|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-502 |
0e+00 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 1014.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 1 MSNHLFDA-MRAAAPADAPFMRTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVY 79
Cdd:PRK07514 1 MNNNLFDAlRAAFADRDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 80 LPLNTAYTLAELDYFIGDAEPRLVVVASAAREGVATIAQRHGAI-VETLDADGSGSLLDLARDEPADFVDASRSADDLAA 158
Cdd:PRK07514 81 LPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPhVETLDADGTGSLLEAAAAAPDDFETVPRGADDLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSL 238
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 239 MPEATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIA 318
Cdd:PRK07514 241 MPRATVMMGVPTFYTRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGK 398
Cdd:PRK07514 321 GTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 399 DLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTE 478
Cdd:PRK07514 401 DLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
490 500
....*....|....*....|....
gi 1037244487 479 DLPRNTMGKVQKNILRQQYADLYT 502
Cdd:PRK07514 481 ELPRNTMGKVQKNLLREQYADLFA 504
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
24-495 |
0e+00 |
|
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: 583.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:cd05941 8 DGDSITYADLVARAARLANRLlALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVvasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsadDLAAILYTSGTTGRSKGAMLTHGNLLSN 182
Cdd:cd05941 88 VL--------------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 183 ALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEV--VSLMPEATMLMGVPTFYVRLLQSPR 260
Cdd:cd05941 118 VRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVaiSRLMPSITVFMGVPTIYTRLLQYYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 F--------GKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRV 332
Cdd:cd05941 198 AhftdpqfaRAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 333 TDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVI-SGGYNIYPK 411
Cdd:cd05941 278 VDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIkSGGYKVSAL 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 412 EVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGA-VLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:cd05941 358 EIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAaALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNK 437
|
....*
gi 1037244487 491 NILRQ 495
Cdd:cd05941 438 KELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
25-500 |
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: 516.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:COG0318 22 GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VAsaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsaddlaAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:COG0318 102 TA---------------------------------------------------LILYTSGTTGRPKGVMLTHRNLLANAA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFG 262
Cdd:COG0318 131 AIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERerVTVLFGVPTMLARLLRHPEFA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 263 KEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTS-NPYD-GKRIAGTVGLPLPDVRVRVTDPaTGLV 340
Cdd:COG0318 211 RYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTvNPEDpGERRPGSVGRPLPGVEVRIVDE-DGRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 341 LPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRI 420
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAH 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 421 EGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYADL 500
Cdd:COG0318 369 PGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
25-494 |
3.16e-161 |
|
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: 465.50 E-value: 3.16e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd05936 22 GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASaaregvatiaqrhgaivetldadgsgSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd05936 102 VAV--------------------------SFTDLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDY--WRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLM--PEATMLMGVPTFYVRLLQSPR 260
Cdd:cd05936 156 QIKAWleDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIrkHRVTIFPGVPTMYIALLNAPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN-MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPAtGL 339
Cdd:cd05936 236 FKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDD-GE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDR 419
Cdd:cd05936 315 ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037244487 420 IEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05936 394 HPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
25-496 |
1.75e-140 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 414.30 E-value: 1.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK07656 28 DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VAS-------AAREGVATIaqRHGAIVETLDADGSGSLLD-----LARDEPADFVdASRSADDLAAILYTSGTTGRSKGA 172
Cdd:PRK07656 108 VLGlflgvdySATTRLPAL--EHVVICETEEDDPHTEKMKtftdfLAAGDPAERA-PEVDPDDVADILFTSGTTGRPKGA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 173 MLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPT 250
Cdd:PRK07656 185 MLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETerITVLPGPPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQSPRFGKEAAANIRLFISGSA----PLLAETHTEFEARTghaILERYGMTETN-MNTSNPYDGKR--IAGTVGL 323
Cdd:PRK07656 265 MYNSLLQHPDRSAEDLSSLRLAVTGAAsmpvALLERFESELGVDI---VLTGYGLSEASgVTTFNRLDDDRktVAGTIGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 324 PLPDVRVRVTDPaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVIS 403
Cdd:PRK07656 342 AIAGVENKIVNE-LGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 404 GGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRN 483
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKN 500
|
490
....*....|...
gi 1037244487 484 TMGKVQKNILRQQ 496
Cdd:PRK07656 501 ATGKVLKRALREK 513
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
25-499 |
1.34e-138 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 409.58 E-value: 1.34e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK06187 29 GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASaarEGVATIAQ--------RHGAIVETLDADGSGSLL----DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGA 172
Cdd:PRK06187 109 VDS---EFVPLLAAilpqlptvRTVIVEGDGPAAPLAPEVgeyeELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 173 MLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATnVTLLAGASMVLLSKFDADEVVSLMPEA--TMLMGVPT 250
Cdd:PRK06187 186 VLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPY-LALMAGAKQVIPRRFDPENLLDLIETErvTFFFAVPT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYD-----GKRIAGTVGLP 324
Cdd:PRK06187 265 IWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETsPVVSVLPPEdqlpgQWTKRRSAGRP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 325 LPDVRVRVTDPAtGLVLPP--EQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVI 402
Cdd:PRK06187 345 LPGVEARIVDDD-GDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDRIKDVII 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPR 482
Cdd:PRK06187 423 SGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPR 502
|
490
....*....|....*..
gi 1037244487 483 NTMGKVQKNILRQQYAD 499
Cdd:PRK06187 503 TSVGKILKRVLREQYAE 519
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
25-490 |
1.55e-137 |
|
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: 403.91 E-value: 1.55e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17631 18 GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17631 98 -------------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFG 262
Cdd:cd17631 129 NALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERhrVTSFFLVPTMIQALLQHPRFA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 263 KEAAANIRLFISGSAPLLAETHTEFEARtGHAILERYGMTETNMNTS--NPYDGKRIAGTVGLPLPDVRVRVTDPAtGLV 340
Cdd:cd17631 209 TTDLSSLRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFVEVRIVDPD-GRE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 341 LPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFtGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRI 420
Cdd:cd17631 287 VPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEH 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 421 EGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:cd17631 366 PAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
155-489 |
9.91e-123 |
|
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: 362.37 E-value: 9.91e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATnVTLLAGASMVLLSKFDADE 234
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLL-GALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 235 VVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN--MNTSN 310
Cdd:cd04433 80 ALELIERekVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVATGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 311 PYDGKRIAGTVGLPLPDVRVRVTDPATGLvLPPEQTGMIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGY 390
Cdd:cd04433 160 PDDDARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATA-AVDEDGWYRTGDLGRLDEDGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQ 470
Cdd:cd04433 238 LYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVRERLAPYKV 317
|
330
....*....|....*....
gi 1037244487 471 PKRIIFTEDLPRNTMGKVQ 489
Cdd:cd04433 318 PRRVVFVDALPRTASGKID 336
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
22-495 |
1.61e-120 |
|
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: 362.40 E-value: 1.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVV-----ASAAREGVATIAQRHGAIVETLDADGSGSLLDLARDEPADFVDASRS---ADDLAAILYTSGTTGRSKGAM 173
Cdd:cd05926 89 LVLTpkgelGPASRAASKLGLAILELALDVGVLIRAPSAESLSNLLADKKNAKSEGvplPDDLALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 174 LTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTF 251
Cdd:cd05926 169 LTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWPDVRDynATWYTAVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 252 YVRLLQSPRFGKEAAANIRLFI-SGSAPLLAETHTEFEARTGHAILERYGMTET--NMnTSNPYD-GKRIAGTVGLPLpD 327
Cdd:cd05926 249 HQILLNRPEPNPESPPPKLRFIrSCSASLPPAVLEALEATFGAPVLEAYGMTEAahQM-TSNPLPpGPRKPGSVGKPV-G 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 328 VRVRVTDPaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYN 407
Cdd:cd05926 327 VEVRILDE-DGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 408 IYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGK 487
Cdd:cd05926 406 ISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGK 485
|
....*...
gi 1037244487 488 VQKNILRQ 495
Cdd:cd05926 486 IQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
24-489 |
5.61e-120 |
|
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: 360.76 E-value: 5.61e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGAIVE------TLDADGSGSLLDLARD---EPADFVDASRSADDLAAILYTSGTTGRSKGAML 174
Cdd:cd05911 87 FTDPDGLEKVKEAAKELGPKDKiivlddKPDGVLSIEDLLSPTLgeeDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLRDYWR--VTSDDRLIHALPIFHTHGLFvATNVTLLAGASMVLLSKFDADEVVSLMP--EATMLMGVPT 250
Cdd:cd05911 167 SHRNLIANLSQVQTFLYgnDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMPKFDSELFLDLIEkyKITFLYLVPP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVR 329
Cdd:cd05911 246 IAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNAtIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIY 409
Cdd:cd05911 326 AKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 410 PKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQ-PKRIIFTEDLPRNTMGKV 488
Cdd:cd05911 406 PAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQlRGGVVFVDEIPKSASGKI 485
|
.
gi 1037244487 489 Q 489
Cdd:cd05911 486 L 486
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
19-404 |
9.42e-118 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 352.77 E-value: 9.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 19 FMRTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDA 98
Cdd:pfam00501 13 ALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 99 EPRLVVVASAAR-EGVATIAQR--HGAIVETLDADGSGSLLDLARDEPADFVD----ASRSADDLAAILYTSGTTGRSKG 171
Cdd:pfam00501 93 GAKVLITDDALKlEELLEALGKleVVKLVLVLDRDPVLKEEPLPEEAKPADVPppppPPPDPDDLAYIIYTSGTTGKPKG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 172 AMLTHGNLLSNALTL----RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE-----A 242
Cdd:pfam00501 173 VMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDPAALLELierykV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 TMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDG---KRIAG 319
Cdd:pfam00501 253 TVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLdedLRSLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 320 TVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKD 399
Cdd:pfam00501 333 SVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKD 412
|
....*
gi 1037244487 400 LVISG 404
Cdd:pfam00501 413 QIKLG 417
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
25-488 |
1.02e-114 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 350.07 E-value: 1.02e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK05605 55 GATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 V----ASAAREGVATIAQRHGAIVE---------------------------TLDADGS---GSLLDLARDEPADFVDAS 150
Cdd:PRK05605 135 VwdkvAPTVERLRRTTPLETIVSVNmiaampllqrlalrlpipalrkaraalTGPAPGTvpwETLVDAAIGGDGSDVSHP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 151 R-SADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL-------TLRDywrvtSDDRLIHALPIFHTHGLFVATNVTLLAGA 222
Cdd:PRK05605 215 RpTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkawvpGLGD-----GPERVLAALPMFHAYGLTLCLTLAVSIGG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 223 SMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLqsprfgKEAAAN------IRLFISGSAPLLAETHTEFEARTGHA 294
Cdd:PRK05605 290 ELVLLPAPDIDLILDAMKKhpPTWLPGVPPLYEKIA------EAAEERgvdlsgVRNAFSGAMALPVSTVELWEKLTGGL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 295 ILERYGMTETN-MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPAT-GLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFT 372
Cdd:PRK05605 364 LVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 373 gDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVL 452
Cdd:PRK05605 444 -DGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAAL 522
|
490 500 510
....*....|....*....|....*....|....*.
gi 1037244487 453 DEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:PRK05605 523 DPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKV 558
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
23-499 |
2.63e-113 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 344.15 E-value: 2.63e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 lVVVASAAREGVATIAQRHGAIVETLDADGSGSLLDlarDEPADFVDasRSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:PRK06839 103 -VLFVEKTFQNMALSMQKVSYVQRVISITSLKEIED---RKIDNFVE--KNESASFIICYTSGTTGKPKGAVLTQENMFW 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSP 259
Cdd:PRK06839 177 NALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKhkVTVVMGVPTIHQALINCS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 260 RFGKEAAANIRLFISGSAPLLAETHTEFEARtGHAILERYGMTETN----MNTSNpyDGKRIAGTVGLPLPDVRVRVTDP 335
Cdd:PRK06839 257 KFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSptvfMLSEE--DARRKVGSIGKPVLFCDYELIDE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 ATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVES 415
Cdd:PRK06839 334 NKNKV-EVGEVGELLIRGPNVMKEYWNRPDATE-ETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQ 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK06839 412 VINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
....
gi 1037244487 496 QYAD 499
Cdd:PRK06839 492 QLKS 495
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
25-495 |
2.60e-107 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 327.72 E-value: 2.60e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGD----AFALSGRIAGAldtlgirpgDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEP 100
Cdd:PRK07787 23 GRVLSRSDlagaATAVAERVAGA---------RRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RLVVVAS-AAREGVATIAQRhgaivetLDADGsgsllDLARDEPadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNL 179
Cdd:PRK07787 94 QAWLGPApDDPAGLPHVPVR-------LHARS-----WHRYPEP--------DPDAPALIVYTSGTTGPPKGVVLSRRAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 180 LSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVV-SLMPEATMLMGVPTFYVRLLQS 258
Cdd:PRK07787 154 AADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYAqALSEGGTLYFGVPTVWSRIAAD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PRFGKeAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpATG 338
Cdd:PRK07787 234 PEAAR-ALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVD-EDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 339 LVLP--PEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGR-GKDLVISGGYNIYPKEVES 415
Cdd:PRK07787 312 GPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK07787 392 ALLGHPGVREAAVVGVPDDDLGQRIVAYVV--GADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
25-494 |
4.69e-107 |
|
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: 325.40 E-value: 4.69e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsadDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd05934 81 V-------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDA----DEVVSLMPEATMLMGVPTFYvrLLQSPR 260
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSAsrfwSDVRRYGATVTNYLGAMLSY--LLAQPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLfiSGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDPaTGLV 340
Cdd:cd05934 190 SPDDRAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD-DGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 341 LPPEQTGMIEIK---GPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEI 417
Cdd:cd05934 267 LPAGEPGELVIRglrGWGFFKGYYNMPEATAEAMRN-GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAI 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 418 DRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05934 346 LRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
25-503 |
3.83e-106 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 326.50 E-value: 3.83e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQRHGAIVETLD-----ADGSGSLLDLARD---EPADFVDASRSADDLAAILYTSGTTGRSKGAMLTH 176
Cdd:PRK08316 114 VDPALAPTAEAALALLPVDTLILSlvlggREAPGGWLDFADWaeaGSVAEPDVELADDDLAQILYTSGTESLPKGAMLTH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 177 GNLLSN---ALTLRDYwrvTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTF 251
Cdd:PRK08316 194 RALIAEyvsCIVAGDM---SADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTIEAerITSFFAPPTV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 252 YVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEAR-TGHAILERYGMTE-----TNMNtsnPYDGKRIAGTVGLPL 325
Cdd:PRK08316 271 WISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERlPGLRFYNCYGQTEiaplaTVLG---PEEHLRRPGSAGRPV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 326 PDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGG 405
Cdd:PRK08316 348 LNVETRVVDDD-GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG-GWFHSGDLGVMDEEGYITVVDRKKDMIKTGG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 406 YNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTM 485
Cdd:PRK08316 426 ENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPS 505
|
490
....*....|....*...
gi 1037244487 486 GKVQKNILRQQYADLYTR 503
Cdd:PRK08316 506 GKILKRELRERYAGAFTD 523
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
24-496 |
6.46e-106 |
|
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: 325.34 E-value: 6.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd05904 29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGaIVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd05904 109 FTTAELAEKLASLALPVV-LLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWR--VTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSP 259
Cdd:cd05904 188 AQFVAGEGsnSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEELLAAIERykVTHLPVVPPIVLALVKSP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 260 RFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETN---MNTSNPYDGKRIAGTVGLPLPDVRVRVTDP 335
Cdd:cd05904 268 IVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQGYGMTESTgvvAMCFAPEKDRAKYGSVGRLVPNVEAKIVDP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 ATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVES 415
Cdd:cd05904 348 ETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKvqknILRQ 495
Cdd:cd05904 428 LLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGK----ILRK 503
|
.
gi 1037244487 496 Q 496
Cdd:cd05904 504 E 504
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
22-499 |
5.26e-99 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 309.35 E-value: 5.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:COG0365 34 DGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASAAREGVATI--------AQRHGAIVETL----------DADGSGSLLDLARDEPADFVDASRSADDLAAILYTS 163
Cdd:COG0365 114 VLITADGGLRGGKVIdlkekvdeALEELPSLEHVivvgrtgadvPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 164 GTTGRSKGAMLTHGNLLSNALTLRDYW-RVTSDDRLIHALPIF----HTHGLFVAtnvtLLAGASMVLL---SKF-DADE 234
Cdd:COG0365 194 GTTGKPKGVVHTHGGYLVHAATTAKYVlDLKPGDVFWCTADIGwatgHSYIVYGP----LLNGATVVLYegrPDFpDPGR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 235 VVSLMPE--ATMLMGVPTFYVRLLqspRFGKEAAAN-----IRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN 307
Cdd:COG0365 270 LWELIEKygVTVFFTAPTAIRALM---KAGDEPLKKydlssLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 308 TSNPYDGKRI-AGTVGLPLPDVRVRVTDPaTGLVLPPEQTGMIEIKG--PNVFKGYWRMPEKTAAEF--TGDGFFISGDL 382
Cdd:COG0365 347 FISNLPGLPVkPGSMGKPVPGYDVAVVDE-DGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 383 GKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVG 459
Cdd:COG0365 426 ARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDelaKELQA 505
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1037244487 460 ALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYAD 499
Cdd:COG0365 506 HVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
27-495 |
9.03e-96 |
|
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: 296.98 E-value: 9.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVA 106
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 107 SAAREgvatiaQRHGAivetldadgsgslldlardEPadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL 186
Cdd:cd05903 81 ERFRQ------FDPAA-------------------MP----------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 187 RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKE 264
Cdd:cd05903 126 AERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREhgVTFMMGATPFLTDLLNAVEEAGE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 265 AAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDG--KRIAGTVGLPLPDVRVRVTDpATGLVLP 342
Cdd:cd05903 206 PLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPApeDRRLYTDGRPLPGVEIKVVD-DTGATLA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 343 PEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEG 422
Cdd:cd05903 285 PGVEGELLSRGPSVFLGYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037244487 423 VVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGAL-QDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd05903 364 VIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
28-500 |
9.35e-95 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 298.26 E-value: 9.35e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 WSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAS 107
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 AAR-----EGVATIA-----QRHGAI----------VETLDADGSG------SLLDLAR---DEPADFVDASRSADDLAA 158
Cdd:PRK08315 124 GFKdsdyvAMLYELApelatCEPGQLqsarlpelrrVIFLGDEKHPgmlnfdELLALGRavdDAELAARQATLDPDDPIN 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVL-LSKFDadevvs 237
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYpGEGFD------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 238 lmPEATM----------LMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTG-HAILERYGMTETN- 305
Cdd:PRK08315 278 --PLATLaaveeerctaLYGVPTMFIAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVIDKMHmSEVTIAYGMTETSp 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 -MNTSNPYDG--KRIAgTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDL 382
Cdd:PRK08315 356 vSTQTRTDDPleKRVT-TVGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 383 GKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQ 462
Cdd:PRK08315 435 AVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCR 514
|
490 500 510
....*....|....*....|....*....|....*...
gi 1037244487 463 DRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYADL 500
Cdd:PRK08315 515 GKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREMMIEE 552
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
24-498 |
4.20e-94 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 294.41 E-value: 4.20e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PRK09088 19 LGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGvatiaqrhGAIVETLDA-DGSGSLLDLARDEPADfvdasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSN 182
Cdd:PRK09088 99 LGDDAVAAG--------RTDVEDLAAfIASADALEPADTPSIP-------PERVSLILFTSGTSGQPKGVMLSERNLQQT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 183 ALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE----ATMLMGVPTFYVRLLQS 258
Cdd:PRK09088 164 AHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDpalgITHYFCVPQMAQAFRAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PRFGKEAAANIRLFISGSAPLLAETHTEFEARtGHAILERYGMTETNMNTSNPYDGKRI---AGTVGLPLPDVRVRVTDp 335
Cdd:PRK09088 244 PGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDVIrakAGAAGIPTPTVQTRVVD- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 ATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVES 415
Cdd:PRK09088 322 DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK09088 402 VLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRD 481
|
...
gi 1037244487 496 QYA 498
Cdd:PRK09088 482 ALA 484
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
29-493 |
2.33e-92 |
|
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: 287.84 E-value: 2.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASa 108
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 aregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRD 188
Cdd:cd05935 82 -------------------------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 189 YWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAA 266
Cdd:cd05935 119 WTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKykVTFWTNIPTMLVDLLATPEFKTRDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 ANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYDGKRIAgTVGLPLPDVRVRVTDPATGLVLPPEQ 345
Cdd:cd05935 199 SSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETmSQTHTNPPLRPKLQ-CLGIP*FGVDARVIDIETGRELPPNE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 346 TGMIEIKGPNVFKGYWRMPEKTAAEFTGDG---FFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEG 422
Cdd:cd05935 278 VGEIVVRGPQIFKGYWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPA 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 423 VVESAVIGVPHPDFGEGVTAIVVRKPG--AVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd05935 358 I*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
39-496 |
9.06e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 290.78 E-value: 9.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAAREGVATI-- 116
Cdd:PRK06710 61 RFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVqs 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 117 AQRHGAIVETLDADgsgsLLDLARDEPADFVDASRS--------------------------------ADDLAAILYTSG 164
Cdd:PRK06710 141 ATKIEHVIVTRIAD----FLPFPKNLLYPFVQKKQSnlvvkvsesetihlwnsvekevntgvevpcdpENDLALLQYTGG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 165 TTGRSKGAMLTHGNLLSNALtLRDYWR---VTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE 241
Cdd:PRK06710 217 TTGFPKGVMLTHKNLVSNTL-MGVQWLyncKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 --ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYDGKRIA 318
Cdd:PRK06710 296 hkVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVThSNFLWEKRVP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGK 398
Cdd:PRK06710 376 GSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVLQ-DGWLHTGDVGYMDEDGFFYVKDRKK 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 399 DLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTE 478
Cdd:PRK06710 455 DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRD 534
|
490
....*....|....*...
gi 1037244487 479 DLPRNTMGKVQKNILRQQ 496
Cdd:PRK06710 535 ELPKTTVGKILRRVLIEE 552
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-494 |
4.97e-91 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 281.47 E-value: 4.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 154 DDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK-FDA 232
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSPsFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 233 DEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAP----LLAETHTEFEARtghAILERYGMTETN- 305
Cdd:cd05917 82 LAVLEAIEKekCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPcppeLMKRVIEVMNMK---DVTIAYGMTETSp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 -MNTSNPYDG--KRIaGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDL 382
Cdd:cd05917 159 vSTQTRTDDSieKRV-NTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 383 GKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQ 462
Cdd:cd05917 238 AVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKAYCK 317
|
330 340 350
....*....|....*....|....*....|..
gi 1037244487 463 DRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05917 318 GKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
27-497 |
8.24e-91 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 286.88 E-value: 8.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV- 105
Cdd:PRK06188 37 RLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 -------ASAAREGVATIAQrhgaiVETLDADGSGS-LLDLARD-EPADFVDASRsADDLAAILYTSGTTGRSKGAMLTH 176
Cdd:PRK06188 117 papfverALALLARVPSLKH-----VLTLGPVPDGVdLLAAAAKfGPAPLVAAAL-PPDIAGLAYTGGTTGKPKGVMGTH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 177 GNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVAtnVTLLAGASMVLLSKFDADEVVSLMPE----ATMLmgVPTFY 252
Cdd:PRK06188 191 RSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFL--PTLLRGGTVIVLAKFDPAEVLRAIEEqritATFL--VPTMI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 253 VRLLQSPRFGKEAAANIRLFISGSAPL----LAETHtefeARTGHAILERYGMTETNMNTS-------NPYDGKRIAgTV 321
Cdd:PRK06188 267 YALLDHPDLRTRDLSSLETVYYGASPMspvrLAEAI----ERFGPIFAQYYGQTEAPMVITylrkrdhDPDDPKRLT-SC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:PRK06188 342 GRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFYYIVDRKKDMI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 402 ISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLP 481
Cdd:PRK06188 420 VTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLP 499
|
490
....*....|....*.
