE-AVLFFSNY-VFDFFVEQMTLALLNG 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNLLITNPR---DIPGFVAELKKTPFTALTGVNTLFnalvnsEEFaalDFSR---LKLSIGGGMAVQRAVADKWQNITKT 351
Cdd:cd17648 163 QKLVVPPDEmrfDPDRFYAYINREKVTYLSGTPSVL------QQY---DLARlphLKRVDAAGEEFTAPVFEKLRSRFAG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RLLEGYGLTEASPLVACCPYDL-AGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVI- 429
Cdd:cd17648 234 LIINAYGPTETTVTNHKRFFPGdQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFl 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 430 ------DKDGWLA-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGE 496
Cdd:cd17648 314 pnpfqtEQERARGrnarlykTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQ 393
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 497 ------LVKIFVVAKDkSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17648 394 sriqkyLVGYYLPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
49-547 |
9.00e-25 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 108.68 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQlVDSGAKAIVVV 128
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLN-LNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR-IETITPKLIIT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SNFASTLEQVVDQTP-VKNVIitglgdLLSAPKRtlvNFVVKYIKRLVPKYS----------LPHAISMRRALRAGKKAQ 197
Cdd:PTZ00237 171 TNYGILNDEIITFTPnLKEAI------ELSTFKP---SNVITLFRNDITSESdlkkietiptIPNTLSWYDEIKKIKENN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 198 ------YVkPVVKSDDIaFLQYTGGTTGVSKGAMLSHGnivANVLQANGAYAPLLNDGKEFVVTALP-----LYHIF--- 263
Cdd:PTZ00237 242 qspfyeYV-PVESSHPL-YILYTSGTTGNSKAVVRSNG---PHLVGLKYYWRSIIEKDIPTVVFSHSsigwvSFHGFlyg 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 264 ALTVNCLLFLHKGAnnllITNPRDIP-GFVAELKKTPFT-ALTGVNTLFNALVNSEEFAAL----DFSRLKLSIGGGMAV 337
Cdd:PTZ00237 317 SLSLGNTFVMFEGG----IIKNKHIEdDLWNTIEKHKVThTLTLPKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 QRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAK---GPQV 414
Cdd:PTZ00237 393 EESIPEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSF 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 415 MLGYWQRPEETAKVIDK-DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPH-E 492
Cdd:PTZ00237 473 ATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDpD 552
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 493 VSGELVKIFVVAKDKSLTEKELIKH-------CRHHLTGYKVPKLVEFRDELPKTNVGKILR 547
Cdd:PTZ00237 553 CYNVPIGLLVLKQDQSNQSIDLNKLkneinniITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
49-441 |
1.09e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.21 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTP-----RELKHqLVDSGAK 123
Cdd:PRK12582 81 VTYGEAKRAVDALAQALL-DLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKH-LFDLVKP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 124 AIVVVSN---FASTLEqVVDQTPVKNVIITGLGDLLSA-PKRTLVnfvvkyikrlvpkyslphAISMRRALRAGKKAqyv 199
Cdd:PRK12582 159 RVVFAQSgapFARALA-ALDLLDVTVVHVTGPGEGIASiAFADLA------------------ATPPTAAVAAAIAA--- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 200 kpvVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGANn 279
Cdd:PRK12582 217 ---ITPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGT- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 280 LLITNPRDIPGFVAELKK-----TP---FTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQ----N 347
Cdd:PRK12582 293 LYIDDGKPLPGMFEETIRnlreiSPtvyGNVPAGYAMLAEAMEKDDALRRSFFKNLRLMAYGGATLSDDLYERMQalavR 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 348 ITKTR--LLEGYGLTEASPlVACCPYDLAGYNGSIGLPAPSTQIQVrgddgqvLPQGETGELFAKGPQVMLGYWQRPEET 425
Cdd:PRK12582 373 TTGHRipFYTGYGATETAP-TTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPELT 444
|
410
....*....|....*.
gi 655376187 426 AKVIDKDGWLATGDIG 441
Cdd:PRK12582 445 AAAFDEEGFYRLGDAA 460
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
37-551 |
1.86e-24 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 107.73 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 37 ADQPAFV------NMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVvvnvnplytp 110
Cdd:PRK10524 67 PEQLALIavstetDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAMLACARIGAI---------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 111 relkHQLVDSG------------AKAIVVVSNFA-STLEQVVDQTPVKNVIITglgdlLSAPKRTLVNFVVKYI--KRLV 175
Cdd:PRK10524 136 ----HSVVFGGfashslaariddAKPVLIVSADAgSRGGKVVPYKPLLDEAIA-----LAQHKPRHVLLVDRGLapMARV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 176 PKYSLPHAismrrALRAGKKAQYVkPV--VKSDDIAFLQYTGGTTGVSKGamlshgnivanVLQANGAYApllndgkefV 253
Cdd:PRK10524 207 AGRDVDYA-----TLRAQHLGARV-PVewLESNEPSYILYTSGTTGKPKG-----------VQRDTGGYA---------V 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 254 VTALPLYHIFA--------------------------LTVNCLLFLHKGannlLITNPRdiPG----FVAELKKTP-FTA 302
Cdd:PRK10524 261 ALATSMDTIFGgkagetffcasdigwvvghsyivyapLLAGMATIMYEG----LPTRPD--AGiwwrIVEKYKVNRmFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 303 LTGVNTLFNAlvNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEAS-PLVACCP--YDLAGYNGS 379
Cdd:PRK10524 335 PTAIRVLKKQ--DPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETGwPILAIARgvEDRPTRLGS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 380 IGLPAPSTQIQVRGD-DGQVLPQGETGELFAKGP------QVMLG--------YWqrpeetaKVIDKDGWlATGDIGYMD 444
Cdd:PRK10524 413 PGVPMYGYNVKLLNEvTGEPCGPNEKGVLVIEGPlppgcmQTVWGdddrfvktYW-------SLFGRQVY-STFDWGIRD 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 445 EKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLT---------EKELI 515
Cdd:PRK10524 485 ADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLadrearlalEKEIM 564
|
570 580 590
....*....|....*....|....*....|....*.
gi 655376187 516 KHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELR 551
Cdd:PRK10524 565 ALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAIQ 600
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
15-550 |
2.19e-24 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 108.21 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 15 AEIDASRYA----SLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIA 90
Cdd:PRK10252 446 AQVNATAVEipetTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 91 LFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVVDQTPvknviitglgdllsapkrtlvnfvvky 170
Cdd:PRK10252 525 LHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTS--------------------------- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 171 ikrlvPKYSLPHAISMRRALRAGKkaqyvkpvvkSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYaPLLNDgk 250
Cdd:PRK10252 578 -----LCYNAPLAPQGAAPLQLSQ----------PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHY-PLTAD-- 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 251 EFVVTALPLyhIFALTV-NCLLFLHKGANnLLITNP---RDiPGFVAEL-KKTPFTALTGVNTLFNALVNS--EEFAALD 323
Cdd:PRK10252 640 DVVLQKTPC--SFDVSVwEFFWPFIAGAK-LVMAEPeahRD-PLAMQQFfAEYGVTTTHFVPSMLAAFVASltPEGARQS 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 324 FSRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVA---CCPYDLAGYNGS---IGLPAPSTQIQVRGDDGQ 397
Cdd:PRK10252 716 CASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSwypAFGEELAAVRGSsvpIGYPVWNTGLRILDARMR 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 398 VLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWL------ATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEV 471
Cdd:PRK10252 796 PVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEI 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 472 EEVVALHPKV---VEVAAVGVPHEVSG----ELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGK 544
Cdd:PRK10252 876 DRAMQALPDVeqaVTHACVINQAAATGgdarQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGK 955
|
....*.