gi 1037244487 482 RNTMGKVQKNILRQQY 497
Cdd:PRK06188 500 LTALGKPDKKALRARY 515
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
25-495 |
1.26e-90 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 287.44 E-value: 1.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREG--VATIaqrhGAIVETLDADGSGSL-----------LDLARDEPADF--------------------VDASR 151
Cdd:PRK12583 123 CADAFKTSdyHAML----QELLPGLAEGQPGALacerlpelrgvVSLAPAPPPGFlawhelqargetvsrealaeRQASL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 152 SADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK-F 230
Cdd:PRK12583 199 DRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLVYPNEaF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 231 DADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETN-- 305
Cdd:PRK12583 279 DPLATLQAVEEerCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAeVQIAYGMTETSpv 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 -MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGK 384
Cdd:PRK12583 359 sLQTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLAT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 385 IDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDR 464
Cdd:PRK12583 438 MDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKAR 517
|
490 500 510
....*....|....*....|....*....|.
gi 1037244487 465 LARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK12583 518 IAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
25-496 |
3.29e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 283.39 E-value: 3.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHG---AIV----ETLDADGSGSLLDLARDEP-------------ADFVDASR-------SADDL 156
Cdd:PRK08314 113 IVGSELAPKVAPAVGNLRlrhVIVaqysDYLPAEPEIAVPAWLRAEPplqalapggvvawKEALAAGLappphtaGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 157 AAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVV 236
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDREAAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 237 SLMP--EATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYD 313
Cdd:PRK08314 273 RLIEryRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQThSNPPD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 GKRIaGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAA---EFTGDGFFISGDLGKIDSDGY 390
Cdd:PRK08314 353 RPKL-QCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEafiEIDGKRFFRTGDLGRMDEEGY 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV--LDEKTIVGALQDRLARY 468
Cdd:PRK08314 432 FFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAY 511
|
490 500
....*....|....*....|....*...
gi 1037244487 469 KQPKRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK08314 512 KYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
27-495 |
2.20e-88 |
|
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: 276.92 E-value: 2.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLvvva 106
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 107 saaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL 186
Cdd:cd05912 77 -----------------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 187 RDYWRVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVLLSKFDADEVVSLMPEA--TMLMGVPTFYVRLLQspRFGKE 264
Cdd:cd05912 110 ALNLGLTEDDNWLCALPLFHISGLSILMR-SVIYGMTVYLVDKFDAEQVLHLINSGkvTIISVVPTMLQRLLE--ILGEG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 265 AAANIRLFISGSAPLLAETHTEFEARtGHAILERYGMTET--NMNTSNPYDGKRIAGTVGLPLPDVRVRVTDPATglvlP 342
Cdd:cd05912 187 YPNNLRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETcsQIVTLSPEDALNKIGSAGKPLFPVELKIEDDGQ----P 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 343 PEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEG 422
Cdd:cd05912 262 PYEVGEILLKGPNVTKGYLNRPDATEESFE-NGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPA 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 423 VVESAVIGVPHPDFGEGVTAIVVRKpgAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd05912 341 IKEAGVVGIPDDKWGQVPVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
20-496 |
8.20e-87 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 277.32 E-value: 8.20e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 20 MRTGSGQ--TWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGD 97
Cdd:PRK13295 46 VRLGTGAprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 98 AEPRLVVVASAAR-----EGVATI-----AQRHgaiVETLDADGSGS----LLDLARDEPAD---FVDASR-SADDLAAI 159
Cdd:PRK13295 126 AESKVLVVPKTFRgfdhaAMARRLrpelpALRH---VVVVGGDGADSfealLITPAWEQEPDapaILARLRpGPDDVTQL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 160 LYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLM 239
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 240 PE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPL---LAETHTEfeaRTGHAILERYGMTETNMNT-SNPYD 313
Cdd:PRK13295 283 RTegVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIpgaLVERARA---ALGAKIVSAWGMTENGAVTlTKLDD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 G-KRIAGTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFtgDGFFISGDLGKIDSDGYVH 392
Cdd:PRK13295 360 PdERASTTDGCPLPGVEVRVVD-ADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIR 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 393 IVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGAL-QDRLARYKQP 471
Cdd:PRK13295 437 ISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIP 516
|
490 500
....*....|....*....|....*
gi 1037244487 472 KRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK13295 517 ERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
25-495 |
1.57e-85 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 271.84 E-value: 1.57e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK03640 25 EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQrhgAIVETLDAdgsgslldlARDEPADFVDASrSADDLAAILYTSGTTGRSKGAMLTHGN----LL 180
Cdd:PRK03640 105 TDDDFEAKLIPGIS---VKFAELMN---------GPKEEAEIQEEF-DLDEVATIMYTSGTTGKPKGVIQTYGNhwwsAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 181 SNALTLRdywrVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQs 258
Cdd:PRK03640 172 GSALNLG----LTEDDCWLAAVPIFHISGLSILMR-SVIYGMRVVLVEKFDAEKINKLLQTggVTIISVVSTMLQRLLE- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 pRFGKEA-AANIRLFISGSAP----LLAEThtefeARTGHAILERYGMTET--NMNTSNPYDGKRIAGTVGLPLPDVRVR 331
Cdd:PRK03640 246 -RLGEGTyPSSFRCMLLGGGPapkpLLEQC-----KEKGIPVYQSYGMTETasQIVTLSPEDALTKLGSAGKPLFPCELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 332 VTDpaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPK 411
Cdd:PRK03640 320 IEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 412 EVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRkpGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKN 491
Cdd:PRK03640 397 EIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
|
....
gi 1037244487 492 ILRQ 495
Cdd:PRK03640 475 ELKQ 478
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
25-494 |
5.92e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 272.79 E-value: 5.92e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTL-GIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR-L 102
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKaL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAA--------REG-----VATIAQRHGAIVETL------------------DADGSGSLLDLARDEPadFVDASR 151
Cdd:PRK05677 127 VCLANMAhlaekvlpKTGvkhviVTEVADMLPPLKRLLinavvkhvkkmvpayhlpQAVKFNDALAKGAGQP--VTEANP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 152 SADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDD---RLIHALPIFHTHGLFVATNVTLLAGASMVLLS 228
Cdd:PRK05677 205 QADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEgceILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 229 K-FDADEVVSLMP--EATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN 305
Cdd:PRK05677 285 NpRDLPAMVKELGkwKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 -MNTSNPYDGKRIaGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGK 384
Cdd:PRK05677 365 pVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIAL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 385 IDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDR 464
Cdd:PRK05677 443 IQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGETLTKEQVMEHMRAN 522
|
490 500 510
....*....|....*....|....*....|
gi 1037244487 465 LARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PRK05677 523 LTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
22-499 |
6.53e-84 |
|
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: 268.94 E-value: 6.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVylPLNT--AYTLAELDYFIGDAE 99
Cdd:COG1021 45 VDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI--PVFAlpAHRRAEISHFAEQSE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 100 PRLVVVASAA-----REGVATIAQRHGAIVETLDADGSGSLLDLA--RDEPADFVDASRSADDLAAILYTSGTTGRSKGA 172
Cdd:COG1021 123 AVAYIIPDRHrgfdyRALARELQAEVPSLRHVLVVGDAGEFTSLDalLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 173 MLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFH--------THGlfvatnvTLLAGASMVLLSKFDADEVVSLMPE--A 242
Cdd:COG1021 203 PRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfplsspgVLG-------VLYAGGTVVLAPDPSPDTAFPLIERerV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 TMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDG-KRIAGTV 321
Cdd:COG1021 276 TVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPeEVILTTQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GLPL-PDVRVRVTDPaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:COG1021 356 GRPIsPDDEVRIVDE-DGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQ 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKpGAVLDEKTIVGALQDR-LARYKQPKRIIFTED 479
Cdd:COG1021 435 INRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDA 513
|
490 500
....*....|....*....|
gi 1037244487 480 LPRNTMGKVQKNILRQQYAD 499
Cdd:COG1021 514 LPLTAVGKIDKKALRAALAA 533
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
26-496 |
2.59e-83 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 267.29 E-value: 2.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAAREGVATIAQRHGAIVETLDADGSGSLLD----LARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNL-- 179
Cdd:PRK07470 111 HADFPEHAAAVRAASPDLTHVVAIGGARAGLDyealVARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHGQMaf 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 180 -LSNALTlrDYWR-VTSDDRLIHALPIFHTHGLFVATNVTllAGASMVLLS--KFDADEVVSLMPE--ATMLMGVPTFYV 253
Cdd:PRK07470 191 vITNHLA--DLMPgTTEQDASLVVAPLSHGAGIHQLCQVA--RGAATVLLPseRFDPAEVWALVERhrVTNLFTVPTILK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 254 RLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTS-------NPYDGK--RIaGTVGLP 324
Cdd:PRK07470 267 MLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNITvlppalhDAEDGPdaRI-GTCGFE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 325 LPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:PRK07470 346 RTGMEVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR-DGWFRTGDLGHLDARGFLYITGRASDMYISG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNT 484
Cdd:PRK07470 424 GSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSG 503
|
490
....*....|..
gi 1037244487 485 MGKVQKNILRQQ 496
Cdd:PRK07470 504 YGKITKKMVREE 515
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
21-500 |
4.50e-81 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 263.50 E-value: 4.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEP 100
Cdd:COG1022 34 EDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RLVVVASAAR-EGVATIAQRHGAIVE--TLDADGSGS---------LLDLARD-EPADFVDASRSA---DDLAAILYTSG 164
Cdd:COG1022 114 KVLFVEDQEQlDKLLEVRDELPSLRHivVLDPRGLRDdprllsldeLLALGREvADPAELEARRAAvkpDDLATIIYTSG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 165 TTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGlFVATNVTLLAGASMVLLSkfDADEVVSLMPEA-- 242
Cdd:COG1022 194 TTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFE-RTVSYYALAAGATVAFAE--SPDTLAEDLREVkp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 TMLMGVPTFY--------VRLLQSPRF-----------GKEAAA---------------------------------NIR 270
Cdd:COG1022 271 TFMLAVPRVWekvyagiqAKAEEAGGLkrklfrwalavGRRYARarlagkspslllrlkhaladklvfsklrealggRLR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 271 LFISGSAPLLAETHTEFEArTGHAILERYGMTET-NMNTSNPYDGKRIaGTVGLPLPDVRVRVTDpatglvlppeqTGMI 349
Cdd:COG1022 351 FAVSGGAALGPELARFFRA-LGIPVLEGYGLTETsPVITVNRPGDNRI-GTVGPPLPGVEVKIAE-----------DGEI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 350 EIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVI-SGGYNIYPKEVESEIDRIEgVVESAV 428
Cdd:COG1022 418 LVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASP-LIEQAV 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 429 IgvphpdFGEG---VTAIVV------------------------RKPgAVLDE-KTIVGALQDRLARYKQPKRII----- 475
Cdd:COG1022 497 V------VGDGrpfLAALIVpdfealgewaeenglpytsyaelaQDP-EVRALiQEEVDRANAGLSRAEQIKRFRllpke 569
|
570 580
....*....|....*....|....*...
gi 1037244487 476 FTED---LPRnTMgKVQKNILRQQYADL 500
Cdd:COG1022 570 FTIEngeLTP-TL-KLKRKVILEKYADL 595
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
25-499 |
6.18e-81 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 262.26 E-value: 6.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 V----ASAAREGVATIAQRH-------------GAIVETL-----------DADGSGSLLD-LARDEPADFVDASRSADD 155
Cdd:PRK07059 126 VlenfATTVQQVLAKTAVKHvvvasmgdllgfkGHIVNFVvrrvkkmvpawSLPGHVRFNDaLAEGARQTFKPVKLGPDD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 156 LAAILYTSGTTGRSKGAMLTHGNLLSNALTLrDYW------RVTSDDRL--IHALPIFHTHGLFVATNVTLLAGASMVL- 226
Cdd:PRK07059 206 VAFLQYTGGTTGVSKGATLLHRNIVANVLQM-EAWlqpafeKKPRPDQLnfVCALPLYHIFALTVCGLLGMRTGGRNILi 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 227 ------------LSKFDadevVSLMPeatmlmGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA 294
Cdd:PRK07059 285 pnprdipgfikeLKKYQ----VHIFP------AVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 295 ILERYGMTETN-MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTG 373
Cdd:PRK07059 355 ITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDD-GNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 374 DGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAvLD 453
Cdd:PRK07059 434 DGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPA-LT 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1037244487 454 EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKvqknILRQQYAD 499
Cdd:PRK07059 513 EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGK----ILRRELRD 554
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
23-497 |
7.05e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 260.22 E-value: 7.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAREGVATIAQRHGAIVETL-----DADGSGSLLDLARDEPADFVDASRSADDLaaiLYTSGTTGRSKGAM--LT 175
Cdd:PRK08276 87 LIVSAALADTAAELAAELPAGVPLLlvvagPVPGFRSYEEALAAQPDTPIADETAGADM---LYSSGTTGRPKGIKrpLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLLSNA---LTLRDYWRVTSDD-RLIHALPIFHTHGLFVATNVTLLAGASmVLLSKFDADEVVSLMPE--ATMLMGVP 249
Cdd:PRK08276 164 GLDPDEAPgmmLALLGFGMYGGPDsVYLSPAPLYHTAPLRFGMSALALGGTV-VVMEKFDAEEALALIERyrVTHSQLVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPRFGKEA--AANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYDGKRIAGTVGLPLp 326
Cdd:PRK08276 243 TMFVRMLKLPEEVRARydVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTvITSEDWLAHPGSVGKAV- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 327 DVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGY 406
Cdd:PRK08276 322 LGEVRILDED-GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 407 NIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFTEDLPRN 483
Cdd:PRK08276 401 NIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDalaAELIAWLRGRLAHYKCPRSIDFEDELPRT 480
|
490
....*....|....
gi 1037244487 484 TMGKVQKNILRQQY 497
Cdd:PRK08276 481 PTGKLYKRRLRDRY 494
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
25-498 |
8.44e-81 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 261.61 E-value: 8.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDY---------FI 95
Cdd:PRK06087 47 GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWvlnkcqakmFF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 96 GD---AEPRLVVVASAAREGVATIaqRHGAIVETLDADGSGSLLD--LARDEP-ADFVDASrsADDLAAILYTSGTTGRS 169
Cdd:PRK06087 127 APtlfKQTRPVDLILPLQNQLPQL--QQIVGVDKLAPATSSLSLSqiIADYEPlTTAITTH--GDELAAVLFTSGTEGLP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 170 KGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMG 247
Cdd:PRK06087 203 KGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQqrCTCMLG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 248 VPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAEThTEFEARTGHAILERYGMTETNMNTSNPYDG--KRIAGTVGLPL 325
Cdd:PRK06087 283 ATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV-ARECQQRGIKLLSVYGSTESSPHAVVNLDDplSRFMHTDGYAA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 326 PDVRVRVTDPATGLVLPPEQTGMIEiKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGG 405
Cdd:PRK06087 362 AGVEIKVVDEARKTLPPGCEGEEAS-RGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 406 YNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVV-RKPGAVLDEKTIVGAL-QDRLARYKQPKRIIFTEDLPRN 483
Cdd:PRK06087 441 ENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRT 520
|
490
....*....|....*
gi 1037244487 484 TMGKVQKNILRQQYA 498
Cdd:PRK06087 521 ASGKIQKFLLRKDIM 535
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
26-494 |
2.35e-80 |
|
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: 257.01 E-value: 2.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVv 105
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 asaaregvatiaqrhgaivetldadgsgslldlardepadfvdasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA-L 184
Cdd:cd05919 88 ---------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKF-DADEVVSLMPE--ATMLMGVPTFYVRLLQSPRF 261
Cdd:cd05919 123 MAREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARfrPTVLYGVPTFYANLLDSCAG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 262 GKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYDGKRIaGTVGLPLPDVRVRVTDPAtGLV 340
Cdd:cd05919 203 SPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVgHIFLSNRPGAWRL-GSTGRPVPGYEIRLVDEE-GHT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 341 LPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRI 420
Cdd:cd05919 281 IPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNG-GWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQH 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 421 EGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEK---TIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05919 360 PAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
28-494 |
9.62e-80 |
|
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: 254.95 E-value: 9.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 WSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVas 107
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 aaregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLR 187
Cdd:cd05972 79 --------------------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 188 DYWRVTSDDrlIH---ALPIFHTHGLFVATNVtLLAGASMVL--LSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQ--S 258
Cdd:cd05972 115 YWLGLRPDD--IHwniADPGWAKGAWSSFFGP-WLLGATVFVyeGPRFDAERILELLERygVTSFCGPPTAYRMLIKqdL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PRFGKEAaanIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpATG 338
Cdd:cd05972 192 SSYKFSH---LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 339 LVLPPEQTGMIEIKGPNV--FKGYWRMPEKTAAEFTGDgFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESE 416
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPglFLGYVGDPEKTEASIRGD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 417 IDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKT---IVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd05972 347 LLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELaeeLQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
.
gi 1037244487 494 R 494
Cdd:cd05972 427 R 427
|
|
| pimA |
TIGR03205 |
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found ... |
29-494 |
1.01e-78 |
|
dicarboxylate--CoA ligase PimA; PimA, a member of a large family of acyl-CoA ligases, is found in a characteristic operon pimFABCDE for the metabolism of pimelate and related compounds. It is found, so far, in Bradyrhizobium japonicum and several strains of Rhodopseudomonas palustris. PimA from R. palustris was shown to be active as a CoA ligase for C(7) to C(14) dicarboxylates and fatty acids.
Pssm-ID: 132249 [Multi-domain] Cd Length: 541 Bit Score: 256.04 E-value: 1.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:TIGR03205 48 TYTELEAMAETAAAALLRAGYGKDASVALYLGNTPDHPINFFGALKAGARVVHLSPLDGERALSHKLSDSGARLLITSDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AreGVATIAQRHGA-------IVETLDADG-SGSLLDLARDEP-----ADFV-DASRSA-------DDLAAILYTSGTTG 167
Cdd:TIGR03205 128 A--ALLPMALKFLEkglldrlIVCEDDNWGkVGTPQAPIPADPrivtyADFVkGAAAPAewpavtpDDVALLQYTGGTTG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 168 RSKGAMLTHGNLLSnALTLRDYW----RVTSDD--RLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE 241
Cdd:TIGR03205 206 LPKGAMLTHGNLTS-AVSIYDVWgkpsRATRGDveRVICVLPLFHIYALTVILLRSLRRGDLISLHQRFDVAAVFRDIEE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 --ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYDGKRIA 318
Cdd:TIGR03205 285 krATVFPGVPTMWIALANDPSLEKRDLSSLATIGSGGAPLPVEVANFFERKTGLKLKSGWGMTETcSPGTGHPPEGPDKP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVT---DPATglVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGfFISGDLGKIDSDGYVHIVG 395
Cdd:TIGR03205 365 GSIGLMLPGIELDVVsldDPTK--VLPPGEVGELRIRGPNVTRGYWNRPEESAEAFVGDR-FLTGDIGYMDTDGYFFLVD 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 396 RGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV---LDEktIVGALQDRLARYKQPK 472
Cdd:TIGR03205 442 RKKDMIISGGFNVYPQMIEQAIYEHPGVQEVIVIGIPDQYRGEAAKAFVKLRPGAKpfsLDE--LRAFLAGKLGKHELPV 519
|
490 500
....*....|....*....|..
gi 1037244487 473 RIIFTEDLPRNTMGKVQKNILR 494
Cdd:TIGR03205 520 AVEFVDELPRTPVGKLSRHELR 541
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
29-494 |
2.21e-78 |
|
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: 254.22 E-value: 2.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQRHGAIVETLDA-------DGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:cd05959 111 LAPVLAAALTKSEHTLVVLIVsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYW 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTL-RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKF-DADEVVSLMPE--ATMLMGVPTFYVRLLQ 257
Cdd:cd05959 191 TAELYaRNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVFKRIRRyrPTVFFGVPTLYAAMLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 SPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYDGKRIaGTVGLPLPDVRVRVTDPA 336
Cdd:cd05959 271 APNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMlHIFLSNRPGRVRY-GTTGKPVPGYEVELRDED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 337 TGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESE 416
Cdd:cd05959 350 GGDV-ADGEPGELYVRGPSSATMYWNNRDKTRDTFQG-EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 417 IDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV---LDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd05959 428 LVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEdseALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
.
gi 1037244487 494 R 494
Cdd:cd05959 508 R 508
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
155-488 |
2.45e-78 |
|
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: 248.34 E-value: 2.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATnVTLLAGASMVLLSKFDADE 234
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLAL-ATFHAGGANVVMEKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 235 VVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPllaETHTEFEARTGHAILERYGMTET-NMNTSNP 311
Cdd:cd17637 80 ALELIEEekVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDAP---ETIQRFEETTGATFWSLYGQTETsGLVTLSP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 312 YDGKriAGTVGLPLPDVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYV 391
Cdd:cd17637 157 YRER--PGSAGRPGPLVRVRIVDDNDRPV-PAGETGEIVVRGPLVFQGYWNLPELTAYTFRN-GWHHTGDLGRFDEDGYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 392 HIVGRG--KDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYK 469
Cdd:cd17637 233 WYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELIEFVGSRIARYK 312
|
330
....*....|....*....
gi 1037244487 470 QPKRIIFTEDLPRNTMGKV 488
Cdd:cd17637 313 KPRYVVFVEALPKTADGSI 331
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
25-498 |
2.93e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 254.70 E-value: 2.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRlVV 104
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH-VV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQrhgAIVETLD---------ADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLT 175
Cdd:PRK07786 119 VTEAALAPVATAVR---DIVPLLStvvvaggssDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGAVLT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLLSNALTLRDYWRV-TSDDRLIHALPIFHTHGLFvATNVTLLAGASMVL--LSKFDADEVVSLMPE--ATMLMGVPT 250
Cdd:PRK07786 196 HANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGIG-SMLPGLLLGAPTVIypLGAFDPGQLLDVLEAekVTGIFLVPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQSPRfGKEAAANIRLFISGSAP----LLAETHTEFearTGHAILERYGMTETNMNTSNpYDGK---RIAGTVGL 323
Cdd:PRK07786 275 QWQAVCAEQQ-ARPRDLALRVLSWGAAPasdtLLRQMAATF---PEAQILAAFGQTEMSPVTCM-LLGEdaiRKLGSVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 324 PLPDVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVIS 403
Cdd:PRK07786 350 VIPTVAARVVDENMNDV-PVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIIS 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 404 GGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIV-VRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPR 482
Cdd:PRK07786 428 GGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPR 507
|
490
....*....|....*.
gi 1037244487 483 NTMGKVQKNILRQQYA 498
Cdd:PRK07786 508 NPAGKVLKTELRERYG 523
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
27-494 |
3.69e-78 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 256.81 E-value: 3.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYlPLN---TAYTLAELdyfIGDAEPRLV 103
Cdd:PRK07529 58 TWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINpllEPEQIAEL---LRAAGAKVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 V-------------VASAARE--GVATIAQRHGA---------IVETLDADGSGSLLD----LARdEPADFVDASR--SA 153
Cdd:PRK07529 134 VtlgpfpgtdiwqkVAEVLAAlpELRTVVEVDLArylpgpkrlAVPLIRRKAHARILDfdaeLAR-QPGDRLFSGRpiGP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 154 DDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK--FD 231
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATPqgYR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 232 ADEVVSLMPE------ATMLMGVPTFYVRLLQSPRfgkeAAANI---RLFISGSAPLLAETHTEFEARTGHAILERYGMT 302
Cdd:PRK07529 293 GPGVIANFWKiveryrINFLSGVPTVYAALLQVPV----DGHDIsslRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLT 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 303 E-TNMNTSNPYDGKRIAGTVGLPLP--DVRVRVTDPATGLV--LPPEQTGMIEIKGPNVFKGYWRmPEKTAAEFTGDGFF 377
Cdd:PRK07529 369 EaTCVSSVNPPDGERRIGSVGLRLPyqRVRVVILDDAGRYLrdCAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 378 ISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTI 457
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAEL 527
|
490 500 510
....*....|....*....|....*....|....*...
gi 1037244487 458 VGALQDRLA-RYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PRK07529 528 LAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
26-479 |
1.19e-77 |
|
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: 250.59 E-value: 1.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 asaaregvatiaqrhgaivetldadgsgslldlarDEPadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:cd05907 84 -----------------------------------EDP----------DDLATIIYTSGTTGRPKGVMLSHRNILSNALA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSkfDADEVVSLMPEA--TMLMGVPTFY------VRLLQ 257
Cdd:cd05907 119 LAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVrpTVFLAVPRVWekvyaaIKVKA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 SPR-----FGKEAAANIRLFISGSAPLLAETHTEFEArTGHAILERYGMTETN-MNTSNPYDGKRIaGTVGLPLPDVRVR 331
Cdd:cd05907 197 VPGlkrklFDLAVGGRLRFAASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSaVVTLNPPGDNRI-GTVGKPLPGVEVR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 332 VTDpatglvlppeqTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVI-SGGYNIYP 410
Cdd:cd05907 275 IAD-----------DGEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIItSGGKNISP 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 411 KEVESEIdRIEGVVESAVIgvphpdFGEG---VTAIVVRKPGAVLDEKT------------------------IVGALQD 463
Cdd:cd05907 344 EPIENAL-KASPLISQAVV------IGDGrpfLVALIVPDPEALEAWAEehgiaytdvaelaanpavraeieaAVEAANA 416
|
490
....*....|....*.
gi 1037244487 464 RLARYKQPKRIIFTED 479
Cdd:cd05907 417 RLSRYEQIKKFLLLPE 432
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
29-495 |
5.02e-77 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 250.63 E-value: 5.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQR----HGAIVETLDADGSGSLLDL---------ARDEPADFVDAS-RSAddlAAILYTSGTTGRSKGAML 174
Cdd:cd12119 107 FLPLLEAIAPRlptvEHVVVMTDDAAMPEPAGVGvlayeellaAESPEYDWPDFDeNTA---AAICYTSGTTGNPKGVVY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLR--DYWRVTSDDRLIHALPIFHTH--GL-FVATnvtlLAGASMVLLSKF-DADEVVSLMPE--ATMLM 246
Cdd:cd12119 184 SHRSLVLHAMAALltDGLGLSESDVVLPVVPMFHVNawGLpYAAA----MVGAKLVLPGPYlDPASLAELIERegVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 247 GVPTFYVRLLQSP-RFGKEAAANIRLFISGSA--PLLAETHTEFEARTGHAilerYGMTETN----MNTSNPYDGKRIAG 319
Cdd:cd12119 260 GVPTVWQGLLDHLeANGRDLSSLRRVVIGGSAvpRSLIEAFEERGVRVIHA----WGMTETSplgtVARPPSEHSNLSED 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 320 -------TVGLPLPDVRVRVTDPATGlVLP--PEQTGMIEIKGPNVFKGYWRMPEkTAAEFTGDGFFISGDLGKIDSDGY 390
Cdd:cd12119 336 eqlalraKQGRPVPGVELRIVDDDGR-ELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQ 470
Cdd:cd12119 414 LTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWL 493
|
490 500
....*....|....*....|....*
gi 1037244487 471 PKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd12119 494 PDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
22-490 |
6.71e-77 |
|
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: 248.90 E-value: 6.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVAsaaregvatiaqrhgaivetldadgsgslldlarDEpadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:cd05914 82 AIFVS----------------------------------DE-----------DDVALINYTSGTTGNSKGVMLTYRNIVS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSL-MPEATMLMGVPTFYV------- 253
Cdd:cd05914 117 NVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKIIALaFAQVTPTLGVPVPLViekifkm 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 254 ------------RLLQSP----RFGKEA--------AANIRLFISGSAPLLAEThTEFEARTGHAILERYGMTETN-MNT 308
Cdd:cd05914 197 diipkltlkkfkFKLAKKinnrKIRKLAfkkvheafGGNIKEFVIGGAKINPDV-EEFLRTIGFPYTIGYGMTETApIIS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 309 SNPYDGKRIaGTVGLPLPDVRVRVTDPAtglvlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSD 388
Cdd:cd05914 276 YSPPNRIRL-GSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 389 GYVHIVGRGKDLVISG-GYNIYPKEVESEIDRIEGVVESAVI---------GVPHPDF----GEGVTAIVVRKPGAVLDE 454
Cdd:cd05914 350 GYLYIRGRKKEMIVLSsGKNIYPEEIEAKINNMPFVLESLVVvqekklvalAYIDPDFldvkALKQRNIIDAIKWEVRDK 429
|
490 500 510
....*....|....*....|....*....|....*..
gi 1037244487 455 ktivgaLQDRLARYKQ-PKRIIFTEDLPRNTMGKVQK 490
Cdd:cd05914 430 ------VNQKVPNYKKiSKVKIVKEEFEKTPKGKIKR 460
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
29-493 |
1.18e-76 |
|
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: 247.36 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREgvatiaqrhgaivETLDADgsgSLLDLARDEPADF-VDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLR 187
Cdd:TIGR01923 81 LEE-------------KDFQAD---SLDRIEAAGRYETsLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 188 DYWRVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVLLSKFdADEVVSLM-PEATMLMGVPTFYVRLLQSpRFGKEaa 266
Cdd:TIGR01923 145 ENLGFTEDDNWLLSLPLYHISGLSILFR-WLIEGATLRIVDKF-NQLLEMIAnERVTHISLVPTQLNRLLDE-GGHNE-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 aNIRLFISG----SAPLLAETHTEfeartGHAILERYGMTET--NMNTSNPyDGKRIAGTVGLPLPDVRVRVTDPATglv 340
Cdd:TIGR01923 220 -NLRKILLGgsaiPAPLIEEAQQY-----GLPIYLSYGMTETcsQVTTATP-EMLHARPDVGRPLAGREIKIKVDNK--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 341 lppEQTGMIEIKGPNVFKGYWRMPEKTAAeFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRI 420
Cdd:TIGR01923 290 ---EGHGEIMVKGANLMKGYLYQGELTPA-FEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 421 EGVVESAVIGVPHPDFGEGVTAIVVRKpgAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:TIGR01923 366 PGIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
25-500 |
1.14e-75 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 248.42 E-value: 1.14e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQ----RHGAIVE--------------------TLDADGSGSLLDLARDEPADFVDASRSADDLAAIL 160
Cdd:PRK06178 136 ALDQLAPVVEQVRAetslRHVIVTSladvlpaeptlplpdslrapRLAAAGAIDLLPALRACTAPVPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 161 YTSGTTGRSKGAMLTHGNLLSNALTlrdYWRVT----SDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVV 236
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMVYTAAA---AYAVAvvggEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVAFM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 237 SLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIR--LFISGSAPLLAETHTEFEARTGHAILE-RYGMTETNmnTSNP 311
Cdd:PRK06178 293 AAVERyrVTRTVMLVDNAVELMDHPRFAEYDLSSLRqvRVVSFVKKLNPDYRQRWRALTGSVLAEaAWGMTETH--TCDT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 312 ---------YDGKRIAGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDL 382
Cdd:PRK06178 371 ftagfqdddFDLLSQPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDI 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 383 GKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQ 462
Cdd:PRK06178 450 GKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCR 529
|
490 500 510
....*....|....*....|....*....|....*....
gi 1037244487 463 DRLARYKQPK-RIIftEDLPRNTMGKVQKNILRQQYADL 500
Cdd:PRK06178 530 ENMAVYKVPEiRIV--DALPMTATGKVRKQDLQALAEEL 566
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
19-498 |
4.12e-75 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 245.37 E-value: 4.12e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 19 FMRTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDA 98
Cdd:PRK13391 16 VIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 99 EPRLVVVASAAREGVATIAQRHGAIVETLDADGSG------SLLDLARDEPADFVDASRSADDLaaiLYTSGTTGRSKG- 171
Cdd:PRK13391 96 GARALITSAAKLDVARALLKQCPGVRHRLVLDGDGelegfvGYAEAVAGLPATPIADESLGTDM---LYSSGTTGRPKGi 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 172 -AMLTHGNlLSNALTLRDY----WRVTSDDRLIHALPIFHTHGLFvATNVTLLAGASMVLLSKFDADEVVSLMPE--ATM 244
Cdd:PRK13391 173 kRPLPEQP-PDTPLPLTAFlqrlWGFRSDMVYLSPAPLYHSAPQR-AVMLVIRLGGTVIVMEHFDAEQYLALIEEygVTH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 245 LMGVPTFYVRLLQSPR--FGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTS-NPYDGKRIAGTV 321
Cdd:PRK13391 251 TQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTAcDSEEWLAHPGTV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GLPLPDVrVRVTDPAtGLVLPPEQTGMIEIKGPNVFKgYWRMPEKTAAEFTGDG-FFISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:PRK13391 331 GRAMFGD-LHILDDD-GAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFM 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFT 477
Cdd:PRK13391 408 IISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPalaAELIAFCRQRLSRQKCPRSIDFE 487
|
490 500
....*....|....*....|.
gi 1037244487 478 EDLPRNTMGKVQKNILRQQYA 498
Cdd:PRK13391 488 DELPRLPTGKLYKRLLRDRYW 508
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
25-496 |
4.21e-75 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 246.59 E-value: 4.21e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQRHGAIVET--LDADGSGSL------LDL-ARDEPADFVDASRSadDLAAILYTSGTTGRSKGAMLT 175
Cdd:PRK06155 124 VEAALLAALEAADPGDLPLPAVwlLDAPASVSVpagwstAPLpPLDAPAPAAAVQPG--DTAAILYTSGTTGPSKGVCCP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLlsnaltlrdYW---------RVTSDDRLIHALPIFHTHGL--FVAtnvTLLAGASMVLLSKFDA----DEVVSLMP 240
Cdd:PRK06155 202 HAQF---------YWwgrnsaedlEIGADDVLYTTLPLFHTNALnaFFQ---ALLAGATYVLEPRFSAsgfwPAVRRHGA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 241 EATMLMG--VPTfyvrLLQSPRFGKEAAANIRLFISGSAPllAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRiA 318
Cdd:PRK06155 270 TVTYLLGamVSI----LLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQR-P 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKG--PNVF-KGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVG 395
Cdd:PRK06155 343 GSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAWR-NLWFHTGDRVVRDADGWFRFVD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 396 RGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRII 475
Cdd:PRK06155 421 RIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVE 500
|
490 500
....*....|....*....|.
gi 1037244487 476 FTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK06155 501 FVAALPKTENGKVQKFVLREQ 521
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
25-497 |
1.56e-74 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 243.64 E-value: 1.56e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK06145 25 DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VAsaaREGVATIAQRHGAIVetLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLlsnal 184
Cdd:PRK06145 105 VD---EEFDAIVALETPKIV--IDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNL----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 tlrdYWR---------VTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPEATMLMG--VPTFYV 253
Cdd:PRK06145 175 ----HWKsidhvialgLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAwmAPVMLS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 254 RLLQSPRFGKEAAANIRLFISGSAPLLAETHTEF-EARTGHAILERYGMTETNMNTSNPYDGKRIA--GTVGLPLPDVRV 330
Cdd:PRK06145 251 RVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFtRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRALAHVEI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 331 RVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDgFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYP 410
Cdd:PRK06145 331 RIADGA-GRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIAS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 411 KEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:PRK06145 409 SEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK 488
|
....*..
gi 1037244487 491 NILRQQY 497
Cdd:PRK06145 489 RVLRDEL 495
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
29-497 |
1.24e-73 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 241.53 E-value: 1.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV---- 104
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIahad 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 ----VASAAREGV--------ATIAQRHGAIVETLDADGSGSLLD--LARDEPADfvdASRSADDlAAILYTSGTTGRSK 170
Cdd:PRK12406 93 llhgLASALPAGVtvlsvptpPEIAAAYRISPALLTPPAGAIDWEgwLAQQEPYD---GPPVPQP-QSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 171 G---AMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHT----HGLFVATnvtllAGASMVLLSKFDADEVVSLMPE-- 241
Cdd:PRK12406 169 GvrrAAPTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHSapnaYGLRAGR-----LGGVLVLQPRFDPEELLQLIERhr 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 -ATMLMgVPTFYVRLLQSPRFGKEA--AANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYDGKRI 317
Cdd:PRK12406 244 iTHMHM-VPTMFIRLLKLPEEVRAKydVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTfATSEDALSH 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 318 AGTVGLPLPDVRVRVTDpATGLVLPPEQTGMI--EIKGPNVFKgYWRMPEKTAaEFTGDGFFISGDLGKIDSDGYVHIVG 395
Cdd:PRK12406 323 PGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIysRIAGNPDFT-YHNKPEKRA-EIDRGGFITSGDVGYLDADGYLFLCD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 396 RGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRII 475
Cdd:PRK12406 400 RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIE 479
|
490 500
....*....|....*....|..
gi 1037244487 476 FTEDLPRNTMGKVQKNILRQQY 497
Cdd:PRK12406 480 IMAELPREDSGKIFKRRLRDPY 501
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
24-498 |
1.46e-73 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 242.19 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGAIVETLDADGSGSLL--DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:PLN02246 127 ITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHfsELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRD------YWrvTSDDRLIHALPIFHTHGLfvatNVTLL----AGASMVLLSKFDADEVVSLMP--EATMLMGVP 249
Cdd:PLN02246 207 SVAQQVDgenpnlYF--HSDDVILCVLPMFHIYSL----NSVLLcglrVGAAILIMPKFEIGALLELIQrhKVTIAPFVP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAIL-ERYGMTET----NMNTS---NPYDGKRIA-GT 320
Cdd:PLN02246 281 PIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLgQGYGMTEAgpvlAMCLAfakEPFPVKSGScGT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 321 VglplpdVR---VRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRG 397
Cdd:PLN02246 361 V------VRnaeLKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 398 KDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFT 477
Cdd:PLN02246 435 KELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFV 514
|
490 500
....*....|....*....|.
gi 1037244487 478 EDLPRNTMGKVQKNILRQQYA 498
Cdd:PLN02246 515 DSIPKAPSGKILRKDLRAKLA 535
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
25-494 |
1.95e-73 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 242.42 E-value: 1.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDT-LGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PRK12492 47 GVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 V----VASAAREGVATIAQRH--------------GAIVETL--------------DADGSGSLLDLARDEPADFVdaSR 151
Cdd:PRK12492 127 VylnmFGKLVQEVLPDTGIEYlieakmgdllpaakGWLVNTVvdkvkkmvpayhlpQAVPFKQALRQGRGLSLKPV--PV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 152 SADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDR----------LIHALPIFHTHGLFVATNVTLLAG 221
Cdd:PRK12492 205 GLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGqplmkegqevMIAPLPLYHIYAFTANCMCMMVSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 222 ASMVLLSkfDADEVVSLMPEA-----TMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAIL 296
Cdd:PRK12492 285 NHNVLIT--NPRDIPGFIKELgkwrfSALLGLNTLFVALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 297 ERYGMTETN-MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDG 375
Cdd:PRK12492 363 EGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDD-GNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEG 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 376 FFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVV-RKPGAVLDE 454
Cdd:PRK12492 442 WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVaRDPGLSVEE 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1037244487 455 ktIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PRK12492 522 --LKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
47-494 |
3.47e-73 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 241.88 E-value: 3.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 47 LGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV----ASAAREGVATIAQRHga 122
Cdd:PRK08974 69 LGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIvsnfAHTLEKVVFKTPVKH-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 123 IVETLDAD----GSGSLLD------------------------LARDEPADFVDASRSADDLAAILYTSGTTGRSKGAML 174
Cdd:PRK08974 147 VILTRMGDqlstAKGTLVNfvvkyikrlvpkyhlpdaisfrsaLHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAML 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLR-DYWRVTSDDR--LIHALPIFHTHGLFVatNVTL---LAGASMVLLSKFDADEVVSLMPEA--TMLM 246
Cdd:PRK08974 227 THRNMLANLEQAKaAYGPLLHPGKelVVTALPLYHIFALTV--NCLLfieLGGQNLLITNPRDIPGFVKELKKYpfTAIT 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 247 GVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN-MNTSNPYDGKRIAGTVGLPL 325
Cdd:PRK08974 305 GVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSpLVSVNPYDLDYYSGSIGLPV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 326 PDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGG 405
Cdd:PRK08974 385 PSTEIKLVDDD-GNEVPPGEPGELWVKGPQVMLGYWQRPEATD-EVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 406 YNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKpGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTM 485
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKK-DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNV 541
|
....*....
gi 1037244487 486 GKVQKNILR 494
Cdd:PRK08974 542 GKILRRELR 550
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
29-428 |
5.34e-72 |
|
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: 234.47 E-value: 5.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAS 107
Cdd:TIGR01733 1 TYRELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 AAREGVATIAQRHGAIVETLDADGSGSLLDLARDEPADfvdasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLR 187
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSG-------PDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 188 DYWRVTSDDRLIHALPIfhTHGLFVATN-VTLLAGASMVLLSKFDADEVVSLMPEA------TMLMGVPTFYVRLLQSPR 260
Cdd:TIGR01733 154 RRYGLDPDDRVLQFASL--SFDASVEEIfGALLAGATLVVPPEDEERDDAALLAALiaehpvTVLNLTPSLLALLAAALP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 fgkEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTE-TNMNTSNPYDGKRIAGTV----GLPLPDVRVRVTD 334
Cdd:TIGR01733 232 ---PALASLRLVILGGEALTPALVDRWRARGPGArLINLYGPTEtTVWSTATLVDPDDAPRESpvpiGRPLANTRLYVLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 335 PATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF--------FISGDLGKIDSDGYVHIVGRGKDLVISGGY 406
Cdd:TIGR01733 309 DDLRPV-PVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEFLGRIDDQVKIRGY 387
|
410 420
....*....|....*....|..
gi 1037244487 407 NIYPKEVESEIDRIEGVVESAV 428
Cdd:TIGR01733 388 RIELGEIEAALLRHPGVREAVV 409
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
155-490 |
6.41e-72 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 231.62 E-value: 6.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADE 234
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 235 VVSLMP--EATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAP----LLAETHTEFEARTghaILERYGMTETNMNT 308
Cdd:cd17638 81 ILEAIEreRITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATvpveLVRRMRSELGFET---VLTAYGLTEAGVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 309 -SNPYDG-KRIAGTVGLPLPDVRVRVTDPatglvlppeqtGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKID 386
Cdd:cd17638 158 mCRPGDDaETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 387 SDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLA 466
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|....
gi 1037244487 467 RYKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKVMK 330
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
25-488 |
8.23e-72 |
|
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: 234.73 E-value: 8.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VAsaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd05930 90 TD----------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIH-ALPIF--HTHGLFVAtnvtLLAGASMVLLSK---FDADEVVSLMPEA--TMLMGVPTFYVRLL 256
Cdd:cd05930 124 WMQEAYPLTPGDRVLQfTSFSFdvSVWEIFGA----LLAGATLVVLPEevrKDPEALADLLAEEgiTVLHLTPSLLRLLL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSPrfGKEAAANIRLFISGSAPLLAETHTEF-EARTGHAILERYGMTETNMNTS------NPYDGKRIagTVGLPLPDVR 329
Cdd:cd05930 200 QEL--ELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATyyrvppDDEEDGRV--PIGRPIPNTR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFI------SGDLGKIDSDGYVHIVGRGKDLVIS 403
Cdd:cd05930 276 VYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPgermyrTGDLVRWLPDGNLEFLGRIDDQVKI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 404 GGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRN 483
Cdd:cd05930 355 RGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
....*
gi 1037244487 484 TMGKV 488
Cdd:cd05930 435 PNGKV 439
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-488 |
1.60e-71 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 234.64 E-value: 1.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 35 ALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGA----VYLPLNTAYTLAELDYFIGDAEPRLVVVASAAR 110
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 111 EGVATIAQRHGAIVETLDADGsgslLDLARDEPADFVDASrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYW 190
Cdd:cd05922 81 DRLRDALPASPDPGTVLDADG----IRAARASAPAHEVSH---EDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 191 RVTSDDRLIHALPIFHTHGLFVaTNVTLLAGASMVL--LSKFDaDEVVSLMPE--ATMLMGVPTFYvRLLQSPRFGKEAA 266
Cdd:cd05922 154 GITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLtnDGVLD-DAFWEDLREhgATGLAGVPSTY-AMLTRLGFDPAKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 ANIRLFISGSAPLLAETHTEF-EARTGHAILERYGMTET--NMNTSNPYDGKRIAGTVGLPLPDVRVRVTDPaTGLVLPP 343
Cdd:cd05922 231 PSLRYLTQAGGRLPQETIARLrELLPGAQVYVMYGQTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDD-DGTPTPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 344 EQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGV 423
Cdd:cd05922 310 GEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037244487 424 VESAVIGVPhPDFGEGVTAIVVRKPGavLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:cd05922 390 IEAAAVGLP-DPLGEKLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKV 451
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
22-499 |
3.67e-70 |
|
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: 233.67 E-value: 3.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGiRPGDRVAVQVEKSAEALILYLACLRSGAV----YLPLNTAYtLAELDYFIGD 97
Cdd:cd05931 19 GGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIavplPPPTPGRH-AERLAAILAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 98 AEPRLVVVASAAREGVATIAQRHGAivetlDADGSGSLLDLARDEPAD-FVDASRSADDLAAILYTSGTTGRSKGAMLTH 176
Cdd:cd05931 97 AGPRVVLTTAAALAAVRAFAASRPA-----AGTPRLLVVDLLPDTSAAdWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 177 GNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVL----------------LSKFDAdevvslmp 240
Cdd:cd05931 172 RNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLmspaaflrrplrwlrlISRYRA-------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 241 eaTMlMGVPTFYVRLLQSpRFGKEAAANI-----RLFISGSAPLLAETHTEFEARTG------HAILERYGMTET----- 304
Cdd:cd05931 244 --TI-SAAPNFAYDLCVR-RVRDEDLEGLdlsswRVALNGAEPVRPATLRRFAEAFApfgfrpEAFRPSYGLAEAtlfvs 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 305 ----------------------NMNTSNPYDGKRIAGtVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWR 362
Cdd:cd05931 320 ggppgtgpvvlrvdrdalagraVAVAADDPAARELVS-CGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 363 MPEKTAAEF------TGDGFFISGDLGKIdSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVES---AVIGVPH 433
Cdd:cd05931 399 RPEATAETFgalaatDEGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcvAAFSVPD 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 434 PDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQ--PKRIIFTE--DLPRNTMGKVQKNILRQQYAD 499
Cdd:cd05931 478 DGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGvaPADVVLVRpgSIPRTSSGKIQRRACRAAYLD 547
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
39-494 |
3.39e-69 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 229.49 E-value: 3.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAARegvatiaq 118
Cdd:cd12118 41 RLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 119 rhgaiVETLDADGSGSLLDL-ARDEpadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDR 197
Cdd:cd12118 113 -----YEDLLAEGDPDFEWIpPADE-----------WDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 198 LIHALPIFHTHGLFVATNVTLLAGASmVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAAN-IRLFIS 274
Cdd:cd12118 177 YLWTLPMFHCNGWCFPWTVAAVGGTN-VCLRKVDAKAIYDLIEKhkVTHFCGAPTVLNMLANAPPSDARPLPHrVHVMTA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 275 GSAP---LLAEThtefeARTGHAILERYGMTET-----------NMNTSNPYDGKRIAGTVGLPLPDVR-VRVTDPATGL 339
Cdd:cd12118 256 GAPPpaaVLAKM-----EELGFDVTHVYGLTETygpatvcawkpEWDELPTEERARLKARQGVRYVGLEeVDVLDPETMK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPP--EQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEI 417
Cdd:cd12118 331 PVPRdgKTIGEIVFRGNIVMKGYLKNPEATAEAFRG-GWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVL 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 418 DRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFtEDLPRNTMGKVQKNILR 494
Cdd:cd12118 410 YKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLR 485
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
25-494 |
5.45e-69 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 227.36 E-value: 5.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd05958 8 EREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVAsaaregvatiaqrhgaivetldadgsgslldlardepadfvDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd05958 88 LCA-----------------------------------------HALTASDDICILAFTSGTTGAPKATMHFHRDPLASA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTL-RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPR 260
Cdd:cd05958 127 DRYaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARykPTVLFTAPTAYRAMLAHPD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET-NMNTSNPYDGKRIaGTVGLPLPDVRVRVTDpATGL 339
Cdd:cd05958 207 AAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMfHIFISARPGDARP-GATGKPVPGYEAKVVD-DEGN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPPEQTGMIEIKGPNvfkGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDR 419
Cdd:cd05958 285 PVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQ 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 420 IEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEkTIVGALQD----RLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05958 362 HPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGP-VLARELQDhakaHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
22-493 |
1.11e-65 |
|
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: 219.89 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVylPLNT--AYTLAELDYFIGDAE 99
Cdd:cd05920 35 VDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV--PVLAlpSHRRSELSAFCAHAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 100 PRLVVVASAAREgvatiaqrhgaivetldadgsgslldlaRDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNL 179
Cdd:cd05920 113 AVAYIVPDRHAG----------------------------FDHRALARELAESIPEVALFLLSGGTTGTPKLIPRTHNDY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 180 LSNALTLRDYWRVTSDDRLIHALPIFHTH-----GLFVatnvTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFY 252
Cdd:cd05920 165 AYNVRASAEVCGLDQDTVYLAVLPAAHNFplacpGVLG----TLLAGGRVVLAPDPSPDAAFPLIERegVTVTALVPALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 253 VRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYD-GKRIAGTVGLPL-PDVRV 330
Cdd:cd05920 241 SLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDpDEVIIHTQGRPMsPDDEI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 331 RVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYP 410
Cdd:cd05920 321 RVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 411 KEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAvldektiVGALQDR-------LARYKQPKRIIFTEDLPRN 483
Cdd:cd05920 400 EEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPP-------PSAAQLRrflrergLAAYKLPDRIEFVDSLPLT 472
|
490
....*....|
gi 1037244487 484 TMGKVQKNIL 493
Cdd:cd05920 473 AVGKIDKKAL 482
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
24-495 |
3.06e-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: 220.09 E-value: 3.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGAIVETLDADGSGSLLDLARDE------------PADFV-DASRSADDLAAILYTSGTTGRSK 170
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYtfitqnlppgfnEYDFKpPSFDRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 171 GAMLTHGNLLSNALTLRD---YWRVTSDDRLIHALPIFHTHGLFVaTNVTLLAGASMVLLSKFDADEVVSLMPE--ATML 245
Cdd:cd17642 201 GVQLTHKNIVARFSHARDpifGNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKFEEELFLRSLQDykVQSA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 246 MGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTG-HAILERYGMTETNMNTSNPYDGKRIAGTVGLP 324
Cdd:cd17642 280 LLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKlPGIRQGYGLTETTSAILITPEGDDKPGAVGKV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 325 LPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:cd17642 360 VPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPK-RIIFTEDLPRN 483
Cdd:cd17642 440 GYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKG 519
|
490
....*....|..