gi 655376187 545 ILRREL 550
Cdd:PRK10252 956 LDRKAL 961
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-552 |
3.41e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.94 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 3 QPWINSLpADVPAEidasryASLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLqndlkLQKG---DR-VA 78
Cdd:PRK12467 3082 HAWNATA-AAYPSE------RLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRL-----IAIGvgpDVlVG 3149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 79 IMMPNLLQYPIALFGVLRAGMVVVNVNPLYtPRE-LKHQLVDSGAKAIVvvsNFASTLEQVVDQTPVKNVIITGlGDLLS 157
Cdd:PRK12467 3150 VAVERSVEMIVALLAVLKAGGAYVPLDPEY-PRErLAYMIEDSGVKLLL---TQAHLLEQLPAPAGDTALTLDR-LDLNG 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 158 APKRTLVnfvvkyikrlvpkyslphaismrralragkkaqyvkPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIvANVLQ 237
Cdd:PRK12467 3225 YSENNPS------------------------------------TRVMGENLAYVIYTSGSTGKPKGVGVRHGAL-ANHLC 3267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 238 ANGAYAPLLNDGKEFVVTALPlyhiFALTV-NCLLFLHKGANNLLITNP-RDIPGFVAELKKTPFTALTGVNTLFNALVN 315
Cdd:PRK12467 3268 WIAEAYELDANDRVLLFMSFS----FDGAQeRFLWTLICGGCLVVRDNDlWDPEELWQAIHAHRISIACFPPAYLQQFAE 3343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 316 SEEFAalDFSRLKLSIGGGMAVQRAVADKWQNITKTR-LLEGYGLTEA--SPLVACCPYD---LAGYnGSIGLPAPSTQI 389
Cdd:PRK12467 3344 DAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEAvvTVTLWKCGGDavcEAPY-APIGRPVAGRSI 3420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 390 QVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLA-------TGDIGYMDEKGFFYIVDRKKDMILVS 462
Cdd:PRK12467 3421 YVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGsggrlyrTGDLARYRADGVIEYLGRIDHQVKIR 3500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 463 GFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKiFVVAKDKSLTEKELIK-HCRHHLTGYKVPKLVEFRDELPKTN 541
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVA-YVVPADPQGDWRETLRdHLAASLPDYMVPAQLLVLAAMPLGP 3579
|
570
....*....|.
gi 655376187 542 VGKILRRELRD 552
Cdd:PRK12467 3580 NGKVDRKALPD 3590
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-550 |
6.33e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 107.17 E-value: 6.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 14 PAEIDASRyaSLLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFG 93
Cdd:PRK12467 1567 HTGYPLAR--LVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLI-ALGVGPEVLVGIAVERSLEMVVGLLA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 94 VLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVvvsnfasTLEQVVDQTPVKNviitGLGDL-LSAPKRTLVNfvvkyik 172
Cdd:PRK12467 1644 ILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL-------TQSHLQARLPLPD----GLRSLvLDQEDDWLEG------- 1705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 173 rlvpkYSLPHAISmrralragkkaqyvkpVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkef 252
Cdd:PRK12467 1706 -----YSDSNPAV----------------NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAAD---- 1760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 253 vvtALPLYHIFALTVNCLLFLH---KGAnNLLITNP---RDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSr 326
Cdd:PRK12467 1761 ---VVLQFTSFAFDVSVWELFWpliNGA-RLVIAPPgahRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLS- 1835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 327 LKLSIGGGMAVQRAVADKW-QNITKTRLLEGYGLTEASPLVA---CCPYDLAGYNGS-IGLPAPSTQIQVRGDDGQVLPQ 401
Cdd:PRK12467 1836 LRRVVCGGEALEVEALRPWlERLPDTGLFNLYGPTETAVDVThwtCRRKDLEGRDSVpIGQPIANLSTYILDASLNPVPI 1915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 402 GETGELFAKGPQVMLGYWQRPEETAK--VIDKDGWLA-----TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEV 474
Cdd:PRK12467 1916 GVAGELYLGGVGLARGYLNRPALTAErfVADPFGTVGsrlyrTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEAR 1995
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 475 VALHPKVVEvaAVGVPHE-VSGELVKIFVVAKDKSLTE---------KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGK 544
Cdd:PRK12467 1996 LREQGGVRE--AVVIAQDgANGKQLVAYVVPTDPGLVDddeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGK 2073
|
....*.
gi 655376187 545 ILRREL 550
Cdd:PRK12467 2074 LDRKAL 2079
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
47-551 |
1.24e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 105.36 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 47 ATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:PLN02654 119 ASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNF-----ASTLEQVVDQT---PVKNVIITGLG---DLLSAPKRTLVNFVVK---YIKRLVPKYSLPHAISMrralra 192
Cdd:PLN02654 198 TCNAVkrgpkTINLKDIVDAAldeSAKNGVSVGICltyENQLAMKREDTKWQEGrdvWWQDVVPNYPTKCEVEW------ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 193 gkkaqyvkpvVKSDDIAFLQYTGGTTGVSKGamlshgnivanVLQANGAYapllndgkeFVVTALPLYH--------IFA 264
Cdd:PLN02654 272 ----------VDAEDPLFLLYTSGSTGKPKG-----------VLHTTGGY---------MVYTATTFKYafdykptdVYW 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 265 LTVNCLLF----------LHKGANNLLITNPRDIPG------FVAELKKTPF-TALTGVNTLfnaLVNSEEFAAlDFSRL 327
Cdd:PLN02654 322 CTADCGWItghsyvtygpMLNGATVLVFEGAPNYPDsgrcwdIVDKYKVTIFyTAPTLVRSL---MRDGDEYVT-RHSRK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 328 KLSIGGGMA----------VQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDlagyNGSIGLPAPSTQIQVRGDDGQ 397
Cdd:PLN02654 398 SLRVLGSVGepinpsawrwFFNVVGDSRCPISDTWWQTETGGFMITPLPGAWPQK----PGSATFPFFGVQPVIVDEKGK 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 398 VLpQGE-TGELFAKGP-----QVMLGYWQRpEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEV 471
Cdd:PLN02654 474 EI-EGEcSGYLCVKKSwpgafRTLYGDHER-YETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEV 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 472 EEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDK-SLTE---KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILR 547
Cdd:PLN02654 552 ESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGvPYSEelrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
....
gi 655376187 548 RELR 551
Cdd:PLN02654 632 RILR 635
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
470-544 |
2.71e-23 |
|
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: 93.38 E-value: 2.71e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 470 EVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKD-KSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGK 544
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-550 |
3.59e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.65 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 1 MDQPWiNSLPADVPAEIDASRyaslleMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIM 80
Cdd:PRK12316 3042 LLEAW-NATAAEYPLERGVHR------LFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLI-ERGVGPDVLVGVA 3113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAivvvsnfastleqvvdqtpvknviitglgdLLSAPK 160
Cdd:PRK12316 3114 VERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQL------------------------------LLSQSH 3163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 161 rtlvnfvvkyikrlvpkYSLPHAISMRRAL--RAGKKAQYVKPVVKS--DDIAFLQYTGGTTGVSKGAMLSHGNIVANVL 236
Cdd:PRK12316 3164 -----------------LRLPLAQGVQVLDldRGDENYAEANPAIRTmpENLAYVIYTSGSTGKPKGVGIRHSALSNHLC 3226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 237 QANGAYAPLLNDgkefVVTALPLYHIFALTVNCLLFLHKGANNLL--ITNPRDIPGFVAELKKTPFTALTGVNTLFNALV 314
Cdd:PRK12316 3227 WMQQAYGLGVGD----RVLQFTTFSFDVFVEELFWPLMSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL 3302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 315 nsEEFAALDFSRLKLSIGGGMAVQRAVADKWqnITKTRLLEGYGLTEAS--PLVACCPYDLAGYnGSIGLPAPSTQIQVR 392
Cdd:PRK12316 3303 --EEEDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATitVTHWQCVEEGKDA-VPIGRPIANRACYIL 3377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWLA------TGDIGYMDEKGFFYIVDRKKDMILVSGFNV 466
Cdd:PRK12316 3378 DGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPgerlyrTGDLARYRADGVIEYIGRVDHQVKIRGFRI 3457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 467 FPNEVEEVVALHPKVVEVAAVGVPHEvsgELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKIL 546
Cdd:PRK12316 3458 ELGEIEARLLEHPWVREAVVLAVDGR---QLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLD 3534
|
....