gi 1037244487 484 TMGKVQKNILRQ 495
Cdd:cd17642 520 LTGKIDRRKIRE 531
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
154-494 |
5.03e-65 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 214.65 E-value: 5.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 154 DDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLS----- 228
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 229 -KFDADEVVSLMP--EATMLMGVPTFYVRLLQSPrfGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTE-T 304
Cdd:cd05944 82 nPGLFDNFWKLVEryRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEaT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 305 NMNTSNPYDGKRIAGTVGLPLP--DVRVRVTDPATGLVLP--PEQTGMIEIKGPNVFKGYWRMPEKTAAeFTGDGFFISG 380
Cdd:cd05944 160 CLVAVNPPDGPKRPGSVGLRLPyaRVRIKVLDGVGRLLRDcaPDEVGEICVAGPGVFGGYLYTEGNKNA-FVADGWLNTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 381 DLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGA 460
Cdd:cd05944 239 DLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEEELLAW 318
|
330 340 350
....*....|....*....|....*....|....*
gi 1037244487 461 LQDRLA-RYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05944 319 ARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
21-494 |
8.64e-65 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 218.40 E-value: 8.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEP 100
Cdd:PRK08008 31 SGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RLVVVASA--------AREGVATIAQRHGAIVETLDADGSGSLLDLARDEPADFVDA-SRSADDLAAILYTSGTTGRSKG 171
Cdd:PRK08008 111 SLLVTSAQfypmyrqiQQEDATPLRHICLTRVALPADDGVSSFTQLKAQQPATLCYApPLSTDDTAEILFTSGTTSRPKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 172 AMLTHGNLLSNALtlrdY--WRV--TSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATML 245
Cdd:PRK08008 191 VVITHYNLRFAGY----YsaWQCalRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCKyrATIT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 246 MGVPTFYVRLLQSPRFGKEAAANIR--LFIsgsAPLLAETHTEFEARTGHAILERYGMTET--NMNTSNPYDgKRIAGTV 321
Cdd:PRK08008 267 ECIPMMIRTLMVQPPSANDRQHCLRevMFY---LNLSDQEKDAFEERFGVRLLTSYGMTETivGIIGDRPGD-KRRWPSI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GLPLPDVRVRVTDpATGLVLPPEQTGMIEIKG---PNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGK 398
Cdd:PRK08008 343 GRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRC 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 399 DLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTE 478
Cdd:PRK08008 422 NMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRK 501
|
490
....*....|....*.
gi 1037244487 479 DLPRNTMGKVQKNILR 494
Cdd:PRK08008 502 DLPRNCSGKIIKKNLK 517
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
25-494 |
9.23e-65 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 219.75 E-value: 9.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAG-ALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PRK08751 48 GKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQrhGAIVETLDADGSGSLLDLARDEPADFV--------------DASR------------------ 151
Cdd:PRK08751 128 VVIDNFGTTVQQVIA--DTPVKQVITTGLGDMLGFPKAALVNFVvkyvkklvpeyrinGAIRfrealalgrkhsmptlqi 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 152 SADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSD-----DRLIHALPIFHTHGLFVATNVTLLAGASMVL 226
Cdd:PRK08751 206 EPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegcEVVITALPLYHIFALTANGLVFMKIGGCNHL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 227 LSK-FDADEVVSLMPEA--TMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTE 303
Cdd:PRK08751 286 ISNpRDMPGFVKELKKTrfTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 304 TNMNTS-NPYDGKRIAGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDL 382
Cdd:PRK08751 366 TSPAACiNPLTLKEYNGSIGLPIPSTDACIKDDA-GTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDI 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 383 GKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGAlQ 462
Cdd:PRK08751 445 ARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHA-R 523
|
490 500 510
....*....|....*....|....*....|..
gi 1037244487 463 DRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PRK08751 524 ANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
28-495 |
2.00e-64 |
|
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: 215.37 E-value: 2.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 WSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVas 107
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 aaregvatiaqrhgaivetldaDGSgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL- 186
Cdd:cd05971 85 ----------------------DGS---------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVq 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 187 -------RD---YWrVTSDDRLIHAL-----PIFHtHGlfvatnVTLLAGASmvllSKFDADEVVSLMPE--ATMLMGVP 249
Cdd:cd05971 122 fpfnlfpRDgdlYW-TPADWAWIGGLldvllPSLY-FG------VPVLAHRM----TKFDPKAALDLMSRygVTTAFLPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNM---NTSNPYDGKriAGTVGLPLP 326
Cdd:cd05971 190 TALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLvigNCSALFPIK--PGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 327 DVRVRVTDpATGLVLPPEQTGMIEIKGPN--VFKGYWRMPEKTAAEFTGDgFFISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:cd05971 268 GHRVAIVD-DNGTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYFWYVGRDDDVITSS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGaVLDEKTIVGALQD----RLARYKQPKRIIFTEDL 480
Cdd:cd05971 346 GYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPG-ETPSDALAREIQElvktRLAAHEYPREIEFVNEL 424
|
490
....*....|....*
gi 1037244487 481 PRNTMGKVQKNILRQ 495
Cdd:cd05971 425 PRTATGKIRRRELRA 439
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
25-488 |
5.52e-64 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 215.66 E-value: 5.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGD----AFALSGRIAGaldtlGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEP 100
Cdd:cd05909 5 GTSLTYRKlltgAIALARKLAK-----MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RLVVVAsaaREGVATIAQRHGAIVETL-------DADGSGSLLD----------LARDEPADFVDASRSADDLAAILYTS 163
Cdd:cd05909 80 KTVLTS---KQFIEKLKLHHLFDVEYDarivyleDLRAKISKADkckaflagkfPPKWLLRIFGVAPVQPDDPAVILFTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 164 GTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLL-SKFDADEVVSLMPE- 241
Cdd:cd05909 157 GSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHpNPLDYKKIPELIYDk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 -ATMLMGVPTF---YVRLLQSPRFgkeaaANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTET----NMNTSNPyd 313
Cdd:cd05909 237 kATILLGTPTFlrgYARAAHPEDF-----SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspviSVNTPQS-- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 gKRIAGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFtGDGFFISGDLGKIDSDGYVHI 393
Cdd:cd05909 310 -PNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 394 VGRGKDLVISGGYNIYPKEVESEIDRIEGV-VESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQdrLARYKQPK 472
Cdd:cd05909 388 TGRLSRFAKIAGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNAG--ISNLAKPS 465
|
490
....*....|....*.
gi 1037244487 473 RIIFTEDLPRNTMGKV 488
Cdd:cd05909 466 YIHQVEEIPLLGTGKP 481
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
39-493 |
6.12e-64 |
|
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: 6.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAArEGVATIAQ 118
Cdd:cd05923 40 AVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAVDA-QVMDAIFQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 119 RHGAIVETLDADGSGSLldlARDEPAdFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL--RDYWRVTSDD 196
Cdd:cd05923 119 SGVRVLALSDLVGLGEP---ESAGPL-IEDPPREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 197 RLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMP--EATMLMGVPTFYVRLLQSPRFGKEAAANIRLFIS 274
Cdd:cd05923 195 VVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEqeRVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 275 GSA----PLLAETHTEFEARtghaILERYGMTETnMNTSnpYDGKRIAGTVGLPLPDVRVRVTDPATGLV--LPPEQTGM 348
Cdd:cd05923 275 AGAtmpdAVLERVNQHLPGE----KVNIYGTTEA-MNSL--YMRDARTGTEMRPGFFSEVRIVRIGGSPDeaLANGEEGE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 349 IEIK--GPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVES 426
Cdd:cd05923 348 LIVAaaADAAFTGYLNQPEATAKKLQ-DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEV 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 427 AVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd05923 427 VVIGVADERWGQSVTACVVPREGTLSADELDQFCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
26-480 |
1.36e-63 |
|
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: 214.14 E-value: 1.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:cd17640 84 EN--------------------------------------------DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRLIHALPIFHTHGLFVATNVtLLAGASMVLLS-KFDADEVVSLMPeaTMLMGVPT--------FYVRLL 256
Cdd:cd17640 120 LSDIVPPQPGDRFLSILPIWHSYERSAEYFI-FACGCSQAYTSiRTLKDDLKRVKP--HYIVSVPRlweslysgIQKQVS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSPRFGKEAA------ANIRLFISGSAPLLAETHTEFEArTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRV 330
Cdd:cd17640 197 KSSPIKQFLFlfflsgGIFKFGISGGGALPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 331 RVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKD-LVISGGYNIY 409
Cdd:cd17640 276 KIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDtIVLSNGENVE 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037244487 410 PKEVEseidriEGVVESAVIGvphpdfgegvTAIVVRKpgavlDEKTIvGAL----QDRLARYKQPKRIIFTEDL 480
Cdd:cd17640 356 PQPIE------EALMRSPFIE----------QIMVVGQ-----DQKRL-GALivpnFEELEKWAKESGVKLANDR 408
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-495 |
1.63e-63 |
|
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: 213.15 E-value: 1.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVasa 108
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 aregvaTIAQRHgaivetldadgsgslldlardepadfvdasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRD 188
Cdd:cd05973 79 ------DAANRH------------------------------KLDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 189 YWRVTSDDRLIHALPIFHTHGLFVATNVTLLAG-ASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYvRLLQSPRFGKEA 265
Cdd:cd05973 123 AVDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPTILLEGGFSVESTWRVIERlgVTNLAGSPTAY-RLLMAAGAEVPA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 266 AANIRLFISGSA--PLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRI--AGTVGLPLPDVRVRVTDPAtGLVL 341
Cdd:cd05973 202 RPKGRLRRVSSAgePLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPvhAGSAGRAMPGWRVAVLDDD-GDEL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 342 PPEQTGMIEIKGPNV----FKGYWRMPEKTAAeftgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEI 417
Cdd:cd05973 281 GPGEPGRLAIDIANSplmwFRGYQLPDTPAID----GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESAL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 418 DRIEGVVESAVIGVPHPDFGEGVTAIVVRKPG-----AVLDE-KTIVgalQDRLARYKQPKRIIFTEDLPRNTMGKVQKN 491
Cdd:cd05973 357 IEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGhegtpALADElQLHV---KKRLSAHAYPRTIHFVDELPKTPSGKIQRF 433
|
....
gi 1037244487 492 ILRQ 495
Cdd:cd05973 434 LLRR 437
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
149-488 |
6.85e-63 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 222.11 E-value: 6.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 149 ASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLL- 227
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHp 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 228 SKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN 305
Cdd:PRK08633 857 DPTDALGIAKLVAKhrATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETS 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 ----MNTSNPYDGKRI------AGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTA---AEFT 372
Cdd:PRK08633 937 pvasVNLPDVLAADFKrqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAeviKDID 1016
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 373 GDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRI--EGVVESAVIGVPHPDFGEGVtaIVVRKPGA 450
Cdd:PRK08633 1017 GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPDEKKGEKL--VVLHTCGA 1094
|
330 340 350
....*....|....*....|....*....|....*....
gi 1037244487 451 vLDEKTIVGAL-QDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:PRK08633 1095 -EDVEELKRAIkESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
40-494 |
8.13e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 214.02 E-value: 8.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 40 IAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTaytlaeldyfiGDAEPRLVVVAsaAREGVATIA-- 117
Cdd:PRK07788 87 LARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNT-----------GFSGPQLAEVA--AREGVKALVyd 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 118 QRHGAIVETLDADGSGSL-LDLARDEPADFVDASRSADDLAA----------------ILYTSGTTGRSKGAMLTHGNLL 180
Cdd:PRK07788 154 DEFTDLLSALPPDLGRLRaWGGNPDDDEPSGSTDETLDDLIAgsstaplpkppkpggiVILTSGTTGTPKGAPRPEPSPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 181 SN--ALTLRDYWRvtSDDRLIHALPIFHTHGLFVAtNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLL 256
Cdd:PRK07788 234 APlaGLLSRVPFR--AGETTLLPAPMFHATGWAHL-TLAMALGSTVVLRRRFDPEATLEDIAKhkATALVVVPVMLSRIL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSP--RFGKEAAANIRL-FISGSApLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYDGKRIAGTVGLPLPDVRVRV 332
Cdd:PRK07788 311 DLGpeVLAKYDTSSLKIiFVSGSA-LSPELATRALEAFGPVLYNLYGSTEVAFATiATPEDLAEAPGTVGRPPKGVTVKI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 333 TDPAtGLVLPPEQTGMIEIKGPNVFKGYW--RMPEKTaaeftgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYP 410
Cdd:PRK07788 390 LDEN-GNEVPRGVVGRIFVGNGFPFEGYTdgRDKQII------DGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFP 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 411 KEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:PRK07788 463 AEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLK 542
|
....
gi 1037244487 491 NILR 494
Cdd:PRK07788 543 RELR 546
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
21-496 |
2.28e-62 |
|
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: 212.33 E-value: 2.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAE 99
Cdd:cd05928 35 GKGDEVKWSFRELGSLSRKAANVLsGACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 100 PRLVVVASAAREGVATIAQ-----RHGAIVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAML 174
Cdd:cd05928 115 AKCIVTSDELAPEVDSVASecpslKTKLLVSEKSRDGWLNFKELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLRDYWR-VTSDDrlihalpIFHT---HGLFVATNVTL----LAGASMV--LLSKFDADEVVSLMPE--A 242
Cdd:cd05928 195 SHSSLGLGLKVNGRYWLdLTASD-------IMWNtsdTGWIKSAWSSLfepwIQGACVFvhHLPRFDPLVILKTLSSypI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 TMLMGVPTFYvRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVG 322
Cdd:cd05928 268 TTFCGAPTVY-RMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 323 LPLPDVRVRVTDpATGLVLPPEQTGMIEIK-GPN----VFKGYWRMPEKTAAEFTGDgFFISGDLGKIDSDGYVHIVGRG 397
Cdd:cd05928 347 KASPPYDVQIID-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGD-FYLTGDRGIMDEDGYFWFMGRA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 398 KDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPG-AVLDEKTIVGALQDRL----ARYKQPK 472
Cdd:cd05928 425 DDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQfLSHDPEQLTKELQQHVksvtAPYKYPR 504
|
490 500
....*....|....*....|....
gi 1037244487 473 RIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:cd05928 505 KVEFVQELPKTVTGKIQRNELRDK 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
155-501 |
3.19e-62 |
|
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: 206.03 E-value: 3.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVAtNVTLLAGASMVLLSKFDADE 234
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAIL-VRSLLAGAELVLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 235 VVSLMPEATMLMGVPTFYVRLLQSPrFGKEAAANIRLFISGSAPLLAETHTEFEARtGHAILERYGMTET-NMNTSNPYD 313
Cdd:cd17630 80 EDLAPPGVTHVSLVPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETaSQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 GKRiAGTVGLPLPDVRVRVTDPatglvlppeqtGMIEIKGPNVFKGYWRMPEKTaaEFTGDGFFISGDLGKIDSDGYVHI 393
Cdd:cd17630 158 GFG-RGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVP--EFNEDGWFTTKDLGELHADGRLTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 394 VGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKR 473
Cdd:cd17630 224 LGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--GRGPADPAELRAWLKDKLARFKLPKR 301
|
330 340
....*....|....*....|....*...
gi 1037244487 474 IIFTEDLPRNTMGKVQknilRQQYADLY 501
Cdd:cd17630 302 IYPVPELPRTGGGKVD----RRALRAWL 325
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
24-502 |
7.56e-62 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 211.62 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:PLN02574 63 TGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAREGVATIAQRHGAIVETLDADG----SGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGN 178
Cdd:PLN02574 143 AFTSPENVEKLSPLGVPVIGVPENYDFDSkrieFPKFYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRN 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 179 LLSNALTL-----RDYWRVTSDDRLIHALPIFHTHG--LFVATNVTLlaGASMVLLSKFDADEVVSLMP--EATMLMGVP 249
Cdd:PLN02574 223 LIAMVELFvrfeaSQYEYPGSDNVYLAALPMFHIYGlsLFVVGLLSL--GSTIVVMRRFDASDMVKVIDrfKVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPR-FGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETNMNTSNPYDGKRIA--GTVGLPL 325
Cdd:PLN02574 301 PILMALTKKAKgVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFIQGYGMTESTAVGTRGFNTEKLSkySSVGLLA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 326 PDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGG 405
Cdd:PLN02574 381 PNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 406 YNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTM 485
Cdd:PLN02574 461 FQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPA 540
|
490
....*....|....*..
gi 1037244487 486 GKvqknILRQQYADLYT 502
Cdd:PLN02574 541 GK----ILRRELKRSLT 553
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
23-496 |
3.14e-61 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 209.60 E-value: 3.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:PRK06164 31 DEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAR--------EGVATIAQR--HGAIVETLDADGSGSLLDLARDEPADFVD-------ASRSAD-DLAAILYT-S 163
Cdd:PRK06164 111 LVVWPGFKgidfaailAAVPPDALPplRAIAVVDDAADATPAPAPGARVQLFALPDpappaaaGERAADpDAGALLFTtS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 164 GTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVLLSKFDADEVVSLMPEA- 242
Cdd:PRK06164 191 GTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLG-ALAGGAPLVCEPVFDAARTARALRRHr 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 -TMLMGVPTFYVRLLQSPrfGKEAA-ANIRLF-ISGSAPLLAETHTEFEARtGHAILERYGMTE-----TNMNTSNPYDG 314
Cdd:PRK06164 270 vTHTFGNDEMLRRILDTA--GERADfPSARLFgFASFAPALGELAALARAR-GVPLTGLYGSSEvqalvALQPATDPVSV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 315 KRIAGtvGLPL-PDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHI 393
Cdd:PRK06164 347 RIEGG--GRPAsPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVY 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 394 VGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVtAIVVRKPGAVLDEKTIVGALQDRLARYKQPKR 473
Cdd:PRK06164 425 QTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDGASPDEAGLMAACREALAGFKVPAR 503
|
490 500
....*....|....*....|....*.
gi 1037244487 474 IIFTEDLPRNTMG---KVQKNILRQQ 496
Cdd:PRK06164 504 VQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
25-493 |
1.09e-60 |
|
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: 206.37 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd12116 10 DRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGvatiaqrhgaivetLDADGSGSLLDLARDE-PADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd12116 90 TDDALPDR--------------LPAGLPVLLLALAAAAaAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRVTSDDRL---------IHALPIFhthglfvatnVTLLAGASMVLLSKFDADEVVSLM-----PEATMLMGVP 249
Cdd:cd12116 156 HSMRERLGLGPGDRLlavttyafdISLLELL----------LPLLAGARVVIAPRETQRDPEALArlieaHSITVMQATP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSprfGKEAAANIRLFISGSA--PLLAEthtEFEARTGhAILERYGMTETNM-NTSNPYDGKRIAGTVGLPLP 326
Cdd:cd12116 226 ATWRMLLDA---GWQGRAGLTALCGGEAlpPDLAA---RLLSRVG-SLWNLYGPTETTIwSTAARVTAAAGPIPIGRPLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 327 DVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKD 399
Cdd:cd12116 299 NTQVYVLDAALRPV-PPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 400 LVISGGYNIYPKEVESEIDRIEGVVESAVIgVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTED 479
Cdd:cd12116 378 QVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDA 456
|
490
....*....|....
gi 1037244487 480 LPRNTMGKVQKNIL 493
Cdd:cd12116 457 LPLTANGKLDRKAL 470
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
29-498 |
1.85e-60 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 207.43 E-value: 1.85e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:PRK05852 45 SYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDAD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQRHGAIVETLDAD--GSGSLLDLARDE-----PADFVDASRSADDlAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:PRK05852 125 GPHDRAEPTTRWWPLTVNVGGDsgPSGGTLSVHLDAateptPATSTPEGLRPDD-AMIMFTGGTTGLPKMVPWTHANIAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPIFHTHGLfVATNVTLLAGASMVLL---SKFDA----DEVVSLmpEATMLMGVPTFYVR 254
Cdd:PRK05852 204 SVRAIITGYRLSPRDATVAVMPLYHGHGL-IAALLATLASGGAVLLparGRFSAhtfwDDIKAV--GATWYTAVPTIHQI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 LLQSPR---FGKEAAAnIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN-----------TSNPYDGKRIAGT 320
Cdd:PRK05852 281 LLERAAtepSGRKPAA-LRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQvtttqiegigqTENPVVSTGLVGR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 321 VGLPlpdvRVRVTDPaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:PRK05852 360 STGA----QIRIVGS-DGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT-DGWLRTGDLGSLSAAGDLSIRGRIKEL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDL 480
Cdd:PRK05852 434 INRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGL 513
|
490
....*....|....*...
gi 1037244487 481 PRNTMGKVQKNILRQQYA 498
Cdd:PRK05852 514 PHTAKGSLDRRAVAEQFG 531
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
25-488 |
3.17e-60 |
|
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: 204.79 E-value: 3.17e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd05945 14 GRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd05945 94 ADG----------------------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPiFH----THGLFVAtnvtLLAGASMVLLSKFDADEVVSL---MPEA--TMLMGVPTFYVRL 255
Cdd:cd05945 128 WMLSDFPLGPGDVFLNQAP-FSfdlsVMDLYPA----LASGATLVPVPRDATADPKQLfrfLAEHgiTVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 256 LQSPRFGKEAAANIRLFISGSAPLLAETHTEFEART-GHAILERYGMTETNMN-TSNPYDGKRIAG----TVGLPLPDVR 329
Cdd:cd05945 203 LLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAvTYIEVTPEVLDGydrlPIGYAKPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGD---GFFISGDLGKIDSDGYVHIVGRGKDLVISGGY 406
Cdd:cd05945 283 LVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 407 NIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV-LDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTM 485
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNAN 441
|
...
gi 1037244487 486 GKV 488
Cdd:cd05945 442 GKI 444
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
26-487 |
5.36e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 203.58 E-value: 5.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAAREGVATIAQRHG---AIVETldADGSGSLL--------DLARDEPADFVDASRSADDLAaILYTSGTTGRSKGAML 174
Cdd:PRK07798 107 EREFAPRVAEVLPRLPklrTLVVV--EDGSGNDLlpgavdyeDALAAGSPERDFGERSPDDLY-LLYTGGTTGMPKGVMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLRDYWRV----TSDD-----------RLIHALPIFHTHGLFvATNVTLLAGASMVLLS--KFDADEVVS 237
Cdd:PRK07798 184 RQEDIFRVLLGGRDFATGepieDEEElakraaagpgmRRFPAPPLMHGAGQW-AAFAALFSGQTVVLLPdvRFDADEVWR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 238 LMPE--ATMLMGVPTFYVR-LLQSPRFGKEA-AANIRLFISGSAPLLAETHTEF-EARTGHAILERYGMTET-NMNTSNP 311
Cdd:PRK07798 263 TIERekVNVITIVGDAMARpLLDALEARGPYdLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSETgFGGSGTV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 312 YDGkriAGTVGLPL--PDVRVRVTDPATGLVLP-PEQTGMIEIKGPnVFKGYWRMPEKTAAEF-TGDG--FFISGDLGKI 385
Cdd:PRK07798 343 AKG---AVHTGGPRftIGPRTVVLDEDGNPVEPgSGEIGWIARRGH-IPLGYYKDPEKTAETFpTIDGvrYAIPGDRARV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 386 DSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRL 465
Cdd:PRK07798 419 EADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSL 498
|
490 500
....*....|....*....|..