gi 655376187 547 RREL 550
Cdd:PRK12316 3535 RKAL 3538
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
357-552 |
6.09e-23 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 101.61 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTE-ASPLVACCPYD-LAGYNGSiGLPAPSTQIQVRgddgqvlpQGETGELFAKGPQVMLGYWQrpeetaKVIDKDGW 434
Cdd:PRK07445 261 YGMTEtASQIATLKPDDfLAGNNSS-GQVLPHAQITIP--------ANQTGNITIQAQSLALGYYP------QILDSQGI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 435 LATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKSLTEKEL 514
Cdd:PRK07445 326 FETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEEL 405
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 655376187 515 IKHCRHHLTGYKVPK---LVEfrdELPKTNVGKILRRELRD 552
Cdd:PRK07445 406 KTAIKDQLSPFKQPKhwiPVP---QLPRNPQGKINRQQLQQ 443
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
352-554 |
6.16e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 102.41 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RLLEGYGLTEASPLVA---CCPydlagyNGSIGLPAPSTQI-----------QVRGDDGQVL-PQGETGELFAK-GPQVM 415
Cdd:PRK13388 290 QVEDGYGSSEGAVIVVrepGTP------PGSIGRGAPGVAIynpetltecavARFDAHGALLnADEAIGELVNTaGAGFF 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 416 LGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSG 495
Cdd:PRK13388 364 EGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 496 ELV-KIFVVAKDKSLTEKELIK--HCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:PRK13388 443 DQVmAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIAQG 504
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
27-550 |
7.13e-23 |
|
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: 101.74 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 27 EMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNP 106
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQS-LGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 107 LYTPRELKHQLVDsgakaivvvsnfastleqvvdqtpvknviiTGLGDLLSAPkrtlvnfvvkyikrlvpkyslphaism 186
Cdd:cd17644 83 NYPQERLTYILED------------------------------AQISVLLTQP--------------------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 187 rralragkkaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAP------LLNDGKEFVVTALPLY 260
Cdd:cd17644 106 -------------------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGItssdrvLQFASIAFDVAAEEIY 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 261 hifaltvnclLFLHKGANNLLITNP--RDIPGFVAELKKTPFTALTGVNTLFNALVN--SEEFAALDfSRLKLSIGGGMA 336
Cdd:cd17644 167 ----------VTLLSGATLVLRPEEmrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLelLLSTIDLP-SSLRLVIVGGEA 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 337 VQRAVADKWQNIT--KTRLLEGYGLTEASPLVACC----PYDLAGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAK 410
Cdd:cd17644 236 VQPELVRQWQKNVgnFIQLINVYGPTEATIAATVCrltqLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 411 GPQVMLGYWQRPEETAKVIDKDGWLA--------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKvV 482
Cdd:cd17644 316 GVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHND-V 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 483 EVAAVGVPHEVSGE--LVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17644 395 KTAVVIVREDQPGNkrLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-554 |
6.02e-22 |
|
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: 98.69 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 47 ATLTYRKLEERSRAFAAYLqNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:cd05910 1 SRLSFRELDERSDRIAQGL-TAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSnfastleqvvdqtpvknviitglgdllsapkrtlvnfvvkyikrlvpkyslphaismrralragkkaqyvkpvvKSD 206
Cdd:cd05910 80 GIP--------------------------------------------------------------------------KAD 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkefvvTALPLYHIFALtVNCLLFLHKGANNLLITNPR 286
Cdd:cd05910 86 EPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE------VDLATFPLFAL-FGPALGLTSVIPDMDPTRPA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 287 DI-PGFVAE-LKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNIT--KTRLLEGYGLTEA 362
Cdd:cd05910 159 RAdPQKLVGaIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVACCPYDL--------AGYNGS-IGLPAPSTQIQV---------RGDDGQVLPQGETGELFAKGPQVMLGYWQRPEE 424
Cdd:cd05910 239 LPVSSIGSRELlatttaatSGGAGTcVGRPIPGVRVRIieiddepiaEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 425 TA--KVIDKDG--WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGV--PHEVSGELV 498
Cdd:cd05910 319 TAlaKIDDNSEgfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVgkPGCQLPVLC 398
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655376187 499 --KIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVeFRDELP---KTNvGKILRRELRDEA 554
Cdd:cd05910 399 vePLPGTITPRARLEQELRALAKDYPHTQRIGRFL-IHPSFPvdiRHN-AKIFREKLAVWA 457
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
46-554 |
7.35e-22 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 98.65 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 46 GATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI 125
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQ-AQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 vvvsnfastleqvvdqtpvknviITGLGDLLsapkrtlvnfvvkyikrlvpkyslphaismrraLRAGKKAQYVKPVVKS 205
Cdd:cd05939 80 -----------------------IFNLLDPL---------------------------------LTQSSTEPPSQDDVNF 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVanvLQANGAYAPLLNDGKEFVVTALPLYHIFALTV---NCLLFlhkgANNLLI 282
Cdd:cd05939 104 RDKLFYIYTSGTTGLPKAAVIVHSRYY---RIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMgvgQALLH----GSTVVI 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQravadKWQNITK----TRLLEGYG 358
Cdd:cd05939 177 RKKFSASNFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQ-----IWEQFVRrfgiPQIGEFYG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASplvaCCPYDLAGYNGSIG-----LPA----------PSTQIQVRGDDGQVLP--QGETGELFAKGPQ-----VML 416
Cdd:cd05939 252 ATEGN----SSLVNIDNHVGACGfnsriLPSvypirlikvdEDTGELIRDSDGLCIPcqPGEPGLLVGKIIQndplrRFD 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 417 GYWQRpEETAKVIDK------DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVA--LHPKVVEVAAVG 488
Cdd:cd05939 328 GYVNE-GATNKKIARdvfkkgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSnvLGLEDVVVYGVE 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 489 VPHeVSGELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRDEA 554
Cdd:cd05939 407 VPG-VEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEG 471
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
49-481 |
1.58e-21 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 98.65 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVV 128
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVA-LGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 SNFASTLEQVVDQ-TPVKNVI-ITGLGDLLSAPKRTLVNFVVkyikrlvpkyslphaISMRRALRAGKKAQYVKPVVKSD 206
Cdd:PLN02387 186 SKQLKKLIDISSQlETVKRVIyMDDEGVDSDSSLSGSSNWTV---------------SSFSEVEKLGKENPVDPDLPSPN 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 207 DIAFLQYTGGTTGVSKGAMLSHGNIVANVlQANGAYAPLLNdGKEFVVTALPLYHIFALTVNCLLFLHKGA----NNLLI 282
Cdd:PLN02387 251 DIAVIMYTSGSTGLPKGVMMTHGNIVATV-AGVMTVVPKLG-KNDVYLAYLPLAHILELAAESVMAAVGAAigygSPLTL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 283 TN-----PRDIPGFVAELKKTPFTAL--------TGV-----------NTLFN-------ALVNSEEFAA---------- 321
Cdd:PLN02387 329 TDtsnkiKKGTKGDASALKPTLMTAVpaildrvrDGVrkkvdakgglaKKLFDiaykrrlAAIEGSWFGAwglekllwda 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 322 LDFSRLKLSIGG-------GMAVQRAVADKWQNIT-KTRLLEGYGLTEASPLVACCPYDLAGYnGSIGLPAPSTQIQ-VR 392
Cdd:PLN02387 409 LVFKKIRAVLGGrirfmlsGGAPLSGDTQRFINIClGAPIGQGYGLTETCAGATFSEWDDTSV-GRVGPPLPCCYVKlVS 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVL------PQGEtgeLFAKGPQVMLGYWQRPEETAKV--IDKDG--WLATGDIGYMDEKGFFYIVDRKKDMI-LV 461
Cdd:PLN02387 488 WEEGGYLisdkpmPRGE---IVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQ 564
|
490 500
....*....|....*....|
gi 655376187 462 SGFNVFPNEVEEVVALHPKV 481
Cdd:PLN02387 565 HGEYVSLGKVEAALSVSPYV 584
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
190-533 |
5.37e-21 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 97.01 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 190 LRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIV---ANVLQANGAYAPLLNDgKEFVVTALPLYHIFALT 266
Cdd:PLN02614 207 LKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVtliAGVIRLLKSANAALTV-KDVYLSYLPLAHIFDRV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 267 VNCLLFLHKGANNLLITNPRDIPGFVAELKKTPFTAL--------TGVNT-----------LFNALVN------------ 315
Cdd:PLN02614 286 IEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVprvldrvySGLQKklsdggflkkfVFDSAFSykfgnmkkgqsh 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 316 ---SEEFAALDFSRLKLSIGGGMAVQRAVADKWQNITKTRL--------LEGYGLTEASPLVACCPYDLAGYNGSIGLPA 384
Cdd:PLN02614 366 veaSPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLrvvacchvLQGYGLTESCAGTFVSLPDELDMLGTVGPPV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 385 PSTQIQVRG---DDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMI-L 460
Cdd:PLN02614 446 PNVDIRLESvpeMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFkL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 461 VSGFNVFPNEVEEVVAlHPKVVE------------VAAVGVPHE-----------VSGELVKIFVVAKDKSLTEKELIKH 517
Cdd:PLN02614 525 SQGEYVAVENIENIYG-EVQAVDsvwvygnsfesfLVAIANPNQqilerwaaengVSGDYNALCQNEKAKEFILGELVKM 603
|
410
....*....|....*..
gi 655376187 518 CRHH-LTGYKVPKLVEF 533
Cdd:PLN02614 604 AKEKkMKGFEIIKAIHL 620
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
206-550 |
3.21e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.62 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLqangAYAPLLNDGKEFVVtALPLYHIFALTV----NCLLFlhkGANNLL 281
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQL----SKVPYLALSEADVI-AQTASQSFDISVwqflAAPLF---GARVEI 3940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 ITN--PRDIPGFVAELKKTPFTALTGVNTLFNALVnSEEFAALDFSRLKLSIGGGMAVQraVADKW-QNITKTRLLEGYG 358
Cdd:PRK05691 3941 VPNaiAHDPQGLLAHVQAQGITVLESVPSLIQGML-AEDRQALDGLRWMLPTGEAMPPE--LARQWlQRYPQIGLVNAYG 4017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASPLVACCPYDLAGYNGS---IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLGYWQRPEETAKVIDKDGWL 435
Cdd:PRK05691 4018 PAECSDDVAFFRVDLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFG 4097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 436 A-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEvAAVGVPHEVSGELVKIFVVAKDKS 508
Cdd:PRK05691 4098 ApgerlyrTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTV 4176
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 655376187 509 LTEKELIKHCRHHLTG----YKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK05691 4177 LAQGALLERIKQRLRAelpdYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
48-552 |
7.79e-20 |
|
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: 93.18 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKaivv 127
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 128 vsnFASTLEQVVDQTPVKNviitglgdLLSAPKRTLVNfvvkyiKRLVPKYSLPHAISMRRalRAGKKAQYVKPVVKSDD 207
Cdd:cd05905 90 ---VALTVEACLKGLPKKL--------LKSKTAAEIAK------KKGWPKILDFVKIPKSK--RSKLKKWGPHPPTRDGD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTG------VSKGAMLSHGNIVANVLQANgayapllndGKEFVVTALPLYHIFALTVNCLLFLHKGANNLL 281
Cdd:cd05905 151 TAYIEYSFSSDGslsgvaVSHSSLLAHCRALKEACELY---------ESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTIL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 I------TNPrdiPGFVAELKK-TPFTALTGVNTLFNALVNSEEFAA------LDFSRLKLSIgggmavqraVAD--KWQ 346
Cdd:cd05905 222 IppelmkTNP---LLWLQTLSQyKVRDAYVKLRTLHWCLKDLSSTLAslknrdVNLSSLRMCM---------VPCenRPR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 347 NITKTRLLE-----GYGLTEASPLVACCPYDLAGYNGSIGlPAPSTQ-----------IQVRGDD----------GQVLP 400
Cdd:cd05905 290 ISSCDSFLKlfqtlGLSPRAVSTEFGTRVNPFICWQGTSG-PEPSRVyldmralrhgvVRLDERDkpnslplqdsGKVLP 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 401 ----------------QGETGELFAKGPQVMLGYWQRPEET------------AKVIDKDGWLATGDIGY---------- 442
Cdd:cd05905 369 gaqvaivnpetkglckDGEIGEIWVNSPANASGYFLLDGETndtfkvfpstrlSTGITNNSYARTGLLGFlrptkctdln 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 443 MDEKGFFYIVDRKKDMILVSGFNVFPNEVEE-VVALHPKVVEVAAVgvphEVSGELVkifVVAKDKSLTEKEL------- 514
Cdd:cd05905 449 VEEHDLLFVVGSIDETLEVRGLRHHPSDIEAtVMRVHPYRGRCAVF----SITGLVV---VVAEQPPGSEEEAldlvplv 521
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 655376187 515 IKHC--RHHLTGYKVpKLVEfRDELPKTNVGKILRRELRD 552
Cdd:cd05905 522 LNAIleEHQVIVDCV-ALVP-PGSLPKNPLGEKQRMEIRQ 559
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
201-551 |
7.83e-20 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 92.91 E-value: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 201 PVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVlqaNGAYAPLLNDGKEFVV-TALPLYHIFALTvncllFLHKGAnn 279
Cdd:PRK05851 147 TPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNL---RGLNARVGLDAATDVGcSWLPLYHDMGLA-----FLLTAA-- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 280 llitnprdIPGfvAELKKTPFTA-----------LTGVNTLFNALVN---------SEEFAALDFSRLKLSIGGGMAV-- 337
Cdd:PRK05851 217 --------LAG--APLWLAPTTAfsaspfrwlswLSDSRATLTAAPNfaynligkyARRVSDVDLGALRVALNGGEPVdc 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 338 ---QR-AVADKWQNITKTRLLEGYGLTEASPLVACcPY--------DLAGYNGS-------IGLPAPSTQIQVRGDDGQV 398
Cdd:PRK05851 287 dgfERfATAMAPFGFDAGAAAPSYGLAESTCAVTV-PVpgiglrvdEVTTDDGSgarrhavLGNPIPGMEVRISPGDGAA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 399 LPQG-ETGELFAKGPQVMLGYW-QRPeetakvIDKDGWLATGDIGYMDEKGFFyIVDRKKDMILVSGFNVFPNEVEEVVA 476
Cdd:PRK05851 366 GVAGrEIGEIEIRGASMMSGYLgQAP------IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 477 LHPKVVE--VAAVGVPhevSGELVKIFVVA-----KDKSLTEKELIKH----CrhhltGYkVPKLVEFRD--ELPKTNVG 543
Cdd:PRK05851 439 QVRGVREgaVVAVGTG---EGSARPGLVIAaefrgPDEAGARSEVVQRvaseC-----GV-VPSDVVFVApgSLPRTSSG 509
|
....*...