gi 1037244487 466 ARYKQPKRIIFTEDLPRNTMGK 487
Cdd:PRK07798 499 AGYKVPRAIWFVDEVQRSPAGK 520
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
22-494 |
6.85e-59 |
|
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: 202.19 E-value: 6.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:cd17651 15 VAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASAAREGVATIAqrhGAIVETLDAdgsgSLLDLARDEPadfvDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:cd17651 95 LVLTHPALAGELAVEL---VAVTLLDQP----GAAAGADAEP----DPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPI---FHTHGLFvatnVTLLAGASMVLLS---KFDADEVVSLMPEATM-LMGVPTFYVR 254
Cdd:cd17651 164 LVAWQARASSLGPGARTLQFAGLgfdVSVQEIF----STLCAGATLVLPPeevRTDPPALAAWLDEQRIsRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 -LLQSPRFGKEAAANIR-LFISGSAPLLAETHTEFEARTGHAILE-RYGMTETNMNTS----NPYDGKRIAGTVGLPLPD 327
Cdd:cd17651 240 aLAEHGRPLGVRLAALRyLLTGGEQLVLTEDLREFCAGLPGLRLHnHYGPTETHVVTAlslpGDPAAWPAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 328 VRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:cd17651 320 TRVYVLDAALRPV-PPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLGRADDQV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 402 ISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLP 481
Cdd:cd17651 399 KIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALP 478
|
490
....*....|...
gi 1037244487 482 RNTMGKVQKNILR 494
Cdd:cd17651 479 LTPNGKLDRRALP 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
25-493 |
2.60e-58 |
|
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: 200.58 E-value: 2.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRlVV 104
Cdd:cd17646 21 GRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA-VV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQRHGAIVETLDADGSGslldlarDEPADFVDasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17646 100 LTTADLAARLPAGGDVALLGDEALAAPPA-------TPPLVPPR----PDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPI-FHTHG--LFVAtnvtLLAGASMVLL---SKFDADEVVSLMPE--ATMLMGVPTFYVRLL 256
Cdd:cd17646 169 WMQDEYPLGPGDRVLQKTPLsFDVSVweLFWP----LVAGARLVVArpgGHRDPAYLAALIREhgVTTCHFVPSMLRVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSPRFGkeAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN-TSNPYDGKRIAGTV--GLPLPDVRVRVT 333
Cdd:cd17646 245 AEPAAG--SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDvTHWPVRGPAETPSVpiGRPVPNTRLYVL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 334 DPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGGYN 407
Cdd:cd17646 323 DDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFLGRSDDQVKIRGFR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 408 IYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV-LDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMG 486
Cdd:cd17646 402 VEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANG 481
|
....*..
gi 1037244487 487 KVQKNIL 493
Cdd:cd17646 482 KLDRAAL 488
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
159-488 |
9.75e-58 |
|
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: 194.44 E-value: 9.75e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATnVTLLAGASMVLLSKFDADEVVSL 238
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTL-ATFHAGGTNVFVRRVDAEEVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 239 MpEA-----TMLMGvPTfyvrLLQSPRFGKEAAANIRLFISGSA-----PLLAETHTEFEARTGHailerYGMTE-TNMN 307
Cdd:cd17636 84 I-EAercthAFLLP-PT----IDQIVELNADGLYDLSSLRSSPAapewnDMATVDTSPWGRKPGG-----YGQTEvMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 308 TSNPYDGKRIaGTVGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLGKIDS 387
Cdd:cd17636 153 TFAALGGGAI-GGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-GWHHTNDLGRREP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 388 DGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLAR 467
Cdd:cd17636 230 DGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIAS 309
|
330 340
....*....|....*....|.
gi 1037244487 468 YKQPKRIIFTEDLPRNTMGKV 488
Cdd:cd17636 310 YKKPKSVEFADALPRTAGGAD 330
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
19-496 |
4.50e-57 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 198.66 E-value: 4.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 19 FMRTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDA 98
Cdd:PLN02330 47 FVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 99 EPRLVVVASAAREGVATIAQRHGAIVETLDADGSG--SLLDlARDEPADFVDASR-SADDLAAILYTSGTTGRSKGAMLT 175
Cdd:PLN02330 127 GAKLIVTNDTNYGKVKGLGLPVIVLGEEKIEGAVNwkELLE-AADRAGDTSDNEEiLQTDLCALPFSSGTTGISKGVMLT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLLSNALTlrDYWRVTSDD----RLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVS--LMPEATMLMGVP 249
Cdd:PLN02330 206 HRNLVANLCS--SLFSVGPEMigqvVTLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNalITQEVSFAPIVP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPRFGKEAAANIRL--FISGSAPLLAETHTEFEAR-TGHAILERYGMTETNMNT---SNPYDGKRIA--GTV 321
Cdd:PLN02330 284 PIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITlthGDPEKGHGIAkkNSV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 402 ISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLP 481
Cdd:PLN02330 444 KYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIP 523
|
490
....*....|....*
gi 1037244487 482 RNTMGKVQKNILRQQ 496
Cdd:PLN02330 524 KSLSGKIMRRLLKEK 538
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
52-494 |
2.08e-56 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 195.29 E-value: 2.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 52 GDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL--AELDYFIGDAePRLVVVASAAREGVATIAQRHGAIVETLDA 129
Cdd:cd05929 20 LDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVfaAAAAWKCGAC-PAYKSSRAPRAEACAIIEIKAAALVCGLFT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 130 DGSGSLLDLARDEPADFVDASRSADDLA--AILYTSGTTGRSKGAMLTHGNLLSNALTLRDyWRVTS----DDRLIHALP 203
Cdd:cd05929 99 GGGALDGLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMA-AALGFgpgaDSVYLSPAP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 204 IFHTHGlFVATNVTLLAGASMVLLSKFDADEVVSLMP--EATMLMGVPTFYVRLLQSPR--FGKEAAANIRLFISGSAPL 279
Cdd:cd05929 178 LYHAAP-FRWSMTALFMGGTLVLMEKFDPEEFLRLIEryRVTFAQFVPTMFVRLLKLPEavRNAYDLSSLKRVIHAAAPC 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 280 LAETHTEFEARTGHAILERYGMTETNMNTS-NPYDGKRIAGTVGLPLPDvRVRVTDpATGLVLPPEQTGMIEIKGPNVFK 358
Cdd:cd05929 257 PPWVKEQWIDWGGPIIWEYYGGTEGQGLTIiNGEEWLTHPGSVGRAVLG-KVHILD-EDGNEVPPGEIGEVYFANGPGFE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 359 gYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGE 438
Cdd:cd05929 335 -YTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQ 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 439 GVTAIVVRKPGAV---LDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:cd05929 414 RVHAVVQPAPGADagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
26-500 |
2.68e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 196.32 E-value: 2.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSygDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:PRK08162 44 RTWA--ETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ----ASAAREGVATIAQRHGAIVETLDADGSGSL----LD----LARDEPaDFvDASRSADDLAAIL--YTSGTTGRSKG 171
Cdd:PRK08162 122 dtefAEVAREALALLPGPKPLVIDVDDPEYPGGRfigaLDyeafLASGDP-DF-AWTLPADEWDAIAlnYTSGTTGNPKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 172 AMLTH-G---NLLSNALTlrdyWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGAsMVLLSKFDADEVVSLMPE--ATML 245
Cdd:PRK08162 200 VVYHHrGaylNALSNILA----WGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGT-NVCLRKVDPKLIFDLIREhgVTHY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 246 MGVPTFYVRLLQSPRFGKEAAAN-IRLFISGSAPllAETHTEFEARTGHAILERYGMTET----NMNTSNPydgkriaGT 320
Cdd:PRK08162 275 CGAPIVLSALINAPAEWRAGIDHpVHAMVAGAAP--PAAVIAKMEEIGFDLTHVYGLTETygpaTVCAWQP-------EW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 321 VGLPLPD---------VR------VRVTDPATGLVLPP--EQTGMIEIKGPNVFKGYWRMPEKTAAEFTGdGFFISGDLG 383
Cdd:PRK08162 346 DALPLDEraqlkarqgVRyplqegVTVLDPDTMQPVPAdgETIGEIMFRGNIVMKGYLKNPKATEEAFAG-GWFHTGDLA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 384 KIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQD 463
Cdd:PRK08162 425 VLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCRE 504
|
490 500 510
....*....|....*....|....*....|....*..
gi 1037244487 464 RLARYKQPKRIIFTEdLPRNTMGKVQKNILRQQYADL 500
Cdd:PRK08162 505 HLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQAKSL 540
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
25-488 |
3.66e-56 |
|
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: 202.78 E-value: 3.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATiaqrHGAIVETLDADGsgslldlARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:COG1020 579 TQSALAARLPE----LGVPVLALDALA-------LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLA 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPI---FHTHGLFVAtnvtLLAGASMVLLSK---FDADEVVSLMPE--ATMLMGVPTFYVRLL 256
Cdd:COG1020 648 WMQRRYGLGPGDRVLQFASLsfdASVWEIFGA----LLSGATLVLAPPearRDPAALAELLARhrVTVLNLTPSLLRALL 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSprfGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILE-RYGMTETNMNTS------NPYDGKRIagTVGLPLPDVR 329
Cdd:COG1020 724 DA---APEALPSLRLVLVGGEALPPELVRRWRARLPGARLVnLYGPTETTVDSTyyevtpPDADGGSV--PIGRPIANTR 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFI-------SGDLGKIDSDGYVHIVGRGKDLV- 401
Cdd:COG1020 799 VYVLDAH-LQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpgarlyrTGDLARWLPDGNLEFLGRADDQVk 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 402 ISgGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLP 481
Cdd:COG1020 878 IR-GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLP 956
|
....*..
gi 1037244487 482 RNTMGKV 488
Cdd:COG1020 957 LTGNGKL 963
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
22-497 |
6.19e-55 |
|
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: 192.88 E-value: 6.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDyfigDAEPR 101
Cdd:cd05906 34 DGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPN----ARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 L----------VVVASAAR-EGVATIAQRHGAIVETLDAdgsgslLDLARDEPADFVDASRSADDLAAILYTSGTTGRSK 170
Cdd:cd05906 110 LrhiwqllgspVVLTDAELvAEFAGLETLSGLPGIRVLS------IEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 171 GAMLTHGNLLSNAL-TLRDYwRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMV----------------LLSKFDAD 233
Cdd:cd05906 184 AVPLTHRNILARSAgKIQHN-GLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVhvpteeiladplrwldLIDRYRVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 234 evVSLMPEatmlmgvpTFYVRLLQSPRFGKEAAAN---IRLFISGSAPLLAET-------HTEFEARTgHAILERYGMTE 303
Cdd:cd05906 263 --ITWAPN--------FAFALLNDLLEEIEDGTWDlssLRYLVNAGEAVVAKTirrllrlLEPYGLPP-DAIRPAFGMTE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 304 T----NMNTSNPYDGKRIAGT---VGLPLPDVRVRVTDPaTGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF 376
Cdd:cd05906 332 TcsgvIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDD-EGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 377 FISGDLGKIDsDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPhpdfgegvtaivVRKPGAVLDEKT 456
Cdd:cd05906 411 FRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFA------------VRDPGAETEELA 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 457 IV----GALQDRLARYKQ-------------PKRII--FTEDLPRNTMGKVQKNILRQQY 497
Cdd:cd05906 478 IFfvpeYDLQDALSETLRairsvvsrevgvsPAYLIplPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
25-494 |
3.00e-54 |
|
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: 188.73 E-value: 3.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVv 104
Cdd:cd17649 10 DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvatIAQrHGaivetldadgsgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17649 89 -----------LTH-HP--------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPI----FHtHGLFVAtnvtLLAGASMVLLSK---FDADEVVSLMPEATM-LMGVPTFYVR-- 254
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFnfdgAH-EQLLPP----LICGACVVLRPDelwASADELAEMVRELGVtVLDLPPAYLQql 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 LLQSPRFGKEAAANIRLFISGSAPLLAETHTefEARTGHAIL-ERYGMTETNMnTSNPYDGKRIAGT------VGLPLPD 327
Cdd:cd17649 200 AEEADRTGDGRPPSLRLYIFGGEALSPELLR--RWLKAPVRLfNAYGPTEATV-TPLVWKCEAGAARagasmpIGRPLGG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 328 VRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFI-------SGDLGKIDSDGYVHIVGRGKDL 400
Cdd:cd17649 277 RSAYILDADLNPV-PVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGApgsrlyrTGDLARWRDDGVIEYLGRVDHQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAV-LDEKTIVGALQDRLARYKQPKRIIFTED 479
Cdd:cd17649 356 VKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpELRAQLRTALRASLPDYMVPAHLVFLAR 435
|
490
....*....|....*
gi 1037244487 480 LPRNTMGKVQKNILR 494
Cdd:cd17649 436 LPLTPNGKLDRKALP 450
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
24-494 |
3.12e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 190.22 E-value: 3.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRlV 103
Cdd:PRK13390 21 TGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGAR-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAqrhGAIVETLDADGsGSLLDLARDEPADFVDASRSADDL--AAILYTSGTTGRSKGamlTHGNLLS 181
Cdd:PRK13390 100 LVASAALDGLAAKV---GADLPLRLSFG-GEIDGFGSFEAALAGAGPRLTEQPcgAVMLYSSGTTGFPKG---IQPDLPG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NAL---------TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGaSMVLLSKFDADEVVSLMPE--ATMLMGVPT 250
Cdd:PRK13390 173 RDVdapgdpivaIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGG-TVVLAKRFDAQATLGHVERyrITVTQMVPT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQ--SPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN-MNTSNPYDGKRIAGTVGLP-LP 326
Cdd:PRK13390 252 MFVRLLKldADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHgMTFIDSPDWLAHPGSVGRSvLG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 327 DVRVRVTDpatGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTA-AEFTGDGFFIS-GDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:PRK13390 332 DLHICDDD---GNELPAGRIGTVYFERDRLPFRYLNDPEKTAaAQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFTEDLP 481
Cdd:PRK13390 409 GVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDelaRELIDYTRSRIAHYKAPRSVEFVDELP 488
|
490
....*....|...
gi 1037244487 482 RNTMGKVQKNILR 494
Cdd:PRK13390 489 RTPTGKLVKGLLR 501
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
28-494 |
2.93e-53 |
|
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: 185.78 E-value: 2.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 WSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAS 107
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 aaregvatiaqrhgaivetldadgsgSLLDlardepadfvdaSRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLR 187
Cdd:cd05969 81 --------------------------ELYE------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 188 DYWRVTSDDRLIH-ALPIFHThGLFVATNVTLLAGASMVLL-SKFDADEVVSLMPE--ATMLMGVPTfYVRLLQspRFGK 263
Cdd:cd05969 123 YVLDLHPDDIYWCtADPGWVT-GTVYGIWAPWLNGVTNVVYeGRFDAESWYGIIERvkVTVWYTAPT-AIRMLM--KEGD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 264 EAAA-----NIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRI-AGTVGLPLPDVRVRVTDpAT 337
Cdd:cd05969 199 ELARkydlsSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIkPGSMGKPLPGVKAAVVD-EN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 338 GLVLPPEQTGMIEIKG--PNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVES 415
Cdd:cd05969 278 GNELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEK---TIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNI 492
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
..
gi 1037244487 493 LR 494
Cdd:cd05969 437 LK 438
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
161-488 |
1.69e-52 |
|
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: 180.29 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 161 YTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVtLLAGASMVLLSKFDADEVVSLMP 240
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKSWIRKIN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 241 E--ATMLMGVPTfyvrLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETNMNTSNPYDGKRI 317
Cdd:cd17633 86 QynATVIYLVPT----MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFYGTSELSFITYNFNQESRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 318 AGTVGLPLPDVRVRVTDPATGLVlppeqtGMIEIKGPNVFKGYWRmpektAAEFTGDGFFISGDLGKIDSDGYVHIVGRG 397
Cdd:cd17633 162 PNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 398 KDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkpGAVLDEKTIVGALQDRLARYKQPKRIIFT 477
Cdd:cd17633 231 SDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFV 307
|
330
....*....|.
gi 1037244487 478 EDLPRNTMGKV 488
Cdd:cd17633 308 DSLPYTSSGKI 318
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
29-496 |
3.92e-52 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 183.83 E-value: 3.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPgDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVvasA 108
Cdd:PRK07638 28 TYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIV---T 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQRHGAIVETldaDGSGSLLDLARDEPADFVDASRSADDLAailYTSGTTGRSKGAMLTHGNLLSNALTLRD 188
Cdd:PRK07638 104 ERYKLNDLPDEEGRVIEI---DEWKRMIEKYLPTYAPIENVQNAPFYMG---FTSGSTGKPKAFLRAQQSWLHSFDCNVH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 189 YWRVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVLLSKFDADEVVSLMPEA--TMLMGVPTFYVRLLQSPRFgkeaA 266
Cdd:PRK07638 178 DFHMKREDSVLIAGTLVHSLFLYGAIS-TLYVGQTVHLMRKFIPNQVLDKLETEniSVMYTVPTMLESLYKENRV----I 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 ANIRLFISGSAPLLAETHTEFEARTGHAIL-ERYGMTETNMNTS-NPYDGKRIAGTVGLPLPDVRVRVTDPAtGLVLPPE 344
Cdd:PRK07638 253 ENKMKIISSGAKWEAEAKEKIKNIFPYAKLyEFYGASELSFVTAlVDEESERRPNSVGRPFHNVQVRICNEA-GEEVQKG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 345 QTGMIEIKGPNVFKGYwRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVV 424
Cdd:PRK07638 332 EIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVD 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1037244487 425 ESAVIGVPHPDFGEGVTAIVvrKPGAvlDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK07638 411 EIVVIGVPDSYWGEKPVAII--KGSA--TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
24-488 |
4.71e-52 |
|
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: 183.63 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQrhgAIVETLDADGSgslldlardePADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd12114 89 LTDGPDAQLDVAVFD---VLILDLDALAA----------PAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRVTSDDRLIhALPIFH----THGLFVAtnvtLLAGASMVLLS---KFDADEVVSLMPE------------ATM 244
Cdd:cd12114 156 LDINRRFAVGPDDRVL-ALSSLSfdlsVYDIFGA----LSAGATLVLPDearRRDPAHWAELIERhgvtlwnsvpalLEM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 245 LMGVPTFYVRLLQSPRF----G-----------KEAAANIRLFISGSApllaethTEfeaRTGHAILerYGMTETNMN-T 308
Cdd:cd12114 231 LLDVLEAAQALLPSLRLvllsGdwipldlparlRALAPDARLISLGGA-------TE---ASIWSIY--HPIDEVPPDwR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 309 SNPYdgkriagtvGLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEF----TGDGFFISGDLGK 384
Cdd:cd12114 299 SIPY---------GRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFvthpDGERLYRTGDLGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 385 IDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDR 464
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQT 448
|
490 500
....*....|....*....|....
gi 1037244487 465 LARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:cd12114 449 LPAYMIPSRVIALEALPLTANGKV 472
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
40-496 |
6.68e-51 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 182.31 E-value: 6.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 40 IAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVvasaAREGVATIAQR 119
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV----TDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 120 HGA----------IVETLDADGSGSLLDLARDEP-------ADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSN 182
Cdd:PLN02860 121 LQNdrlpslmwqvFLESPSSSVFIFLNSFLTTEMlkqralgTTELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 183 ALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVtLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPR 260
Cdd:PLN02860 201 SLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAM-LMVGACHVLLPKFDAKAALQAIKQhnVTSMITVPAMMADLISLTR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAAN--IRLFISG----SAPLLAETHTEFEARtghAILERYGMTET----------------------NMNTSNPY 312
Cdd:PLN02860 280 KSMTWKVFpsVRKILNGggslSSRLLPDAKKLFPNA---KLFSAYGMTEAcssltfmtlhdptlespkqtlqTVNQTKSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 313 DGKRIAGT-VGLPLPDVRVRVTDPAtglvlpPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYV 391
Cdd:PLN02860 357 SVHQPQGVcVGKPAPHVELKIGLDE------SSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 392 HIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIV--------------VRKPGAVLDEKTi 457
Cdd:PLN02860 431 WLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwsdnekeNAKKNLTLSSET- 509
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1037244487 458 vgaLQD-----RLARYKQPKRIIFTED-LPRNTMGKVQKNILRQQ 496
Cdd:PLN02860 510 ---LRHhcrekNLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRRE 551
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
40-495 |
1.03e-50 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 181.11 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 40 IAGALDTLGIRPGDRVAVQVEKS---AEALIlylACLRSGAVYLPLNTAYT---LAE------LDYFIGDAE-----PRL 102
Cdd:PRK13382 81 LAAALQALPIGEPRVVGIMCRNHrgfVEALL---AANRIGADILLLNTSFAgpaLAEvvtregVDTVIYDEEfsatvDRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAREGVATIAQRHGAIVETLDADGSGslldlARDEPADfvdasRSADdlaAILYTSGTTGRSKGAMLTH--GNLL 180
Cdd:PRK13382 158 LADCPQATRIVAWTDEDHDLTVEVLIAAHAG-----QRPEPTG-----RKGR---VILLTSGTTGTPKGARRSGpgGIGT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 181 SNALTLRDYWRvtSDDRLIHALPIFHTHGlFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQS 258
Cdd:PRK13382 225 LKAILDRTPWR--AEEPTVIVAPMFHAWG-FSQLVLAASLACTIVTRRRFDPEATLDLIDRhrATGLAVVPVMFDRIMDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PR--FGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNM-NTSNPYDGKRIAGTVGLPLPDVRVRVTDP 335
Cdd:PRK13382 302 PAevRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRILDQ 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 aTGLVLPPEQTGMIEIKGPNVFKGYwrMPEKTAAefTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVES 415
Cdd:PRK13382 382 -DFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 416 EIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK13382 457 TLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQA 536
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
162-495 |
2.81e-50 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 178.26 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 162 TSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSddrlIHA---LPIFHTHGLFVATNvTLLAGASMVLL--SKFDADEVV 236
Cdd:PRK07445 128 TGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQ----VNSfcvLPLYHVSGLMQFMR-SFLTGGKLVILpyKRLKSGQEL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 237 SLMPEATMLMGVPTFYVRLLQSPrfgKEAAANIRLFISGSAP----LLAEthtefeARTGHAILE-RYGMTET--NMNTS 309
Cdd:PRK07445 203 PPNPSDFFLSLVPTQLQRLLQLR---PQWLAQFRTILLGGAPawpsLLEQ------ARQLQLRLApTYGMTETasQIATL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 310 NPYD---GKRiagTVGLPLPDVRVRVTDPATGLvlppeqtgmIEIKGPNVFKGYWrmPEKTAAeftgDGFFISGDLGKID 386
Cdd:PRK07445 274 KPDDflaGNN---SSGQVLPHAQITIPANQTGN---------ITIQAQSLALGYY--PQILDS----QGIFETDDLGYLD 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 387 SDGYVHIVGRGKDLVISGGYNIYPKEVESEIdRIEGVVES-AVIGVPHPDFGEGVTAIVVRKPGAVlDEKTIVGALQDRL 465
Cdd:PRK07445 336 AQGYLHILGRNSQKIITGGENVYPAEVEAAI-LATGLVQDvCVLGLPDPHWGEVVTAIYVPKDPSI-SLEELKTAIKDQL 413
|
330 340 350
....*....|....*....|....*....|
gi 1037244487 466 ARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PRK07445 414 SPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
25-496 |
5.50e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 179.11 E-value: 5.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDR-VAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:PRK07867 26 DSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREgvatIAQRHGAIVETLDADGSG--SLLDLARDEPADFVDASrsADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:PRK07867 106 LTESAHAE----LLDGLDPGVRVINVDSPAwaDELAAHRDAEPPFRVAD--PDDLFMLIFTSGTSGDPKAVRCTHRKVAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADevvSLMPE-----ATML--MGVPTFYVr 254
Cdd:PRK07867 180 AGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSAS---GFLPDvrrygATYAnyVGKPLSYV- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 lLQSPRFGKEAAANIRLFI--SGSAPLLAethtEFEARTGHAILERYGMTETNMNTSNPYDGKriAGTVGLPLPDVRVRv 332
Cdd:PRK07867 256 -LATPERPDDADNPLRIVYgnEGAPGDIA----RFARRFGCVVVDGFGSTEGGVAITRTPDTP--PGALGPLPPGVAIV- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 333 tDPATGLVLPP------------EQTG-MIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKD 399
Cdd:PRK07867 328 -DPDTGTECPPaedadgrllnadEAIGeLVNTAGPGGFEGYYNDPEADAERMR-GGVYWSGDLAYRDADGYAYFAGRLGD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 400 LVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGAL--QDRLARYKQPKRIIFT 477
Cdd:PRK07867 406 WMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVC 485
|
490
....*....|....*....
gi 1037244487 478 EDLPRNTMGKVQKNILRQQ 496
Cdd:PRK07867 486 AELPRTATFKVLKRQLSAE 504
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
25-493 |
2.01e-49 |
|
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: 175.96 E-value: 2.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17643 10 DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17643 90 T----------------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIhalpIFHTHG-------LFVAtnvtLLAGASMVLLSKFdadevVSLMPEA----------TMLMG 247
Cdd:cd17643 124 ATQRWFGFNEDDVWT----LFHSYAfdfsvweIWGA----LLHGGRLVVVPYE-----VARSPEDfarllrdegvTVLNQ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 248 VPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA---ILERYGMTETNMNTS----NPYDGKRIAG- 319
Cdd:cd17643 191 TPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDrpqLVNMYGITETTVHVTfrplDAADLPAAAAs 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 320 TVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVH 392
Cdd:cd17643 271 PIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 393 IVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIgvPHpDFGEGVTAIV---VRKPGAVLDEKTIVGALQDRLARYK 469
Cdd:cd17643 350 YLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVI--VR-EDEPGDTRLVayvVADDGAAADIAELRALLKELLPDYM 426
|
490 500
....*....|....*....|....
gi 1037244487 470 QPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd17643 427 VPARYVPLDALPLTVNGKLDRAAL 450
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
26-500 |
3.65e-49 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 177.10 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVylPLNTAYT--LAELDYFIGDAEPRLV 103
Cdd:PRK10946 47 RQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFShqRSELNAYASQIEPALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVAS-----AAREGVATIAQRHGA--IVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTH 176
Cdd:PRK10946 125 IADRqhalfSDDDFLNTLVAEHSSlrVVLLLNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 177 GnllsnaltlrDYW----------RVTSDDRLIHALPIFHTHGLFV--ATNVtLLAGASMVLLSKFDAD----------- 233
Cdd:PRK10946 205 N----------DYYysvrrsveicGFTPQTRYLCALPAAHNYPMSSpgALGV-FLAGGTVVLAPDPSATlcfpliekhqv 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 234 EVVSLMPEATMLmgvptfYVRLLQSPRfGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN-TSNPY 312
Cdd:PRK10946 274 NVTALVPPAVSL------WLQAIAEGG-SRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNyTRLDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 313 DGKRIAGTVGLPL-PDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYV 391
Cdd:PRK10946 347 SDERIFTTQGRPMsPDDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYI 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 392 HIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTA-IVVRKPgavldektiVGALQDR------ 464
Cdd:PRK10946 426 TVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAfLVVKEP---------LKAVQLRrflreq 496
|
490 500 510
....*....|....*....|....*....|....*..
gi 1037244487 465 -LARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYADL 500
Cdd:PRK10946 497 gIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASR 533
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
29-499 |
8.18e-49 |
|
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: 176.25 E-value: 8.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIR--PGDRVAVQVEKSAEALILYLACLRSGAVYLPLntaY-TLAE--LDYFIGDAEPRLV 103
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPL---YdTLGPeaIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVAsaarEGVATIaqrhgaiveTLDAdgsgsLLDLARDEPADFVDASRsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd05927 84 FCD----AGVKVY---------SLEE-----FEKLGKKNKVPPPPPKP--EDLATICYTSGTTGNPKGVMLTHGNIVSNV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 ----LTLRDYWRVTSDDRLIHALPIFHthgLF--VATNVTLLAGAS--------MVLLskfdaDEVVSLMPeaTMLMGVP 249
Cdd:cd05927 144 agvfKILEILNKINPTDVYISYLPLAH---IFerVVEALFLYHGAKigfysgdiRLLL-----DDIKALKP--TVFPGVP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLL---------QSPR-------------------------------FGKEAAA---NIRLFISGSAPLLAETHTE 286
Cdd:cd05927 214 RVLNRIYdkifnkvqaKGPLkrklfnfalnyklaelrsgvvraspfwdklvFNKIKQAlggNVRLMLTGSAPLSPEVLEF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 287 FEARTGHAILERYGMTETNMNT--SNPYDgkRIAGTVGLPLPDVRVRVTD-PATG-LVLPPEQTGMIEIKGPNVFKGYWR 362
Cdd:cd05927 294 LRVALGCPVLEGYGQTECTAGAtlTLPGD--TSVGHVGGPLPCAEVKLVDvPEMNyDAKDPNPRGEVCIRGPNVFSGYYK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 363 MPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV-ISGGYNIYPKEVESEIDRIEGVV---------ESAVIGVP 432
Cdd:cd05927 372 DPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVAPEKIENIYARSPFVAqifvygdslKSFLVAIV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 433 HPDF------------GEGVTAIVVRKP---GAVLDEKTIVGAlQDRLARYKQPKRII-----FTE--DLPRNTMgKVQK 490
Cdd:cd05927 452 VPDPdvlkewaaskggGTGSFEELCKNPevkKAILEDLVRLGK-ENGLKGFEQVKAIHlepepFSVenGLLTPTF-KLKR 529
|
....*....
gi 1037244487 491 NILRQQYAD 499
Cdd:cd05927 530 PQLKKYYKK 538
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
25-493 |
1.14e-47 |
|
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: 171.61 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VAsaarEGVATIAQRHGAIVETLDADgsgslldlaRDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd12117 100 TD----RSLAGRAGGLEVAVVIDEAL---------DAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TlRDYWRVTSDDRLIHALPI-FH--THGLFVAtnvtLLAGASMVLLSK---FDADEVVSLMPE---ATMLMGVPTFYVRL 255
Cdd:cd12117 167 N-TNYVTLGPDDRVLQTSPLaFDasTFEIWGA----LLNGARLVLAPKgtlLDPDALGALIAEegvTVLWLTAALFNQLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 256 LQSPrfgkEAAANIR-LFISGSAPLLAETHTEFEARTGHAILERYGMTE-TNMNTSNPYDGKRIAGT---VGLPLPDVRV 330
Cdd:cd12117 242 DEDP----ECFAGLReLLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTEnTTFTTSHVVTELDEVAGsipIGRPIANTRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 331 RVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:cd12117 318 YVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLPDGRLEFLGRIDDQVKIR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNT 484
Cdd:cd12117 397 GFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTA 474
|
....*....
gi 1037244487 485 MGKVQKNIL 493
Cdd:cd12117 475 NGKVDRRAL 483
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
23-434 |
1.24e-47 |
|
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: 172.27 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVV---------ASAAREGVATIAQrhgAIVETLDADGSGSLLdLARDEPADfVDASRSADDLAAILYTSGTTGRSKGAM 173
Cdd:cd05932 82 LFVgklddwkamAPGVPEGLISISL---PPPSAANCQYQWDDL-IAQHPPLE-ERPTRFPEQLATLIYTSGTTGQPKGVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 174 LTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHT-------HGLFVATNVTLLAGAsmvlLSKFDADevvSLMPEATMLM 246
Cdd:cd05932 157 LTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVtervfveGGSLYGGVLVAFAES----LDTFVED---VQRARPTLFF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 247 GVPTFYV----------------RLLQSPRFG-----KEAAA----NIRLFISGSAPlLAETHTEFEARTGHAILERYGM 301
Cdd:cd05932 230 SVPRLWTkfqqgvqdkipqqklnLLLKIPVVNslvkrKVLKGlgldQCRLAGCGSAP-VPPALLEWYRSLGLNILEAYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 302 TETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpatglvlppeqTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGD 381
Cdd:cd05932 309 TENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGD 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 382 LGKIDSDGYVHIVGRGKDLV-ISGGYNIYPKEVESEI---DRIEGVVesaVIG--VPHP 434
Cdd:cd05932 378 KGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLaehDRVEMVC---VIGsgLPAP 433
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-493 |
4.48e-47 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 176.12 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVv 104
Cdd:PRK12467 535 EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLL- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvatIAQRHGAIVETLDADGSGSLLDLARDE----PADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLL 180
Cdd:PRK12467 614 -----------LTQSHLLAQLPVPAGLRSLCLDEPADLlcgySGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALA 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 181 SNALTLRDYWRVTSDDRLIH----ALPIFHTHgLFVAtnvtLLAGASMVLLSK---FDADEVVSLMPE--ATMLMGVPTF 251
Cdd:PRK12467 683 NYVCVIAERLQLAADDSMLMvstfAFDLGVTE-LFGA----LASGATLHLLPPdcaRDAEAFAALMADqgVTVLKIVPSH 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 252 YVRLLQSPRfGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTS--NPYDGKRIAGTV--GLPLPD 327
Cdd:PRK12467 758 LQALLQASR-VALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVStyELSDEERDFGNVpiGQPLAN 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 328 VRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:PRK12467 837 LGLYILDHYLNPV-PVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYRADGVIEYLGRMDHQ 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHpDFGEGVTAIVVRKPGAVLDEKTIVG-----ALQDRLARYKQPKRII 475
Cdd:PRK12467 916 VKIRGFRIELGEIEARLLAQPGVREAVVLAQPG-DAGLQLVAYLVPAAVADGAEHQATRdelkaQLRQVLPDYMVPAHLL 994
|
490
....*....|....*...
gi 1037244487 476 FTEDLPRNTMGKVQKNIL 493
Cdd:PRK12467 995 LLDSLPLTPNGKLDRKAL 1012
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
29-493 |
7.20e-47 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 170.96 E-value: 7.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:PRK05857 43 RYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQRHG---AIVETLDADGSGSLLDLARDEPADFVDASrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:PRK05857 123 SKMASSAVPEALHsipVIAVDIAAVTRESEHSLDAASLAGNADQG--SEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRD---YWRVTSDDRLIHA-LPIFHTHGLFVATNvTLLAGASMV--------LLSKFDADEVvslmpeATMLMgVPTFYV 253
Cdd:PRK05857 201 LQKeglNWVTWVVGETTYSpLPATHIGGLWWILT-CLMHGGLCVtggenttsLLEILTTNAV------ATTCL-VPTLLS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 254 RLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEArTGHAILERYGMTETN-----MNTSNPYDGKRIAGTVGLPLPDV 328
Cdd:PRK05857 273 KLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEA-TGVRTAQVYGLSETGctalcLPTDDGSIVKIEAGAVGRPYPGV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 329 RVRVT-----DPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVIS 403
Cdd:PRK05857 352 DVYLAatdgiGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTA-EVLIDGWVNTGDLLERREDGFFYIKGRSSEMIIC 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 404 GGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYK-------QPKRIIF 476
Cdd:PRK05857 431 GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV--ASAELDESAARALKHTIAARFRresepmaRPSTIVI 508
|
490
....*....|....*..
gi 1037244487 477 TEDLPRNTMGKVQKNIL 493
Cdd:PRK05857 509 VTDIPRTQSGKVMRASL 525
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
24-401 |
1.69e-46 |
|
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: 168.93 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 24 SGQTW-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGavyLPLNTAY-TLAEldyfigdaepr 101
Cdd:cd17639 1 GEYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYaTLGE----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 lvvvasaarEGVATiaqrhgAIVETldadGSGSLLdlardepadfvdASRSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:cd17639 67 ---------DALIH------SLNET----ECSAIF------------TDGKPDDLACIMYTSGSTGNPKGVMLTHGNLVA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 --NALTLRDYWRVTSDDRLIHALPIFHTHGlFVATNVTLLAGASM------VLLSKFDAD---EVVSLMPeaTMLMGVP- 249
Cdd:cd17639 116 giAGLGDRVPELLGPDDRYLAYLPLAHIFE-LAAENVCLYRGGTIgygsprTLTDKSKRGckgDLTEFKP--TLMVGVPa 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 -------------------------TFYVRLLQSPRFGKEAAA---------------NIRLFISGSAPLLAETHtEFEA 289
Cdd:cd17639 193 iwdtirkgvlaklnpmgglkrtlfwTAYQSKLKALKEGPGTPLldelvfkkvraalggRLRYMLSGGAPLSADTQ-EFLN 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 290 RTGHAILERYGMTET--NMNTSNPYDGKriAGTVGLPLPDVRVRVTDPATGLVLP--PEQTGMIEIKGPNVFKGYWRMPE 365
Cdd:cd17639 272 IVLCPVIQGYGLTETcaGGTVQDPGDLE--TGRVGPPLPCCEIKLVDWEEGGYSTdkPPPRGEILIRGPNVFKGYYKNPE 349
|
410 420 430
....*....|....*....|....*....|....*.
gi 1037244487 366 KTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:cd17639 350 KTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLV 385
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
39-496 |
4.01e-46 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 171.37 E-value: 4.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAAREGVATiaq 118
Cdd:PRK06060 42 RLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQP--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 119 rhGAIVETLDAdgsgsLLDLARDEPADFvdASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL-RDYWRVTSDDR 197
Cdd:PRK06060 119 --SRVAEAAEL-----MSEAARVAPGGY--EPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKALRLTPEDT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 198 LIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMP---EATMLMGVPTFYVRLLQSprFGKEAAANIRLFIS 274
Cdd:PRK06060 190 GLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSarfGPSVLYGVPNFFARVIDS--CSPDSFRSLRCVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 275 -GSA--PLLAETHTEFEArtGHAILERYGMTETNMN-TSNPYDGKRIaGTVGLPLPDVRVRVTDPaTGLVLPPEQTGMIE 350
Cdd:PRK06060 268 aGEAleLGLAERLMEFFG--GIPILDGIGSTEVGQTfVSNRVDEWRL-GTLGRVLPPYEIRVVAP-DGTTAGPGVEGDLW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 351 IKGPNVFKGYWRMPEKTaaeFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIG 430
Cdd:PRK06060 344 VRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 431 VPHPDFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK06060 421 VRESTGASTLQAFLVATSGATIDGsvmRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
26-488 |
3.00e-45 |
|
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: 167.37 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAA-REG--------VATIAQRHGAIVETL----------DADGSGSLL--DLARDEPADFVDASRSADDLAAILYTSG 164
Cdd:cd17634 163 ADGGvRAGrsvplkknVDDALNPNVTSVEHVivlkrtgsdiDWQEGRDLWwrDLIAKASPEHQPEAMNAEDPLFILYTSG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 165 TTGRSKGAMLTHGN-LLSNALTLR--------DYWRVTSDDRLIhalpIFHTHGLFVAtnvtLLAGASMVLLSKF----D 231
Cdd:cd17634 243 TTGKPKGVLHTTGGyLVYAATTMKyvfdygpgDIYWCTADVGWV----TGHSYLLYGP----LACGATTLLYEGVpnwpT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 232 ADEVVSLMPE--ATMLMGVPTfYVRLLQSPrfGKEAAA-----NIRLFISGSAPLLAETH---TEFEARTGHAILERYGM 301
Cdd:cd17634 315 PARMWQVVDKhgVNILYTAPT-AIRALMAA--GDDAIEgtdrsSLRILGSVGEPINPEAYewyWKKIGKEKCPVVDTWWQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 302 TETNMNTSNPYDGKR--IAGTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKG--PNVFKGYWRMPEKTAAEF--TGDG 375
Cdd:cd17634 392 TETGGFMITPLPGAIelKAGSATRPVFGVQPAVVD-NEGHPQPGGTEGNLVITDpwPGQTRTLFGDHERFEQTYfsTFKG 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 376 FFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGaVLDEK 455
Cdd:cd17634 471 MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHG-VEPSP 549
|
490 500 510
....*....|....*....|....*....|....*..
gi 1037244487 456 TIVGALQDRLAR----YKQPKRIIFTEDLPRNTMGKV 488
Cdd:cd17634 550 ELYAELRNWVRKeigpLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
28-499 |
9.43e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 164.88 E-value: 9.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 WSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAS 107
Cdd:PRK07008 40 YTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 AAREGVATIAQRHGAI---VETLDAD----GSGSLL---DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHG 177
Cdd:PRK07008 120 TFLPLVDALAPQCPNVkgwVAMTDAAhlpaGSTPLLcyeTLVGAQDGDYDWPRFDENQASSLCYTSGTTGNPKGALYSHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 178 N--LLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLlAGASMVLLSK-FDADEVVSLMPE--ATMLMGVPTFY 252
Cdd:PRK07008 200 StvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPGPdLDGKSLYELIEAerVTFSAGVPTVW 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 253 VRLLQSPRFGKEAAANI-RLFISGSA--PLLAEThteFEARTGHAILERYGMTE----------TNMNTSNPYDGKR-IA 318
Cdd:PRK07008 279 LGLLNHMREAGLRFSTLrRTVIGGSAcpPAMIRT---FEDEYGVEVIHAWGMTEmsplgtlcklKWKHSQLPLDEQRkLL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDPAtGLVLPPE--QTGMIEIKGPNVFKGYWRMPEKTAAeftgDGFFISGDLGKIDSDGYVHIVGR 396
Cdd:PRK07008 356 EKQGRVIYGVDMKIVGDD-GRELPWDgkAFGDLQVRGPWVIDRYFRGDASPLV----DGWFPTGDVATIDADGFMQITDR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 397 GKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIF 476
Cdd:PRK07008 431 SKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVF 510
|
490 500
....*....|....*....|...
gi 1037244487 477 TEDLPRNTMGKVQKNILRQQYAD 499
Cdd:PRK07008 511 VDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
25-471 |
1.36e-44 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 165.43 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK08279 60 DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQ---RHGAI-----VETLDADGSGSLLDLARDEPADFVDASRS--ADDLAAILYTSGTTGRSKGAML 174
Cdd:PRK08279 140 VGEELVEAFEEARAdlaRPPRLwvaggDTLDDPEGYEDLAAAAAGAPTTNPASRSGvtAKDTAFYIYTSGTTGLPKAAVM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 175 THGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDA----DEVVSLmpEATMLMgvpt 250
Cdd:PRK08279 220 SHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSAsrfwDDVRRY--RATAFQ---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 fYV----R-LLQSPRFGKEAAANIRLFIsgSAPLLAETHTEFEARTG-HAILERYGMTETNMNTSNpYDGKRiaGTVG-L 323
Cdd:PRK08279 294 -YIgelcRyLLNQPPKPTDRDHRLRLMI--GNGLRPDIWDEFQQRFGiPRILEFYAASEGNVGFIN-VFNFD--GTVGrV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 324 PLPDVR----VRVtDPATGLVL----------PPEQTG----MIEIKGPnvFKGYwRMPEKTAAE-----FT-GDGFFIS 379
Cdd:PRK08279 368 PLWLAHpyaiVKY-DVDTGEPVrdadgrcikvKPGEVGlligRITDRGP--FDGY-TDPEASEKKilrdvFKkGDAWFNT 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 380 GDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFG--EGVTAIVVRkPGAVLDEKTI 457
Cdd:PRK08279 444 GDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDgrAGMAAIVLA-DGAEFDLAAL 522
|
490
....*....|....
gi 1037244487 458 VGALQDRLARYKQP 471
Cdd:PRK08279 523 AAHLYERLPAYAVP 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-504 |
6.67e-44 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 167.06 E-value: 6.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLL 4653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQrhgaiVETLDADGSGSLLDLARDEPADFVDasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK12316 4654 TQSHLLQRLPIPDG-----LASLALDRDEDWEGFPAHDPAVRLH----PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLH 4724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIH----ALPIFHtHGLFVAtnvtLLAGASMVLL--SKFDADEVVSLMPEA--TMLMGVPTFYVRLL 256
Cdd:PRK12316 4725 ATGERYELTPDDRVLQfmsfSFDGSH-EGLYHP----LINGASVVIRddSLWDPERLYAEIHEHrvTVLVFPPVYLQQLA 4799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN----TSNPYDGK-RIAGTVGLPLPDVRVR 331
Cdd:PRK12316 4800 EHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTvllwKARDGDACgAAYMPIGTPLGNRSGY 4879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 332 VTDPATGLvLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:PRK12316 4880 VLDGQLNP-LPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQVKIR 4958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPdFGEGVTAIVVRKPGAVLDEKTIVGALQDRLAR--------YKQPKRIIF 476
Cdd:PRK12316 4959 GFRIELGEIEARLREHPAVREAVVIAQEGA-VGKQLVGYVVPQDPALADADEAQAELRDELKAalrerlpeYMVPAHLVF 5037
|
490 500
....*....|....*....|....*...
gi 1037244487 477 TEDLPRNTMGKVQKNILRQQYADLYTRT 504
Cdd:PRK12316 5038 LARMPLTPNGKLDRKALPQPDASLLQQA 5065
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
23-496 |
9.49e-44 |
|
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: 162.28 E-value: 9.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:cd05970 43 GEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVAS---------AAREGVATIAQRhgAIVETLDADGSGSLLDLARDEPADF----VDASRSADDLAAILYTSGTTGRS 169
Cdd:cd05970 123 IVAIAednipeeieKAAPECPSKPKL--VWVGDPVPEGWIDFRKLIKNASPDFerptANSYPCGEDILLVYFSSGTTGMP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 170 KgaMLTHGNL--LSNALTLRdYWRVTSDDRLiHaLPIFHThGLFVATNVTL----LAGASMVL--LSKFDADEVVSLMPE 241
Cdd:cd05970 201 K--MVEHDFTypLGHIVTAK-YWQNVREGGL-H-LTVADT-GWGKAVWGKIygqwIAGAAVFVydYDKFDPKALLEKLSK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 --ATMLMGVPTFYvRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAG 319
Cdd:cd05970 275 ygVTTFCAPPTIY-RFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATFPWMEPKPG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 320 TVGLPLPDVRVRVTDPaTGLVLPPEQTGMIEI---KGPNV--FKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIV 394
Cdd:cd05970 354 SMGKPAPGYEIDLIDR-EGRSCEAGEEGEIVIrtsKGKPVglFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYLWFV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 395 GRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVV----RKPGAVLdEKTIVGALQDRLARYKQ 470
Cdd:cd05970 432 GRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVlakgYEPSEEL-KKELQDHVKKVTAPYKY 510
|
490 500
....*....|....*....|....*.
gi 1037244487 471 PKRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:cd05970 511 PRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
29-499 |
1.18e-43 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 161.84 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATIAQR----HGAIVETLDA-------DGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTH- 176
Cdd:PRK06018 121 FVPILEKIADKlpsvERYVVLTDAAhmpqttlKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHr 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 177 GNLLSNALTL-RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLaGASMVLL-SKFDADEVVSLM--PEATMLMGVPTFY 252
Cdd:PRK06018 201 SNVLHALMANnGDALGTSAADTMLPVVPLFHANSWGIAFSAPSM-GTKLVMPgAKLDGASVYELLdtEKVTFTAGVPTVW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 253 VRLLQSPRFGKEAAANIRLFISGSAPL---LAETHTEFEARTGHAilerYGMTETN-MNT---------SNPYDGK-RIA 318
Cdd:PRK06018 280 LMLLQYMEKEGLKLPHLKMVVCGGSAMprsMIKAFEDMGVEVRHA----WGMTEMSpLGTlaalkppfsKLPGDARlDVL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDPAtGLVLPPE--QTGMIEIKGPNVFKGYWRMPEKTaaeFTGDGFFISGDLGKIDSDGYVHIVGR 396
Cdd:PRK06018 356 QKQGYPPFGVEMKITDDA-GKELPWDgkTFGRLKVRGPAVAAAYYRVDGEI---LDDDGFFDTGDVATIDAYGYMRITDR 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 397 GKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIF 476
Cdd:PRK06018 432 SKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAF 511
|
490 500
....*....|....*....|...