gi 655376187 544 KILRRELR 551
Cdd:PRK05851 510 KLRRLAVK 517
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
49-454 |
7.84e-20 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 92.96 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAaylqndLKLQK--GDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:PRK06334 46 LSYNQVRKAVIALA------TKVSKypDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNFASTLEQV---VDQTPVKNVIITGLGDLLSAPKRTLVNFVVkyikrlvpkySLPHAISMRRALRAGKKaqyvkpvv 203
Cdd:PRK06334 120 TSKQLMQHLAQThgeDAEYPFSLIYMEEVRKELSFWEKCRIGIYM----------SIPFEWLMRWFGVSDKD-------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 204 kSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDgkeFVVTALPLYHIFALTVNCLLFLHKGANNLLIT 283
Cdd:PRK06334 182 -PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDD---VMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAY 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 284 NPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQRAVADKWQNI-TKTRLLEGYGLTEA 362
Cdd:PRK06334 258 NPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTfPHIQLRQGYGTTEC 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 363 SPLVACCPYDLAGYNGSIGLPAPSTQIQVRGDDGQV-LPQGETGELFAKGPQVMLGYWQRPEETAKV-IDKDGWLATGDI 440
Cdd:PRK06334 338 SPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDFGQGFVeLGGETWYVTGDL 417
|
410
....*....|....
gi 655376187 441 GYMDEKGFFYIVDR 454
Cdd:PRK06334 418 GYVDRHGELFLKGR 431
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-550 |
1.43e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.31 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 25 LLEMLESAVNTYADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNV 104
Cdd:PRK05691 1133 LPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPL 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 105 NPLYTPRELKHQLVDSGAKAIVVVSNFASTLEQVvdqtpvKNVIITGLGDLlsapkrTLVNFVVKyikrlVPKYSLpHAi 184
Cdd:PRK05691 1212 DPDYPAERLAYMLADSGVELLLTQSHLLERLPQA------EGVSAIALDSL------HLDSWPSQ-----APGLHL-HG- 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 185 smrralragkkaqyvkpvvksDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAplLNDGKEFVVTAlPLYhiFA 264
Cdd:PRK05691 1273 ---------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYA--LDDSDVLMQKA-PIS--FD 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 265 LTV-NCLLFLHKGAnNLLITNP---RDiPGFVAEL-KKTPFTALTGVNTLFNALVnsEEFAALDFSRLKLSIGGGMAVQR 339
Cdd:PRK05691 1327 VSVwECFWPLITGC-RLVLAGPgehRD-PQRIAELvQQYGVTTLHFVPPLLQLFI--DEPLAAACTSLRRLFSGGEALPA 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 340 AVADK-WQNITKTRLLEGYGLTEASPLVA---CCPYDlaGYNGSIGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVM 415
Cdd:PRK05691 1403 ELRNRvLQRLPQVQLHNRYGPTETAINVThwqCQAED--GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLA 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 416 LGYWQRPEETAK--VIDKDG-----WLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKvVEVAAVG 488
Cdd:PRK05691 1481 RGYLGRPALTAErfVPDPLGedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPG-VAQAAVL 1559
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 489 VPHEVSG-ELVKIFVVAKDKSLTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK05691 1560 VREGAAGaQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
204-492 |
1.00e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 89.87 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 204 KSDDIAFLQYTGGTTGVSKGAMLSHGNiVANVLQANGAYAPLLNDG---KEFVVTALPLYHIFAlTVNCLLFLHKGAN-- 278
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEA-VATFVRGVDLFMEQFEDKmthDDVYLSFLPLAHILD-RMIEEYFFRKGASvg 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 279 ------NLLitnpRDIpgfVAELKKTPFT---------------ALTGVNTL----FNALVN----------SEEFAA-- 321
Cdd:PLN02430 296 yyhgdlNAL----RDD---LMELKPTLLAgvprvferihegiqkALQELNPRrrliFNALYKyklawmnrgySHKKASpm 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 322 ---LDF--------SRLKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEASPLVACCPYDLAGYNGSIGLPAPSTQIQ 390
Cdd:PLN02430 369 adfLAFrkvkaklgGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMLGTVGAPAVYNELR 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 391 VR-----GDDgqvlPQGET--GELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSG 463
Cdd:PLN02430 449 LEevpemGYD----PLGEPprGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQ 523
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 655376187 464 FNVFPNEVEEVVALHPKVVE------------VAAVGVPHE 492
Cdd:PLN02430 524 GEYVALEYLENVYGQNPIVEdiwvygdsfksmLVAVVVPNE 564
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
202-553 |
1.11e-17 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 85.95 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 202 VVKSDDIAFLQYTGGTTGVSKGAMLSHG-NIVANVLQANGayapLLNDGKEFVVTALPLYHIFAL---TVNCLLflhkGA 277
Cdd:cd05937 83 IVDPDDPAILIYTSGTTGLPKAAAISWRrTLVTSNLLSHD----LNLKNGDRTYTCMPLYHGTAAflgACNCLM----SG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 278 NNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAvqravADKWQ------NITKT 351
Cdd:cd05937 155 GTLALSRKFSASQFWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLR-----PDIWErfrerfNVPEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RllEGYGLTEAsplvaccPYDLAGYN------GSIGLPAPSTQIQVRGD---------DGQVL-----------PQGETG 405
Cdd:cd05937 230 G--EFYAATEG-------VFALTNHNvgdfgaGAIGHHGLIRRWKFENQvvlvkmdpeTDDPIrdpktgfcvraPVGEPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 406 E----LFAKGPQVMLGYWQRPEETAK-----VIDK-DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV 475
Cdd:cd05937 301 EmlgrVPFKNREAFQGYLHNEDATESklvrdVFRKgDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 476 ALHPKVVEVAAVGV--PH---EVSGELVKIFVVAKDKS-LTEKELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRE 549
Cdd:cd05937 381 GAHPDIAEANVYGVkvPGhdgRAGCAAITLEESSAVPTeFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGV 460
|
....
gi 655376187 550 LRDE 553
Cdd:cd05937 461 LRDE 464
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-550 |
3.50e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 85.99 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 37 ADQPAFVNMGATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQ 116
Cdd:PRK05691 2202 PQAPALTFAGQTLSYAELDARANRLARALR-ERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYM 2280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 117 LVDSGakaIVVVSNFASTLEqvvdqtpvknviitGLGDLLSApkrtlvnfvvkyikrlVPKYSLPHAISMRRALRAGKKA 196
Cdd:PRK05691 2281 IEDSG---IGLLLSDRALFE--------------ALGELPAG----------------VARWCLEDDAAALAAYSDAPLP 2327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 197 QYVKPvvksDDIAFLQYTGGTTGVSKGAMLSHGNIV---ANVLQANGAYApllnDGKEfvvtaLPLYHI-F-ALTVNCLL 271
Cdd:PRK05691 2328 FLSLP----QHQAYLIYTSGSTGKPKGVVVSHGEIAmhcQAVIERFGMRA----DDCE-----LHFYSInFdAASERLLV 2394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 272 FLHKGANNLLIT----NPRDIPGFVAELKKT--PFTALTGvNTLFNALVNSEEFaaldfSRLKLSIGGGMAVqraVADKW 345
Cdd:PRK05691 2395 PLLCGARVVLRAqgqwGAEEICQLIREQQVSilGFTPSYG-SQLAQWLAGQGEQ-----LPVRMCITGGEAL---TGEHL 2465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 346 QNITKT----RLLEGYGLTEA--SPLVACCPYDLAGYNGS--IGLPAPSTQIQVRGDDGQVLPQGETGELFAKGPQVMLG 417
Cdd:PRK05691 2466 QRIRQAfapqLFFNAYGPTETvvMPLACLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQG 2545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 418 YWQRPEETAKVIDKDGWLA-------TGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVE--VAAVG 488
Cdd:PRK05691 2546 YHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREavVLALD 2625
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 655376187 489 VPhevSGELVKIFVVAKDKSLTE------KELIK-HCRHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:PRK05691 2626 TP---SGKQLAGYLVSAVAGQDDeaqaalREALKaHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
201-462 |
2.27e-14 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 76.03 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 201 PVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANgayaPLLNDGKEFVVTA------LPLYHIFALTVNcLLFLH 274
Cdd:PLN02861 215 PPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLSTD----HLLKVTDRVATEEdsyfsyLPLAHVYDQVIE-TYCIS 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 275 KGAN-NLLITNPRDIPGFVAELKKTPFTAL--------TGVN-----------TLFNALVN----------SEEFAA--- 321
Cdd:PLN02861 290 KGASiGFWQGDIRYLMEDVQALKPTIFCGVprvydriyTGIMqkissggmlrkKLFDFAYNyklgnlrkglKQEEASprl 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 322 --LDFSRLKLSIGG-------GMA-VQRAVADKWQNITKTRLLEGYGLTEAsplVACCPYDLAG---YNGSIGLPAPStq 388
Cdd:PLN02861 370 drLVFDKIKEGLGGrvrlllsGAApLPRHVEEFLRVTSCSVLSQGYGLTES---CGGCFTSIANvfsMVGTVGVPMTT-- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 389 IQVR-------GDDGqvLPQGETGELFAKGPQVMLGYWQRPEETAKVIdKDGWLATGDIGYMDEKGFFYIVDRKKDMILV 461
Cdd:PLN02861 445 IEARlesvpemGYDA--LSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKL 521
|
.
gi 655376187 462 S 462
Cdd:PLN02861 522 S 522
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
24-462 |
2.31e-13 |
|
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: 72.87 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 24 SLLEMLESAVNTYADQPAF------VNMGA--------------TLTYRKLEERSRAFAAYLQNDLKLQKGDRVAIMMPN 83
Cdd:cd17632 23 RLAQIIATVMTGYADRPALgqrateLVTDPatgrttlrllprfeTITYAELWERVGAVAAAHDPEQPVRPGDFVAVLGFT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 84 LLQYPIALFGVLRAGMVVVnvnPLYT---PRELKHQLVDSGAKAIVV-VSNFASTLEQVVD-QTPVKNVIITGLGDL--- 155
Cdd:cd17632 103 SPDYATVDLALTRLGAVSV---PLQAgasAAQLAPILAETEPRLLAVsAEHLDLAVEAVLEgGTPPRLVVFDHRPEVdah 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 156 ---LSAPKRTLVNFVVKYIkrlvpkysLPHAISMRRalRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHgNIV 232
Cdd:cd17632 180 raaLESARERLAAVGIPVT--------TLTLIAVRG--RDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTE-RLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 233 ANVLQANGAyaplLNDGKEFVvtalplyhifALTVNCLLFLHKGANNLLItnprdipGFVAELKKTPFTALTGVNTLFN- 311
Cdd:cd17632 249 ATFWLKVSS----IQDIRPPA----------SITLNFMPMSHIAGRISLY-------GTLARGGTAYFAAASDMSTLFDd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 312 -ALVNSEEFA--------------ALDFSRLKLSIGGGMAVQRAVADKWQNITKTRLL---------------------- 354
Cdd:cd17632 308 lALVRPTELFlvprvcdmlfqryqAELDRRSVAGADAETLAERVKAELRERVLGGRLLaavcgsaplsaemkafmeslld 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 355 ----EGYGLTEASPLV--------ACCPYDLA-----GYNgSIGLPAPStqiqvrgddgqvlpqgetGELFAKGPQVMLG 417
Cdd:cd17632 388 ldlhDGYGSTEAGAVIldgvivrpPVLDYKLVdvpelGYF-RTDRPHPR------------------GELLVKTDTLFPG 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 655376187 418 YWQRPEETAKVIDKDGWLATGDIgyMDEKG---FFYiVDRKKDMILVS 462
Cdd:cd17632 449 YYKRPEVTAEVFDEDGFYRTGDV--MAELGpdrLVY-VDRRNNVLKLS 493
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
203-462 |
1.34e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 70.52 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 203 VKSDD---IAFLQYTGGTTGVSKGAMLSHGNIVANVlqangayAPLLNDG--KEFVVTA----LPLYHIFALTVNCLLFL 273
Cdd:PTZ00342 298 IQNEDpdfITSIVYTSGTSGKPKGVMLSNKNLYNTV-------VPLCKHSifKKYNPKThlsyLPISHIYERVIAYLSFM 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 274 HKGANNLLitnPRDIPGFVAELKKTPFTALTGVNTLFNALVNS--EEFAALDFSR------------------------- 326
Cdd:PTZ00342 371 LGGTINIW---SKDINYFSKDIYNSKGNILAGVPKVFNRIYTNimTEINNLPPLKrflvkkilslrksnnnggfskfleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 327 ---------------LKLSIGGGMAVQRAVADKWQNITKTRLLEGYGLTEAS-PLVAccpYDLAGYN-GSIGLP-APSTQ 388
Cdd:PTZ00342 448 ithisskikdkvnpnLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgPIFV---QHADDNNtESIGGPiSPNTK 524
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 655376187 389 IQVRG----DDGQVLPQGEtgeLFAKGPQVMLGYWQRPEETAKVIDKDGWLATGDIGYMDEKGFFYIVDRKKDMILVS 462
Cdd:PTZ00342 525 YKVRTwetyKATDTLPKGE---LLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLS 599
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
48-553 |
5.87e-12 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 68.57 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 48 TLTYRKLEERSRAfAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAI-- 125
Cdd:PLN03052 208 RMTLSELRSQVSR-VANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIft 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 126 --VVVSNFAST--LEQVVDQTPVKNVIITGLGDLLSAPKRTlvnfvvkyiKRLVPKYSLPHAISMRRAlragkkaQYVKP 201
Cdd:PLN03052 287 qdVIVRGGKSIplYSRVVEAKAPKAIVLPADGKSVRVKLRE---------GDMSWDDFLARANGLRRP-------DEYKA 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 202 VVKS-DDIAFLQYTGGTTGVSKGAMLSHgniVANVLQANGAYAPLlnDGKEFVVTALPL--------YHIFALTVN-CLL 271
Cdd:PLN03052 351 VEQPvEAFTNILFSSGTTGEPKAIPWTQ---LTPLRAAADAWAHL--DIRKGDIVCWPTnlgwmmgpWLVYASLLNgATL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 272 FLHKGAnnlliTNPRDIPGFVAELKktpFTALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAvqravadkwQNITKT 351
Cdd:PLN03052 426 ALYNGS-----PLGRGFAKFVQDAK---VTMLGTVPSIVKTWKNTNCMAGLDWSSIRCFGSTGEA---------SSVDDY 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 352 RLLEGYGltEASPLVACC----------------PYDLAGYNGsiglPAPSTQIQVRGDDGQVLPQGE--TGELfAKGPQ 413
Cdd:PLN03052 489 LWLMSRA--GYKPIIEYCggtelgggfvtgsllqPQAFAAFST----PAMGCKLFILDDSGNPYPDDApcTGEL-ALFPL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 414 vMLG-------------YWQ-RPEETAKVIDKDGwlatgDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV-ALH 478
Cdd:PLN03052 562 -MFGasstllnadhykvYFKgMPVFNGKILRRHG-----DIFERTSGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAAD 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 479 PKVVEVAAVGVPHEVSG-ELVKIFVVAKD---KSLTEKELIKHCRHHLTG-----YKVPKLVEFrDELPKTNVGKILRRE 549
Cdd:PLN03052 636 ESVLETAAIGVPPPGGGpEQLVIAAVLKDppgSNPDLNELKKIFNSAIQKklnplFKVSAVVIV-PSFPRTASNKVMRRV 714
|
....