gi 1037244487 477 TEDLPRNTMGKVQKNILRQQYAD 499
Cdd:PRK06018 512 VDAIPHTATGKILKTALREQFKD 534
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
39-494 |
2.06e-43 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 162.11 E-value: 2.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV----ASAAREGVA 114
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVdrsfEPLAREVLH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 115 TI----AQRHGAIVETLDADG----SGSLLD----LARDEPADFVDAS----RSADDLAAILYTSGTTGRSKGAMLTHGN 178
Cdd:PLN03102 131 LLssedSNLNLPVIFIHEIDFpkrpSSEELDyeclIQRGEPTPSLVARmfriQDEHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 179 LLSNALTLRDYWRVTSDDRLIHALPIFHTHGlFVATNVTLLAGASMVLLSKFDADEVVS--LMPEATMLMGVPTFYVRLL 256
Cdd:PLN03102 211 AYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG-WTFTWGTAARGGTSVCMRHVTAPEIYKniEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 ------QSPRFGKeaaanIRLFISGSAP---LLAETHtefeaRTGHAILERYGMTETN--------------MNTSNPYD 313
Cdd:PLN03102 290 kgnsldLSPRSGP-----VHVLTGGSPPpaaLVKKVQ-----RLGFQVMHAYGLTEATgpvlfcewqdewnrLPENQQME 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 GKRIAGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHI 393
Cdd:PLN03102 360 LKARQGVSILGLADVDVKNKETQESVPRDGKTMGEIVIKGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEI 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 394 VGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGA----------VLDEKTIVGALQD 463
Cdd:PLN03102 439 KDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGEttkedrvdklVTRERDLIEYCRE 518
|
490 500 510
....*....|....*....|....*....|.
gi 1037244487 464 RLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PLN03102 519 NLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
25-488 |
2.60e-43 |
|
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: 158.96 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17652 10 DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17652 90 ----------------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDR-LIHALPIFHthGLFVATNVTLLAGASMVL-----------LSKFDADEVVS--LMPEATmLMGVPT 250
Cdd:cd17652 124 AQIAAFDVGPGSRvLQFASPSFD--ASVWELLMALLAGATLVLapaeellpgepLADLLREHRIThvTLPPAA-LAALPP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQSPRFGKEAAAnirlfisgsaPLLAETHTefearTGHAILERYGMTETNMN-TSNPYDGKRIAGTVGLPLPDVR 329
Cdd:cd17652 201 DDLPDLRTLVVAGEACP----------AELVDRWA-----PGRRMINAYGPTETTVCaTMAGPLPGGGVPPIGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVI 402
Cdd:cd17652 266 VYVLDARLRPV-PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGRADDQVK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPR 482
Cdd:cd17652 345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
....*.
gi 1037244487 483 NTMGKV 488
Cdd:cd17652 425 TPNGKL 430
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
26-494 |
1.02e-42 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 159.68 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:PRK04319 72 EKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLIT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASA--AREGVATIAQ-RHGAIVETLDADGSG--SLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLL 180
Cdd:PRK04319 152 TPAllERKPADDLPSlKHVLLVGEDVEEGPGtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAML 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 181 SN------ALTLRD---YWrVTSDdrlihalPIFHT---HGLFVAtnvtLLAGASMVLL-SKFDA--------DEVVSL- 238
Cdd:PRK04319 232 QHyqtgkyVLDLHEddvYW-CTAD-------PGWVTgtsYGIFAP----WLNGATNVIDgGRFSPerwyrileDYKVTVw 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 239 --MPEA-TMLMGVptfyvrllqsprfGKEAAANIRL----FI-SGSAPLLAET----HTEFeartGHAILERYGMTETNM 306
Cdd:PRK04319 300 ytAPTAiRMLMGA-------------GDDLVKKYDLsslrHIlSVGEPLNPEVvrwgMKVF----GLPIHDNWWMTETGG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 307 NTSNPYDGKRI-AGTVGLPLPDVRVRVTDPaTGLVLPPEQTGMIEIKG--PNVFKGYWRMPEKTAAEFTGdGFFISGDLG 383
Cdd:PRK04319 363 IMIANYPAMDIkPGSMGKPLPGIEAAIVDD-QGNELPPNRMGNLAIKKgwPSMMRGIWNNPEKYESYFAG-DWYVSGDSA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 384 KIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVGA 460
Cdd:PRK04319 441 YMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEelkEEIRGF 520
|
490 500 510
....*....|....*....|....*....|....
gi 1037244487 461 LQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILR 494
Cdd:PRK04319 521 VKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
155-490 |
1.29e-42 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 154.73 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAMLTHGNLLSNALTL-RDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDAD 233
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 234 EVVSLMP--EATMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNP 311
Cdd:cd17635 82 SLFKILTtnAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 312 Y-DGKRIAGTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGY 390
Cdd:cd17635 162 TdDDSIEINAVGRPYPGVDVYLAA-TDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-DGWVNTGDLGERREDGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKpgAVLDEKTIVG---ALQDRLAR 467
Cdd:cd17635 240 LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS--AELDENAIRAlkhTIRRELEP 317
|
330 340
....*....|....*....|...
gi 1037244487 468 YKQPKRIIFTEDLPRNTMGKVQK 490
Cdd:cd17635 318 YARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-493 |
4.63e-42 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 161.28 E-value: 4.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12316 2026 DQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQrhgaiVETLDADGSGSLLDLARDEPADFVDasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK12316 2106 TQRHLLERLPLPAG-----VARLPLDRDAEWADYPDTAPAVQLA----GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPI----FHtHGLFVAtnvtLLAGASMVLL--SKFDADEVVSLMPEATMLMGV-PTFYVRLLQ 257
Cdd:PRK12316 2177 AAGERYELSPADCELQFMSFsfdgAH-EQWFHP----LLNGARVLIRddELWDPEQLYDEMERHGVTILDfPPVYLQQLA 2251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 SPRFGKEAAANIRLFISGSAPLLAETHTE-FEARTGHAILERYGMTETNMN----TSNPYDGKRIAGT-VGLPLPDVRVR 331
Cdd:PRK12316 2252 EHAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTpllwKCRPQDPCGAAYVpIGRALGNRRAY 2331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 332 VTDPATGLvLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:PRK12316 2332 ILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQVKIR 2410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDfGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNT 484
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQDGAS-GKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNP 2489
|
....*....
gi 1037244487 485 MGKVQKNIL 493
Cdd:PRK12316 2490 NGKLDRKAL 2498
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
25-493 |
1.47e-41 |
|
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: 155.18 E-value: 1.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17655 20 DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIaqrhGAIVETLDADgsgslldlARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17655 100 TQSHLQPPIAFI----GLIDLLDEDT--------IYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFhthglFVATnVT-----LLAGASMVLLSKFDADEVVSLMP-----EATMLMGVPTfYVR 254
Cdd:cd17655 168 WANKVIYQGEHLRVALFASIS-----FDAS-VTeifasLLSGNTLYIVRKETVLDGQALTQyirqnRITIIDLTPA-HLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 LLqsPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHA--ILERYGMTETNMN-TSNPYDGKRIAGT---VGLPLPDV 328
Cdd:cd17655 241 LL--DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNptITNAYGPTETTVDaSIYQYEPETDQQVsvpIGKPLGNT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 329 RVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVI 402
Cdd:cd17655 319 RIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQVK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEktivgaLQDRLAR----YKQPKRIIFTE 478
Cdd:cd17655 398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ------LREFLARelpdYMIPSYFIKLD 471
|
490
....*....|....*
gi 1037244487 479 DLPRNTMGKVQKNIL 493
Cdd:cd17655 472 EIPLTPNGKVDRKAL 486
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
22-495 |
2.12e-41 |
|
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: 153.62 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGAT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:cd17653 97 LLLTTD--------------------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHALPIfhthGLFVATNV---TLLAGASMVLlsKFDADEVVSLMPEATMLMGVPTFYVRLlqS 258
Cdd:cd17653 133 YVSQPPARLDVGPGSRVAQVLSI----AFDACIGEifsTLCNGGTLVL--ADPSDPFAHVARTVDALMSTPSILSTL--S 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PRfgkeAAANIRLFISG----SAPLLAEThtefeaRTGHAILERYGMTETNMNTSNP--YDGKRIagTVGLPLPDVRVRV 332
Cdd:cd17653 205 PQ----DFPNLKTIFLGgeavPPSLLDRW------SPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 333 TDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGGY 406
Cdd:cd17653 273 LDADLQPV-PEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRGF 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 407 NIYPKEVESEIDRIEGVVESAVIGVpHPDFgegVTAIVVrkPGAVlDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMG 486
Cdd:cd17653 352 RINLEEIEEVVLQSQPEVTQAAAIV-VNGR---LVAFVT--PETV-DVDGLRSELAKHLPSYAVPDRIIALDSFPLTANG 424
|
....*....
gi 1037244487 487 KVQKNILRQ 495
Cdd:cd17653 425 KVDRKALRE 433
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
151-487 |
9.66e-41 |
|
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: 150.23 E-value: 9.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 151 RSADDLAaILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRV--TSDDRLIHA------LPIFHT----HGLFVATNVTL 218
Cdd:cd05924 1 RSADDLY-ILYTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGefTPSEDAHKAaaaaagTVMFPApplmHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 219 LAGASMVLLS--KFDADEVVSLMPE--ATMLMGVPTFYVR-LLQSPRFGKEA-AANIRLFISGSAPLLAETHTEFEARTG 292
Cdd:cd05924 80 LLGGQTVVLPddRFDPEEVWRTIEKhkVTSMTIVGDAMARpLIDALRDAGPYdLSSLFAISSGGALLSPEVKQGLLELVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 293 HAIL-ERYGMTETNMNTSNpYDGKRIAGTVGLPLPDVRVRVTDPATGLVLPPEQT-GMIEIKGpNVFKGYWRMPEKTAAE 370
Cdd:cd05924 160 NITLvDAFGSSETGFTGSG-HSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGvGWIARRG-HIPLGYYGDEAKTAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 371 F-TGDG--FFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRK 447
Cdd:cd05924 238 FpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1037244487 448 PGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGK 487
Cdd:cd05924 318 EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
29-498 |
1.00e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 153.61 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 AREGVATiaqrhgaivetldADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGamLTHGNLLSNAL---- 184
Cdd:PRK13383 142 FAERIAG-------------ADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKG--VPRAPQLRSAVgvwv 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATnVTLLAGASMVLLSKFDADEVVSL--MPEATMLMGVPTFYVRLLQSPR-- 260
Cdd:PRK13383 207 TILDRTRLRTGSRISVAMPMFHGLGLGMLM-LTIALGGTVLTHRHFDAEAALAQasLHRADAFTAVPVVLARILELPPrv 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-SNPYDGKRIAGTVGLPLPDVRVRVTDpATGL 339
Cdd:PRK13383 286 RARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGAlATPADLRDAPETVGKPVAGCPVRILD-RNNR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPPEQTGMIEIKGPNVFKGYWRMPEKTAAeftgDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDR 419
Cdd:PRK13383 365 PVGPRVTGRIFVGGELAGTRYTDGGGKAVV----DGMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAA 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 420 IEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVqkniLRQQYA 498
Cdd:PRK13383 441 HPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKV----LRKELP 515
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-493 |
3.75e-40 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 155.70 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12467 1597 EQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLL 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQrhgaiVETLDADGSGSLLDLARDE-PADFVDAsrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:PRK12467 1677 TQSHLQARLPLPDG-----LRSLVLDQEDDWLEGYSDSnPAVNLAP----QNLAYVIYTSGSTGRPKGAGNRHGALVNRL 1747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRVTSDDRLIHALPI---FHTHGLFVAtnvtLLAGASMVLL---SKFDADEVVSLMPE--ATMLMGVPTFYVRL 255
Cdd:PRK12467 1748 CATQEAYQLSAADVVLQFTSFafdVSVWELFWP----LINGARLVIAppgAHRDPEQLIQLIERqqVTTLHFVPSMLQQL 1823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 256 LQSPRFGKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT-----SNPYDGKRIAGTVGLPLPDVRV 330
Cdd:PRK12467 1824 LQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVthwtcRRKDLEGRDSVPIGQPIANLST 1903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 331 RVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVIS 403
Cdd:PRK12467 1904 YILDASLNPV-PIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgtvgsrlYRTGDLARYRADGVIEYLGRIDHQVKI 1982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 404 GGYNIYPKEVESEIDRIEGVVESAVIGVPHPDfGEGVTAIVVRKPGAVLDEKTIVGALQDRLAR--------YKQPKRII 475
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREAVVIAQDGAN-GKQLVAYVVPTDPGLVDDDEAQVALRAILKNhlkaslpeYMVPAHLV 2061
|
490
....*....|....*...
gi 1037244487 476 FTEDLPRNTMGKVQKNIL 493
Cdd:PRK12467 2062 FLARMPLTPNGKLDRKAL 2079
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
26-499 |
1.08e-39 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 151.47 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQ-----RHGAIVETLDADGSG-------------SLLDlarDEPADFVDASRSADDLAAILYTSGTT 166
Cdd:PRK05620 117 ADPRLAEQLGEILKecpcvRAVVFIGPSDADSAAahmpegikvysyeALLD---GRSTVYDWPELDETTAAAICYSTGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 167 GRSKGAMLTHGNLLSNALTLR--DYWRVTSDDRLIHALPIFH--THGLFVATnvtLLAGASMVLLSKFDADEVVSLMPEA 242
Cdd:PRK05620 194 GAPKGVVYSHRSLYLQSLSLRttDSLAVTHGESFLCCVPIYHvlSWGVPLAA---FMSGTPLVFPGPDLSAPTLAKIIAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 TM---LMGVPTFYVRLL-----QSPRfgkeaAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMntsnpydg 314
Cdd:PRK05620 271 AMprvAHGVPTLWIQLMvhylkNPPE-----RMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSP-------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 315 kriAGTVGLPLPDV-------------------RVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMP----------- 364
Cdd:PRK05620 338 ---VGTVARPPSGVsgearwayrvsqgrfpaslEYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPteegggaastf 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 365 -----EKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEG 439
Cdd:PRK05620 415 rgedvEDANDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGER 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 440 VTAIVVRKPGAVLDEKT---IVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYAD 499
Cdd:PRK05620 495 PLAVTVLAPGIEPTRETaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLAD 557
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
29-493 |
1.41e-39 |
|
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: 148.77 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVasa 108
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 aregvatiaqrhgaivetldadgsgslldlardEPadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRD 188
Cdd:cd17650 91 ---------------------------------QP----------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 189 YWRVtsdDRLIHALPIFHTHGLFVATN---VTLLAGASMVLL---SKFDADEVVSLM--PEATMLMGVPTFYVRLLQSPR 260
Cdd:cd17650 128 EYEL---DSFPVRLLQMASFSFDVFAGdfaRSLLNGGTLVICpdeVKLDPAALYDLIlkSRITLMESTPALIRPVMAYVY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLLAETHTEFEARTGHA--ILERYGMTETNMNTSNPYDGKRIAGT-----VGLPLPDVRVRVT 333
Cdd:cd17650 205 RNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGmrIINSYGVTEATIDSTYYEEGRDPLGDsanvpIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 334 DPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGGYN 407
Cdd:cd17650 285 DERLQPQ-PVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 408 IYPKEVESEIDRIEGVVESAVIgVPHPDFGE-GVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMG 486
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVVA-VREDKGGEaRLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNG 440
|
....*..
gi 1037244487 487 KVQKNIL 493
Cdd:cd17650 441 KVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-499 |
3.33e-39 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 153.01 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 40 IAGALDTLGIrPGDRVAVQVEKSAEALILYLACLRSGAVYLPlntAYT--------LAELDYFIGDAEPRLVVVASAARE 111
Cdd:PRK05691 53 IAAALQARAS-FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 112 GVATIaqrhgaivETLDADGSGSLLDLARDEPA---DFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRD 188
Cdd:PRK05691 129 SLLQM--------EELAAANAPELLCVDTLDPAlaeAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRH 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 189 YWR--VTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK--FDADEVVSLmpEAT-----MLMGVPTFYVRLLqSP 259
Cdd:PRK05691 201 GFGidLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPayFLERPLRWL--EAIseyggTISGGPDFAYRLC-SE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 260 RFGKEAAANI-----RLFISGSAPLLAETHTEFEAR------TGHAILERYGMTETNMNTSNPYDGKRIA---------- 318
Cdd:PRK05691 278 RVSESALERLdlsrwRVAYSGSEPIRQDSLERFAEKfaacgfDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaeala 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 --------GTV----GLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFT---GDGFFISGDLG 383
Cdd:PRK05691 358 rnraepgtGSVlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVehdGRTWLRTGDLG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 384 KIdSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVES---AVIGVPHP-DFGEGVTAIVVRKPGAVLDEKTIVG 459
Cdd:PRK05691 438 FL-RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgrvAAFAVNHQgEEGIGIAAEISRSVQKILPPQALIK 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1037244487 460 ALQDRLARYKQ--PKRIIFTED--LPRNTMGKVQKNILRQQYAD 499
Cdd:PRK05691 517 SIRQAVAEACQeaPSVVLLLNPgaLPKTSSGKLQRSACRLRLAD 560
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
25-496 |
4.58e-39 |
|
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: 147.50 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsadDLAAILYTSGTTGRSKGAMLTHGNLLsNAL 184
Cdd:cd05940 81 V-------------------------------------------------DAALYIYTSGTTGLPKAAIISHRRAW-RGG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSD-DRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDA----DEVVSLmpEATMLMGVPTFYVRLLQSP 259
Cdd:cd05940 111 AFFAGSGGALPsDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSAsnfwDDIRKY--QATIFQYIGELCRYLLNQP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 260 RFGKEAAANIRLfISGSApLLAETHTEFEARTGHA-ILERYGMTETNMNTSNpYDGKRiaGTVG---------LPLPDVR 329
Cdd:cd05940 189 PKPTERKHKVRM-IFGNG-LRPDIWEEFKERFGVPrIAEFYAATEGNSGFIN-FFGKP--GAIGrnpsllrkvAPLALVK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRV-TD----PATGLV--LPPEQTGMI--EIKGPNVFKGYWRMPEKTAAEFT-----GDGFFISGDLGKIDSDGYVHIVG 395
Cdd:cd05940 264 YDLeSGepirDAEGRCikVPRGEPGLLisRINPLEPFDGYTDPAATEKKILRdvfkkGDAWFNTGDLMRLDGEGFWYFVD 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 396 RGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFG--EGVTAIVVRkPGAVLDEKTIVGALQDRLARYKQPKR 473
Cdd:cd05940 344 RLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDgrAGMAAIVLQ-PNEEFDLSALAAHLEKNLPGYARPLF 422
|
490 500
....*....|....*....|...
gi 1037244487 474 IIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:cd05940 423 LRLQPEMEITGTFKQQKVDLRNE 445
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
23-499 |
1.18e-38 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 148.79 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:cd05968 87 GTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASA-------------AREGVATIAQ-RHGAIVETLDADGSGSLL-DLARDE--PADFVDASRS-ADDLAAILYTSG 164
Cdd:cd05968 167 LITADGftrrgrevnlkeeADKACAQCPTvEKVVVVRHLGNDFTPAKGrDLSYDEekETAGDGAERTeSEDPLMIIYTSG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 165 TTGRSKGAMLTHGNL-LSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNvTLLAGASMVL------------LSKF- 230
Cdd:cd05968 247 TTGKPKGTVHVHAGFpLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFG-GLILGATMVLydgapdhpkadrLWRMv 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 231 DADEVVSLMPEATM---LMGVPTFYVRllqsprfgKEAAANIRLFISGSAPLLAETHTEFEARTGHA---ILERYGMTET 304
Cdd:cd05968 326 EDHEITHLGLSPTLiraLKPRGDAPVN--------AHDLSSLRVLGSTGEPWNPEPWNWLFETVGKGrnpIINYSGGTEI 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 305 NMNTSNPYDGKRI-AGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTG--DGFFISGD 381
Cdd:cd05968 398 SGGILGNVLIKPIkPSSFNGPVPGMKADVLDESGKPARPEVGELVLLAPWPGMTRGFWRDEDRYLETYWSrfDNVWVHGD 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 382 LGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPG----AVLDEKTI 457
Cdd:cd05968 478 FAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvtptEALAEELM 557
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1037244487 458 VGAlQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYAD 499
Cdd:cd05968 558 ERV-ADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAYLG 598
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
42-497 |
3.22e-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: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 42 GALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNtaytlaeldyfIGDAEPRLvvvasaaregvatiaQRHG 121
Cdd:cd05908 30 GALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS-----------IGSNEEHK---------------LKLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 122 AIVETLdadgSGSLLdLARDEPADfvdasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHA 201
Cdd:cd05908 84 KVWNTL----KNPYL-ITEEEVLC-----ELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 202 LPIFHTHGLFVATNVTLLAGASMVllskfdadevvsLMPEATM-------LMGVPTFYVRLLQSPRFG---------KEA 265
Cdd:cd05908 154 MPLTHDMGLIAFHLAPLIAGMNQY------------LMPTRLFirrpilwLKKASEHKATIVSSPNFGykyflktlkPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 266 AAN-----IRLFISGSAPLLAETHTEFEARTG------HAILERYGMTETNMNTSNP----------------YDGKRIA 318
Cdd:cd05908 222 ANDwdlssIRMILNGAEPIDYELCHEFLDHMSkyglkrNAILPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GT------------VGLPLPDVRVRVTDPATGlVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKId 386
Cdd:cd05908 302 EVdkkdsecltfveVGKPIDETDIRICDEDNK-ILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 387 SDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVV--ESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDR 464
Cdd:cd05908 380 RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVElgRVVACGVNNSNTRNEEIFCFIEHRKSEDDFYPLGKKIKKH 459
|
490 500 510
....*....|....*....|....*....|....*
gi 1037244487 465 LARYK--QPKRIIFTEDLPRNTMGKVQKNILRQQY 497
Cdd:cd05908 460 LNKRGgwQINEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-493 |
3.37e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 149.72 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVvv 105
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLL-- 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 asaaregvatIAQRHgaIVETLDADGSGSLLDLarDEPADFVDA--------SRSADDLAAILYTSGTTGRSKGAMLTHG 177
Cdd:PRK12316 613 ----------LSQSH--LGRKLPLAAGVQVLDL--DRPAAWLEGyseenpgtELNPENLAYVIYTSGSTGKPKGAGNRHR 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 178 NLLSNALTLRDYWRVTSDDRLIHALPIFHTHG---LFvatnVTLLAGASMVLLSK---FDADEVVSLMPE--ATMLMGVP 249
Cdd:PRK12316 679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSvweFF----WPLMSGARLVVAAPgdhRDPAKLVELINRegVDTLHFVP 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 250 TFYVRLLQSPrfGKEAAANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTETNMNTSNPYDGKRIAGTV--GLPLP 326
Cdd:PRK12316 755 SMLQAFLQDE--DVASCTSLRRIVCSGEALPADAQEQVFAKLPQAgLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 327 DVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:PRK12316 833 NLACYILD-ANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEYAGRIDHQ 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVphpDFGEGVTAIVVRKPGAVLDEkTIVGALQDRLARYKQPKRIIFTEDL 480
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQLVGYVVLESEGGDWRE-ALKAHLAASLPEYMVPAQWLALERL 987
|
490
....*....|...