gi 655376187 550 LRDE 553
Cdd:PLN03052 715 LRQQ 718
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
208-550 |
7.41e-11 |
|
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: 64.42 E-value: 7.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 208 IAFLQYTGGTTGVSKGAMLSHGNIVANVLQAngayAPLLNDGKEFVVTALPLYHIFALTVNCLLFLHKGAnNLLIT---- 283
Cdd:cd17654 120 LAYVIHTSGTTGTPKIVAVPHKCILPNIQHF----RSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGA-TLLIVptsv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 284 --NPRDIPGFVAELKKTPFTALTgvNTLFNALvNSEEFAALDFSRLK----LSIGGGMAVQRAVADKW-QNITKTRLLEG 356
Cdd:cd17654 195 kvLPSKLADILFKRHRITVLQAT--PTLFRRF-GSQSIKSTVLSATSslrvLALGGEPFPSLVILSSWrGKGNRTRIFNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 357 YGLTEAS--PLVACCPYDLAGYNgsIGLPAPSTQIQVRGDDGqvlpQGETGELFAKGpqVMLGYWQRPEETAKvidKDGW 434
Cdd:cd17654 272 YGITEVScwALAYKVPEEDSPVQ--LGSPLLGTVIEVRDQNG----SEGTGQVFLGG--LNRVCILDDEVTVP---KGTM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 435 LATGDIGYMdEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAavgVPHEVSGELVKIFVVAKDKSLTEKEL 514
Cdd:cd17654 341 RATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCA---VTLSDQQRLIAFIVGESSSSRIHKEL 416
|
330 340 350
....*....|....*....|....*....|....*.
gi 655376187 515 IKhcrHHLTGYKVPKLVEFRDELPKTNVGKILRREL 550
Cdd:cd17654 417 QL---TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
356-555 |
1.23e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 54.11 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 356 GYGLTEASPLVACCPYDlaGYNGsIGLPAPSTQIQVRGDdgqvlpqgetgELFAKGPQVMLGYWQRPEETAkVIDKDGWL 435
Cdd:PRK09029 270 GYGLTEMASTVCAKRAD--GLAG-VGSPLPGREVKLVDG-----------EIWLRGASLALGYWRQGQLVP-LVNDEGWF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 436 ATGDIGYMDEkGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELvKIFVVAKDKSLTEKELI 515
Cdd:PRK09029 335 ATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQR-PVAVVESDSEAAVVNLA 412
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 655376187 516 KHCRHHLTGYKVPklVEFRDeLPKT--NVG-KILRRELRDEAK 555
Cdd:PRK09029 413 EWLQDKLARFQQP--VAYYL-LPPElkNGGiKISRQALKEWVA 452
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
49-546 |
1.39e-07 |
|
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: 54.20 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 49 LTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIVVV 128
Cdd:cd05943 99 VTWAELRRRVARLAAALRA-LGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 129 sNFASTLEQVVDQTPVKNVIITGLGDLLsapKRTLVNFVVKYIKRLVPKYslPHAISMRRALRAGKKAQYVKPVVKSDDI 208
Cdd:cd05943 178 -DAYTYNGKRHDVREKVAELVKGLPSLL---AVVVVPYTVAAGQPDLSKI--AKALTLEDFLATGAAGELEFEPLPFDHP 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 209 AFLQYTGGTTGVSKGAMLSHGNIVANVLQANGayapLLNDGKE------FVVTALPLYH--IFALTVNCLLFLHKGanNL 280
Cdd:cd05943 252 LYILYSSGTTGLPKCIVHGAGGTLLQHLKEHI----LHCDLRPgdrlfyYTTCGWMMWNwlVSGLAVGATIVLYDG--SP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 281 LITNPRDIPGFVAELKKTPFtaltGVN-TLFNALvnsEEF-----AALDFSRLK--LSIGGGMAVQ--RAVADKWqnitK 350
Cdd:cd05943 326 FYPDTNALWDLADEEGITVF----GTSaKYLDAL---EKAglkpaETHDLSSLRtiLSTGSPLKPEsfDYVYDHI----K 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 351 TRLLEGY--GLTE-ASPLVACCPyDLAGYNGSIGLPAPSTQIQVRGDDGQVLPqGETGELFAKG--PQVMLGYWQRPEET 425
Cdd:cd05943 395 PDVLLASisGGTDiISCFVGGNP-LLPVYRGEIQCRGLGMAVEAFDEEGKPVW-GEKGELVCTKpfPSMPVGFWNDPDGS 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 426 ---AKVIDK-DGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIF 501
Cdd:cd05943 473 ryrAAYFAKyPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILF 552
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 655376187 502 VV-AKDKSLTEkELIKH----CRHHLTGYKVPKLVEFRDELPKTNVGKIL 546
Cdd:cd05943 553 VKlREGVELDD-ELRKRirstIRSALSPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| ac_ac_CoA_syn |
TIGR01217 |
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of ... |
47-552 |
1.10e-06 |
|
acetoacetyl-CoA synthase; This enzyme catalyzes the first step of the mevalonate pathway of IPP biosynthesis. Most bacteria do not use this pathway, but rather the deoxyxylulose pathway. [Central intermediary metabolism, Other]
Pssm-ID: 273507 [Multi-domain] Cd Length: 652 Bit Score: 51.42 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 47 ATLTYRKLEERSRAFAAYLQNdLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV 126
Cdd:TIGR01217 113 APVTWAELRRQVASLAAALRA-LGVRPGDRVSGYLPNIPQAVVAMLATASVGAIWSSCSPDFGARGVLDRFQQIEPKLLF 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 127 VVSNFA-STLEQVVDQTPVKnvIITGLGDLlsapKRTLVNFVVKYIKRLVPKysLPHAISMRRALRAGKKAQYVKPVVKS 205
Cdd:TIGR01217 192 TVDGYRyNGKEHDRRDKVAE--VRKELPTL----RAVVHIPYLGPRETEAPK--IDGALDLEDFTAAAQAAELVFEQLPF 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 206 DDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANGAYAPLLNDGKEFVVTALPL----YHIFALTVNCLLFLHKGANnlL 281
Cdd:TIGR01217 264 DHPLWILFSSGTTGLPKCIVHSAGGTLVQHLKEHGLHCDLGPGDRLFYYTTTGWmmwnWLVSGLATGATLVLYDGSP--G 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 282 ITNPRDIPGFVAELKKTPF-TALTGVNTLFNALVNSEEFAALDFSRLKLSIGGGMAVQ--RAVADKWQNITKTRLLEGyG 358
Cdd:TIGR01217 342 FPATNVLWDIAERTGATLFgTSAKYVMACRKAGVHPARTHDLSALQCVASTGSPLPPDgfRWVYDEIKADVWLASISG-G 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 359 LTEASPLVACCPyDLAGYNGSIGLPAPSTQIQVRGDDGQVLpQGETGELFAKG--PQVMLGYWQRPEET---AKVIDK-D 432
Cdd:TIGR01217 421 TDICSCFAGANP-TLPVHIGEIQAPGLGTAVQSWDPEGKPV-TGEVGELVCTNpmPSMPIRFWNDPDGSkyrDAYFDTyP 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 433 GWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFV-VAKDKSLTE 511
Cdd:TIGR01217 499 GVWRHGDWITLTPRGGIVIHGRSDSTLNPQGVRMGSAEIYNAVERLDEVRESLCIGQEQPDGGYRVVLFVhLAPGATLDD 578
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 655376187 512 ---KELIKHCRHHLTGYKVPKLVEFRDELPKTNVGKILRRELRD 552
Cdd:TIGR01217 579 allDRIKRTIRAGLSPRHVPDEIIEVPGIPHTLTGKRVEVAVKR 622
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
322-547 |
1.31e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.92 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 322 LDFSRLKLSI---GGGM---AVQRAVADKWqNItktRLLEGYGLTEASPLVAC-CPYDlAGY--NGSIGLPapstQIqVR 392
Cdd:COG1541 198 IDPRDLSLKKgifGGEPwseEMRKEIEERW-GI---KAYDIYGLTEVGPGVAYeCEAQ-DGLhiWEDHFLV----EI-ID 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 393 GDDGQVLPQGETGEL----FAKGPQVMLGYwqrpeetakvidkdgwlATGDIGY-MDEK---G-----FFYIVDRKKDMI 459
Cdd:COG1541 268 PETGEPVPEGEEGELvvttLTKEAMPLIRY-----------------RTGDLTRlLPEPcpcGrthprIGRILGRADDML 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 460 LVSGFNVFPNEVEEVVALHPKVVEVAAVGVPHEVSGELVKIFVVAKDKsLTEKELIKHCRHHLtgYKVPKL---VEF--R 534
Cdd:COG1541 331 IIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPG-ASLEALAEAIAAAL--KAVLGLraeVELveP 407
|
250
....*....|...
gi 655376187 535 DELPKTnVGKILR 547
Cdd:COG1541 408 GSLPRS-EGKAKR 419
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
37-240 |
4.45e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 46.33 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 37 ADQPAFVNMG-----ATLTYRKLEERSRAFAAYLQnDLKLQKGDRVAIMMPNLLQYPIALFGVLRAGMVVVNVNPlytpr 111
Cdd:PRK03584 98 DDRPAIIFRGedgprRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSP----- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 112 elkhqlvDSGAKAivVVSNFAStLEQVV--------------DQTPVKNVIITGLGDLlsapKRTLvnfVVKYIKRLVPK 177
Cdd:PRK03584 172 -------DFGVQG--VLDRFGQ-IEPKVliavdgyryggkafDRRAKVAELRAALPSL----EHVV---VVPYLGPAAAA 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655376187 178 YSLPHAISMRRALRAGKKAQYVKPVVKSDDIAFLQYTGGTTGVSKGAMLSHGNIVANVLQANG 240
Cdd:PRK03584 235 AALPGALLWEDFLAPAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELG 297
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
81-557 |
8.58e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 45.19 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 81 MPNLLQYPIALFGVLRAGMVVVNVNPLYTPRELKHQLVDSGAKAIV---VVSNFASTL---EQVVDQTPVKNVIITGLGD 154
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFtqdVVLRGGRALplySKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 155 LLSAPKRtlvNFVVKYIKRLVPKYSLPHAISMrralragkkaqYVKPVVK-SDDIAFLQYTGGTTGVSKGAMLSH----- 228
Cdd:PLN03051 81 PVAVPLR---EQDLSWCDFLGVAAAQGSVGGN-----------EYSPVYApVESVTNILFSSGTTGEPKAIPWTHlsplr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 229 -------------GNIVA---NVLQANGA---YAPLLNDGkefvvtALPLYHIFALTVNCLLFLHKGANNLLITnprdIP 289
Cdd:PLN03051 147 casdgwahmdiqpGDVVCwptNLGWMMGPwllYSAFLNGA------TLALYGGAPLGRGFGKFVQDAGVTVLGL----VP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 290 GFVAELKKTpftaltgvntlfnalvNSEEFAALDFSRLKLSIGGGMAvqRAVAD-KWQNITKtrlleGYglteASPLVAC 368
Cdd:PLN03051 217 SIVKAWRHT----------------GAFAMEGLDWSKLRVFASTGEA--SAVDDvLWLSSVR-----GY----YKPVIEY 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 369 CP-YDLA-GY-NGSIGLP-APS--------TQIQVRGDDGQVLPQGET--GELFAKGPqvMLGYWQRpeetakVIDKDG- 433
Cdd:PLN03051 270 CGgTELAsGYiSSTLLQPqAPGafstaslgTRFVLLNDNGVPYPDDQPcvGEVALAPP--MLGASDR------LLNADHd 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 434 ---------WLAT-------GDIGYMDEKGFFYIVDRKKDMILVSGFNVFPNEVEEVV-ALHPKVVEVAAVGVPHEVSG- 495
Cdd:PLN03051 342 kvyykgmpmYGSKgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACdRAVAGIAETAAVGVAPPDGGp 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 655376187 496 ELVKIFVVAKDKSLT-----EKELIKHCRHHLTG-----YKVPKlVEFRDELPKTNVGKILRRELRDEAKSA 557
Cdd:PLN03051 422 ELLVIFLVLGEEKKGfdqarPEALQKKFQEAIQTnlnplFKVSR-VKIVPELPRNASNKLLRRVLRDQLKKE 492
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
266-540 |
2.40e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 43.94 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 266 TVNCLLFLHK-------------GANNLLITNPRDIPGFVAELKKTPFTALTGVNTLFNALVNSEEFAALDFSRLKLSIG 332
Cdd:PRK07868 648 TVYCLTPLHHesgllvslggavvGGSRIALSRGLDPDRFVQEVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIG 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 333 GGMAvqravADKWQNITKT----RLLEGYGLTEASPLVAccpyDLAGYN-GSIGLPAPSTQiQVR-------------GD 394
Cdd:PRK07868 728 SGMP-----TGLWERVVEAfapaHVVEFFATTDGQAVLA----NVSGAKiGSKGRPLPGAG-RVElaaydpehdlileDD 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 395 DG--QVLPQGETGELFAKGPQvmlgywqRPEETAKVI-----DKDGWLATGDIGYMDEKGFFYIVDRKKDMILVSGFNVF 467
Cdd:PRK07868 798 RGfvRRAEVNEVGVLLARARG-------PIDPTASVKrgvfaPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVY 870
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 655376187 468 PNEVEEVVALHPKVVEVAAVGV---PHEVSgelVKIFVVAKDKSLTEKELIKHCRHHLTGYKvPKLVEFRDELPKT 540
Cdd:PRK07868 871 TEPVTDALGRIGGVDLAVTYGVevgGRQLA---VAAVTLRPGAAITAADLTEALASLPVGLG-PDIVHVVPEIPLS 942
|
|
| Pchlide_reductase_N |
cd01979 |
Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide) ... |
54-153 |
4.34e-04 |
|
Pchlide_reductase_N: N protein of the NB protein complex of Protochlorophyllide (Pchlide)_reductase. Pchlide reductase catalyzes the reductive formation of chlorophyllide (chlide) from protochlorophyllide (pchlide) during biosynthesis of chlorophylls and bacteriochlorophylls. This group contains both the light-independent Pchlide reductase (DPOR) and light-dependent Pchlide reductase (LPOR). Angiosperms contain only LPOR, cyanobacteria, algae and gymnosperms contain both DPOR and LPOR, primitive anoxygenic photosynthetic bacteria contain only DPOR. NB is structurally similar to the FeMo protein of nitrogenase, forming an N2B2 heterotetramer. N and B are homologous to the FeMo alpha and beta subunits respectively. Also in common with nitrogenase in vitro DPOR activity requires ATP hydrolysis and dithoionite or ferredoxin as electron donor. The NB protein complex may serve as a catalytic site for Pchlide reduction similar to MoFe for nitrogen reduction.
Pssm-ID: 238937 [Multi-domain] Cd Length: 396 Bit Score: 42.73 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 54 LEERSRAFAAYLQNDLKLQKGDRVAIMMPNLLQYPIALFgVLRAGMVVVNVNPLYTPRELKHQ---LVDSGAKaIVVVSN 130
Cdd:cd01979 256 LAEREARAWRALEPYLDLLRGKSIFFMGDNLLEIPLARF-LTRCGMIVVEVGTPYLDKRFQAAeleLLPPMVR-IVEKPD 333
|
90 100
....*....|....*....|...
gi 655376187 131 FASTLEQVVDQTPvkNVIITGLG 153
Cdd:cd01979 334 NYRQLDRIRELRP--DLVVTGLG 354
|
|
| PRK09275 |
PRK09275 |
bifunctional aspartate transaminase/aspartate 4-decarboxylase; |
63-150 |
5.48e-03 |
|
bifunctional aspartate transaminase/aspartate 4-decarboxylase;
Pssm-ID: 236444 Cd Length: 527 Bit Score: 39.46 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655376187 63 AYLQNDLK----LQKGDRVAIMMPNL---LQYPialfgVL-RAGMVVVNVNPL------YTPRELKhQLVDSGAKAIVVV 128
Cdd:PRK09275 175 CYIFDSLKenglLKAGDKIALMTPIFtpyLEIP-----ELpRYDLEVVHINADeenewqYPDSELE-KLRDPSIKALFLV 248
|
90 100 110
....*....|....*....|....*....|...
gi 655376187 129 --SNFAS------TLEQVVDQTPVKN---VIIT 150
Cdd:PRK09275 249 npSNPPSvamsdeSLEKIADIVNEKRpdlMIIT 281
|
|
| |