gi 1037244487 481 PRNTMGKVQKNIL 493
Cdd:PRK12316 988 PLTPNGKLDRKAL 1000
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
25-493 |
4.17e-38 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 149.04 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK10252 481 RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIAQRHGAIVETLDADGSGSllDLARDEPadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK10252 561 TTADQLPRFADVPDLTSLCYNAPLAPQGAA--PLQLSQP----------HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPifhthglfVATNVT-------LLAGASMVL-----------LSKFDADEVVslmpeaTMLM 246
Cdd:PRK10252 629 WMQNHYPLTADDVVLQKTP--------CSFDVSvweffwpFIAGAKLVMaepeahrdplaMQQFFAEYGV------TTTH 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 247 GVPTFYVRLLQSP---RFGKEAAANIRLFISGSApLLAETHTEFEARTGHAILERYGMTETNMNTSN-PYDGKRIAGTVG 322
Cdd:PRK10252 695 FVPSMLAAFVASLtpeGARQSCASLRQVFCSGEA-LPADLCREWQQLTGAPLHNLYGPTEAAVDVSWyPAFGEELAAVRG 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 323 LPLP------DVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGY 390
Cdd:PRK10252 774 SSVPigypvwNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGA 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGvVESAVI-------GVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQD 463
Cdd:PRK10252 853 VEYLGRSDDQLKIRGQRIELGEIDRAMQALPD-VEQAVThacvinqAAATGGDARQLVGYLVSQSGLPLDTSALQAQLRE 931
|
490 500 510
....*....|....*....|....*....|
gi 1037244487 464 RLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:PRK10252 932 RLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
22-423 |
4.78e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 146.29 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWsyGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGA-----------VYLPLNTAYTLAE 90
Cdd:PRK07768 26 APVRHTW--GEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAsltmlhqptprTDLAVWAEDTLRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 91 LDyFIGDaepRLVVVaSAAREGVATIAQRHGAIVETLDadgsgsllDLARDEPADFVDASrsADDLAAILYTSGTTGRSK 170
Cdd:PRK07768 104 IG-MIGA---KAVVV-GEPFLAAAPVLEEKGIRVLTVA--------DLLAADPIDPVETG--EDDLALMQLTSGSTGSPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 171 GAMLTHGNLLSNALTLRDYWRVTSD-DRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE------AT 243
Cdd:PRK07768 169 AVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAEliskyrGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 244 MLMGvPTF-YV----RLLQSPRFGKEAAANIRLFISGSAPL---LAETHTEFEARTG---HAILERYGMTETNMNTS--- 309
Cdd:PRK07768 249 MTAA-PNFaYAllarRLRRQAKPGAFDLSSLRFALNGAEPIdpaDVEDLLDAGARFGlrpEAILPAYGMAEATLAVSfsp 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 310 ------------------------NPYDGKRIAgTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYwRMPE 365
Cdd:PRK07768 328 cgaglvvdevdadllaalrravpaTKGNTRRLA-TLGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGY-LTMD 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037244487 366 KTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGV 423
Cdd:PRK07768 405 GFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
37-493 |
2.34e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 142.84 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 37 SGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVasaaregvati 116
Cdd:cd12115 34 ANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT----------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 117 aqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLS------NALTLRDYW 190
Cdd:cd12115 103 -----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHRNAAAflqwaaAAFSAEELA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 191 RVTSDDRLIHALPIFHthgLFvatnVTLLAGASMVLlskfdADEVVSLM-----PEATMLMGVPTFYVRLLQSPRFgkea 265
Cdd:cd12115 148 GVLASTSICFDLSVFE---LF----GPLATGGKVVL-----ADNVLALPdlpaaAEVTLINTVPSAAAELLRHDAL---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 266 AANIRLFISGSAPLLAETHTEFEARTGHA-ILERYGMTE-TNMNTSNPYD-GKRIAGTVGLPLPDVRVRVTDPATGLVlP 342
Cdd:cd12115 212 PASVRVVNLAGEPLPRDLVQRLYARLQVErVVNLYGPSEdTTYSTVAPVPpGASGEVSIGRPLANTQAYVLDRALQPV-P 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 343 PEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFIS------GDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESE 416
Cdd:cd12115 291 LGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGarlyrtGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAA 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037244487 417 IDRIEGvVESAVIGVPHPDFGE-GVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd12115 371 LRSIPG-VREAVVVAIGDAAGErRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
23-495 |
4.08e-37 |
|
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: 144.63 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRL 102
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCKL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAREGVATI---------------------AQRHG---AIVETLDADGSgsllDLARDEPADFVDASRSADDLAA 158
Cdd:cd05966 160 VITADGGYRGGKVIplkeivdealekcpsvekvlvVKRTGgevPMTEGRDLWWH----DLMAKQSPECEPEWMDSEDPLF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTH-GNLLSNALTLRDYWRVTSDDrlihalpIF-----------HTHGLFVAtnvtLLAGASMVL 226
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTgGYLLYAATTFKYVFDYHPDD-------IYwctadigwitgHSYIVYGP----LANGATTVM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 227 LskfdadEVVSLMPEA------------TMLMGVPTfYVRLLQspRFGKEAA-----ANIRLFISGSAPLLAETHTEFEA 289
Cdd:cd05966 305 F------EGTPTYPDPgrywdivekhkvTIFYTAPT-AIRALM--KFGDEWVkkhdlSSLRVLGSVGEPINPEAWMWYYE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 290 RTGH---AILERYGMTET--NMNTSNPYDGKRIAGTVGLPLPDVRVRVTDPaTGLVLPPEQTGMIEIKG--PNVFKGYWR 362
Cdd:cd05966 376 VIGKercPIVDTWWQTETggIMITPLPGATPLKPGSATRPFFGIEPAILDE-EGNEVEGEVEGYLVIKRpwPGMARTIYG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 363 MPEKTAAEFTGD--GFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGV 440
Cdd:cd05966 455 DHERYEDTYFSKfpGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAI 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1037244487 441 TAIVVRKPGAVLD---EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd05966 535 YAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
22-497 |
4.11e-37 |
|
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: 144.38 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:cd05967 77 TGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASAAREG---------------VATIAQRHGAIVETLDAdgSGSLLDLARD----------EPADFVdaSRSADDL 156
Cdd:cd05967 157 LIVTASCGIEPgkvvpykplldkaleLSGHKPHHVLVLNRPQV--PADLTKPGRDldwsellakaEPVDCV--PVAATDP 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 157 AAILYTSGTTGRSKGAML-THGNLLSNALTLR--------DYWRVTSDDRLI--HALPIFHThglfvatnvtLLAGASMV 225
Cdd:cd05967 233 LYILYTSGTTGKPKGVVRdNGGHAVALNWSMRniygikpgDVWWAASDVGWVvgHSYIVYGP----------LLHGATTV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 226 L-----LSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAA----ANIR-LFISGSaPLLAETHTEFEARTGH 293
Cdd:cd05967 303 LyegkpVGTPDPGAFWRVIEKyqVNALFTAPTAIRAIRKEDPDGKYIKkydlSSLRtLFLAGE-RLDPPTLEWAENTLGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 294 AILERYGMTETNMN-TSNP--YDGKRI-AGTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGP---NVFKGYWRMPEK 366
Cdd:cd05967 382 PVIDHWWQTETGWPiTANPvgLEPLPIkAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLPlppGCLLTLWKNDER 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 367 TAAEFTGD--GFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIV 444
Cdd:cd05967 461 FKKLYLSKfpGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLV 540
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 445 VRKPGAVLD----EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQY 497
Cdd:cd05967 541 VLKEGVKITaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIA 597
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
29-495 |
4.98e-37 |
|
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: 141.55 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELdyfigdaeprlvvvasa 108
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL----------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 aREGVatiaQRHGAIVETldadgsgslldlardepadfVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALT--- 185
Cdd:cd05974 65 -RDRV----DRGGAVYAA--------------------VDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLStmy 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 ---LRD---YWRVTSDDRLIHALPIFhthglFVATNvtllAGASMVLL--SKFDADEVVSLMPEA--TMLMGVPTFYVRL 255
Cdd:cd05974 120 wigLKPgdvHWNISSPGWAKHAWSCF-----FAPWN----AGATVFLFnyARFDAKRVLAALVRYgvTTLCAPPTVWRML 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 256 LQSPRFGkeAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDP 335
Cdd:cd05974 191 IQQDLAS--FDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 ATGLVLPPEQTGMIEIKGP-NVFKGYWRMPEKTAAEFtGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVE 414
Cdd:cd05974 269 DGAPATEGEVALDLGDTRPvGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 415 SEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKT---IVGALQDRLARYKQPKRIIFTEdLPRNTMGKVQKN 491
Cdd:cd05974 348 SVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETaleIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRV 426
|
....
gi 1037244487 492 ILRQ 495
Cdd:cd05974 427 ELRR 430
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
26-500 |
2.11e-36 |
|
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: 140.76 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd05918 23 GSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:cd05918 103 SSP---------------------------------------------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRL---------IHALPIFhthglfvatnVTLLAGASMVLLSKFD-----ADEVVSLmpEATMLMGVPTF 251
Cdd:cd05918 138 HGRALGLTSESRVlqfasytfdVSILEIF----------TTLAAGGCLCIPSEEDrlndlAGFINRL--RVTWAFLTPSV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 252 yVRLLQsprfgKEAAANIRLFISGSAPLlaeTHTEFEARTGHA-ILERYGMTETNMN-TSNPYDGKRIAGTVGLPLPdVR 329
Cdd:cd05918 206 -ARLLD-----PEDVPSLRTLVLGGEAL---TQSDVDTWADRVrLINAYGPAECTIAaTVSPVVPSTDPRNIGRPLG-AT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPAT-GLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEF-----------TGDG--FFISGDLGKIDSDGYVHIVG 395
Cdd:cd05918 276 CWVVDPDNhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFiedpawlkqegSGRGrrLYRTGDLVRYNPDGSLEYVG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 396 RGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVV------RKPGAVLDEKTIVG---------- 459
Cdd:cd05918 356 RKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAfvvldgSSSGSGDGDSLFLEpsdefralva 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1037244487 460 ----ALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYADL 500
Cdd:cd05918 436 elrsKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRELAESL 480
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
29-438 |
2.58e-36 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 143.57 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDaFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASA 108
Cdd:PRK06814 660 TYRK-LLTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTSRA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 109 ----AREG--VATIAQRHgAIVETLDADGSGSLLD----LARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGN 178
Cdd:PRK06814 739 fiekARLGplIEALEFGI-RIIYLEDVRAQIGLADkikgLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRN 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 179 LLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLL-SKFDadevVSLMPE------ATMLMGVPTF 251
Cdd:PRK06814 818 LLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYpSPLH----YRIIPEliydtnATILFGTDTF 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 252 ---YVRLLQSPRFgkeaaANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETN----MNTsnPYDGKriAGTVGLP 324
Cdd:PRK06814 894 lngYARYAHPYDF-----RSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApviaLNT--PMHNK--AGTVGRL 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 325 LPDVRVRVtDPATGLvlppEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISG 404
Cdd:PRK06814 965 LPGIEYRL-EPVPGI----DEGGRLFVRGPNVMLGYLRAENPGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA 1039
|
410 420 430
....*....|....*....|....*....|....
gi 1037244487 405 GYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGE 438
Cdd:PRK06814 1040 GEMISLAAVEELAAELWPDALHAAVSIPDARKGE 1073
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
128-498 |
5.65e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 137.10 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 128 DADGSGSLLDLAR-DEPADfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDywRVTSDDRLIHALPIFH 206
Cdd:PRK07824 16 DERRAALLRDALRvGEPID--------DDVALVVATSGTTGTPKGAMLTAAALTASADATHD--RLGGPGQWLLALPAHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 207 THGLFVATNvTLLAGASMVLL---SKFDADEvvslMPEATMLMG--------VPTFYVRLLQSPRfGKEAAANIRLFISG 275
Cdd:PRK07824 86 IAGLQVLVR-SVIAGSEPVELdvsAGFDPTA----LPRAVAELGggrrytslVPMQLAKALDDPA-ATAALAELDAVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 276 SAPLLAEThTEFEARTGHAILERYGMTETNMNTSnpYDGKriagtvglPLPDVRVRVTDpatglvlppeqtGMIEIKGPN 355
Cdd:PRK07824 160 GGPAPAPV-LDAAAAAGINVVRTYGMSETSGGCV--YDGV--------PLDGVRVRVED------------GRIALGGPT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 356 VFKGYwRMPEKTAAeFTGDGFFISGDLGKIDsDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPD 435
Cdd:PRK07824 217 LAKGY-RNPVDPDP-FAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDR 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037244487 436 FGEGVTAIVVRKPGA--VLDEktIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYA 498
Cdd:PRK07824 294 LGQRVVAAVVGDGGPapTLEA--LRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFA 356
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
25-493 |
4.87e-35 |
|
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: 136.14 E-value: 4.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17645 21 GQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17645 101 ----------------------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDR-LIHALPIFHTHGLFVATnvTLLAGASMVLLS---KFDADEVVSLMPEAtmlmGVPTFYVRLLQSPR 260
Cdd:cd17645 135 WHRPYFGVTPADKsLVYASFSFDASAWEIFP--HLTAGAALHVVPserRLDLDALNDYFNQE----GITISFLPTGAAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLlaethTEFEaRTGHAILERYGMTE-TNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpaTGL 339
Cdd:cd17645 209 FMQLDNQSLRVLLTGGDKL-----KKIE-RKGYKLVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYILD--EAL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPPE-QTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKE 412
Cdd:cd17645 281 QLQPIgVAGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 413 VESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNI 492
Cdd:cd17645 361 IEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKA 438
|
.
gi 1037244487 493 L 493
Cdd:cd17645 439 L 439
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
20-496 |
5.17e-35 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 137.47 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 20 MRTGsGQTWSYGDAFALSGRIAGALDTLGiRPGDR--VAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGD 97
Cdd:PRK13388 20 VRYG-DRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 98 AEPRLVVVASAaregvatiaqrHGAIVETLDADGSgSLLDLARDEPADFVDASRS--------ADDLAAILYTSGTTGRS 169
Cdd:PRK13388 98 ADCQLLVTDAE-----------HRPLLDGLDLPGV-RVLDVDTPAYAELVAAAGAltphrevdAMDPFMLIFTSGTTGAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 170 KGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATML-- 245
Cdd:PRK13388 166 KAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRygATYFny 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 246 MGVPTFYvrLLQSPRFGKEAAANIRL-FISGSAPllaETHTEFEARTGHAILERYGMTETNMNTSNPYDGKriAGTVGLP 324
Cdd:PRK13388 246 VGKPLAY--ILATPERPDDADNPLRVaFGNEASP---RDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 325 LPDVRVrvTDPATGLVLPP-------------EQTG-MIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGY 390
Cdd:PRK13388 319 APGVAI--YNPETLTECAVarfdahgallnadEAIGeLVNTAGAGFFEGYYNNPEATA-ERMRHGMYWSGDLAYRDADGW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 391 VHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGAL--QDRLARY 468
Cdd:PRK13388 396 IYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLaaQPDLGTK 475
|
490 500
....*....|....*....|....*...
gi 1037244487 469 KQPKRIIFTEDLPRNTMGKVQKNILRQQ 496
Cdd:PRK13388 476 AWPRYVRIAADLPSTATNKVLKRELIAQ 503
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
25-493 |
1.31e-34 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 139.14 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREgvaTIAQRHGAIVETLDADGSGSLLDlarDEPADFVDAsrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK12467 3198 TQAHLLE---QLPAPAGDTALTLDRLDLNGYSE---NNPSTRVMG----ENLAYVIYTSGSTGKPKGVGVRHGALANHLC 3267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPiFHTHGLFVATNVTLLAGASMVLLSK--FDADEVVSLM-PEATMLMGVPTFYVRLLQSPRF 261
Cdd:PRK12467 3268 WIAEAYELDANDRVLLFMS-FSFDGAQERFLWTLICGGCLVVRDNdlWDPEELWQAIhAHRISIACFPPAYLQQFAEDAG 3346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 262 GKEAAANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNT---SNPYDGKRIAGTV--GLPLPDVRVRVTDPA 336
Cdd:PRK12467 3347 GADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVtlwKCGGDAVCEAPYApiGRPVAGRSIYVLDGQ 3426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 337 TGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVISGGYNIY 409
Cdd:PRK12467 3427 LNPV-PVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIE 3505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 410 PKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEkTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQ 489
Cdd:PRK12467 3506 LGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRE-TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVD 3584
|
....
gi 1037244487 490 KNIL 493
Cdd:PRK12467 3585 RKAL 3588
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
23-384 |
2.31e-34 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 136.55 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTW---SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL-----AELDYF 94
Cdd:PRK08180 62 GADGGWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 95 IGDAEPRLVVVASAAR--EGVATIAQRHGAIVETLDADGSG---SLLDLARDEPADFVDASRSA---DDLAAILYTSGTT 166
Cdd:PRK08180 142 LELLTPGLVFADDGAAfaRALAAVVPADVEVVAVRGAVPGRaatPFAALLATPPTAAVDAAHAAvgpDTIAKFLFTSGST 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 167 GRSKGAMLTHGNLLSNALTLRDYWRVTSDDR--LIHALPIFHTHGLFVATNVTLLAGASMVLlskfdaDE---VVSLMPE 241
Cdd:PRK08180 222 GLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGGNHNLGIVLYNGGTLYI------DDgkpTPGGFDE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 ---------ATMLMGVPTFYVRLLQSPRfgKEAA------ANIRLFISGSAPLLAETHTEFEARTGHAILER------YG 300
Cdd:PRK08180 296 tlrnlreisPTVYFNVPKGWEMLVPALE--RDAAlrrrffSRLKLLFYAGAALSQDVWDRLDRVAEATCGERirmmtgLG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 301 MTETN---MNTSNPYDGkriAGTVGLPLPDVRVRvtdpatgLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFF 377
Cdd:PRK08180 374 MTETApsaTFTTGPLSR---AGNIGLPAPGCEVK-------LV-PVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYY 442
|
....*..
gi 1037244487 378 ISGDLGK 384
Cdd:PRK08180 443 RSGDAVR 449
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
21-388 |
2.47e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 136.71 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTW---SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL-----AELD 92
Cdd:PRK12582 71 REPGHGQWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 93 YFIGDAEPRLVVVASAAREGVATIAQRHGA---IVETLDADGSGS--LLDLARDEPADFVDASRSA---DDLAAILYTSG 164
Cdd:PRK12582 151 HLFDLVKPRVVFAQSGAPFARALAALDLLDvtvVHVTGPGEGIASiaFADLAATPPTAAVAAAIAAitpDTVAKYLFTSG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 165 TTGRSKGAMLTHGNLLSNA---LTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLlskfDADEVVSLMPE 241
Cdd:PRK12582 231 STGMPKAVINTQRMMCANIamqEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYI----DDGKPLPGMFE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 242 ATM---------LMG-VPTFYVRLL----QSPRFGKEAAANIRLFISGSAPLLAETHTEFEA----RTGHAIL--ERYGM 301
Cdd:PRK12582 307 ETIrnlreisptVYGnVPAGYAMLAeameKDDALRRSFFKNLRLMAYGGATLSDDLYERMQAlavrTTGHRIPfyTGYGA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 302 TETNMNTSNPYDGKRIAGTVGLPLPDVRVRvtdpatglVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGD 381
Cdd:PRK12582 387 TETAPTTTGTHWDTERVGLIGLPLPGVELK--------LAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGD 458
|
....*...
gi 1037244487 382 LGK-IDSD 388
Cdd:PRK12582 459 AARfVDPD 466
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
27-448 |
3.74e-34 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 136.38 E-value: 3.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TW-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLN---------------------- 83
Cdd:PLN02736 77 KWmTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYdtlgpdavkfivnhaevaaifc 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 84 TAYTLAELDYFIGDAEP-RLVVVASAAREGVATIAQRHGAIVETLDAdgsgsLLDLARDEPADFVDASrsADDLAAILYT 162
Cdd:PLN02736 157 VPQTLNTLLSCLSEIPSvRLIVVVGGADEPLPSLPSGTGVEIVTYSK-----LLAQGRSSPQPFRPPK--PEDVATICYT 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 163 SGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTH-------GLFVATNVTLLAGASMVLLskfdaDEV 235
Cdd:PLN02736 230 SGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYervnqivMLHYGVAVGFYQGDNLKLM-----DDL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 236 VSLMPeaTMLMGVPTFYVRLLQ----------------------------------SPR-----FGKEAAA---NIRLFI 273
Cdd:PLN02736 305 AALRP--TIFCSVPRLYNRIYDgitnavkesgglkerlfnaaynakkqalengknpSPMwdrlvFNKIKAKlggRVRFMS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 274 SGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpatglvLP---------PE 344
Cdd:PLN02736 383 SGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVD------VPemnytsedqPY 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 345 QTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV-ISGGYNIYPKEVESEIDRIEGV 423
Cdd:PLN02736 457 PRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFkLAQGEYIAPEKIENVYAKCKFV 536
|
490 500
....*....|....*....|....*
gi 1037244487 424 VESAVIGvphPDFGEGVTAIVVRKP 448
Cdd:PLN02736 537 AQCFVYG---DSLNSSLVAVVVVDP 558
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
25-471 |
3.75e-34 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 133.84 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDyfigdaeprlvv 104
Cdd:PRK09029 26 DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaarEGVATIAQRHGAiveTLDADGSGSLLDLARDEPADFVDASR-SADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:PRK09029 94 ------ELLPSLTLDFAL---VLEGENTFSALTSLHLQLVEGAHAVAwQPQRLATMTLTSGSTGLPKAAVHTAQAHLASA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRVTSDDRLIHALPIFHTHGLFVatnVT--LLAGASMVL--LSKFDADEV----VSLmpeatmlmgVPTFYVRL 255
Cdd:PRK09029 165 EGVLSLMPFTAQDSWLLSLPLFHVSGQGI---VWrwLYAGATLVVrdKQPLEQALAgcthASL---------VPTQLWRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 256 LQSPrfgkEAAANIRLFISGSAPLLAETHTEFEAR-----TGhailerYGMTEtnMN---TSNPYDGKriaGTVGLPLPD 327
Cdd:PRK09029 233 LDNR----SEPLSLKAVLLGGAAIPVELTEQAEQQgircwCG------YGLTE--MAstvCAKRADGL---AGVGSPLPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 328 VRVRVTDpatglvlppeqtGMIEIKGPNVFKGYWR----MPektaaeFT-GDGFFISGDLGKIDsDGYVHIVGRGKDLVI 402
Cdd:PRK09029 298 REVKLVD------------GEIWLRGASLALGYWRqgqlVP------LVnDEGWFATRDRGEWQ-NGELTILGRLDNLFF 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIvgALQDRLARYKQP 471
Cdd:PRK09029 359 SGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVVESDSEAAVVNLAE--WLQDKLARFQQP 425
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
25-500 |
4.05e-34 |
|
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: 134.09 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIgdaeprlvv 104
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCI--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 vasaaregvaTIAQRHGAIVETLDAdgsgsLLDLARDEPADFVDasRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd05939 72 ----------TVSKAKALIFNLLDP-----LLTQSSTEPPSQDD--VNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDA----DEVVSLMPEATMLMGVPTFYvrLLQSPR 260
Cdd:cd05939 135 GAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAsnfwDDCVKYNCTIVQYIGEICRY--LLAQPP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSapLLAETHTEFEARTGHA-ILERYGMTETNMNTSNpYDGKRIA-GTVGLPLPD---VRVRVTDP 335
Cdd:cd05939 213 SEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPqIGEFYGATEGNSSLVN-IDNHVGAcGFNSRILPSvypIRLIKVDE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 336 AT--------GLVLP--PEQTGMI--EIKGPNV---FKGYwrMPEKTAAE------FT-GDGFFISGDLGKIDSDGYVHI 393
Cdd:cd05939 290 DTgelirdsdGLCIPcqPGEPGLLvgKIIQNDPlrrFDGY--VNEGATNKkiardvFKkGDSAFLSGDVLVMDELGYLYF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 394 VGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGV--PHPDFGEGVTAIVVRKPGAVLDektIVGA-LQDRLARYKQ 470
Cdd:cd05939 368 KDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVevPGVEGRAGMAAIVDPERKVDLD---RFSAvLAKSLPPYAR 444
|
490 500 510
....*....|....*....|....*....|
gi 1037244487 471 PKRIIFTEDLPRNTMGKVQKNILRQQYADL 500
Cdd:cd05939 445 PQFIRLLPEVDKTGTFKLQKTDLQKEGYDP 474
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
23-388 |
8.61e-34 |
|
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: 134.48 E-value: 8.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 23 GSGQTW---SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL-----AELDYF 94
Cdd:cd05921 18 EGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 95 IGDAEPRLVVVASAA--REGVATIAQRHGAIVET---LDADGSGSLLDLARDEPADFVDASRSA---DDLAAILYTSGTT 166
Cdd:cd05921 98 FELLKPGLVFAQDAApfARALAAIFPLGTPLVVSrnaVAGRGAISFAELAATPPTAAVDAAFAAvgpDTVAKFLFTSGST 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 167 GRSKGAMLTHGNLLSNALTLRDYWRVTSDD--RLIHALPIFHTHGLFVATNVTLLAGASMVLlskfDA------------ 232
Cdd:cd05921 178 GLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYI----DDgkpmpggfeetl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 233 DEVVSLMPeaTMLMGVPTFYVRLLQSPRfgKEAA------ANIRLFISGSAPL----------LAETHtefearTGHAI- 295
Cdd:cd05921 254 RNLREISP--TVYFNVPAGWEMLVAALE--KDEAlrrrffKRLKLMFYAGAGLsqdvwdrlqaLAVAT------VGERIp 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 296 -LERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRvtdpatgLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGD 374
Cdd:cd05921 324 mMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELK-------LV-PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEE 395
|
410
....*....|....*
gi 1037244487 375 GFFISGDLGKI-DSD 388
Cdd:cd05921 396 GFYCLGDAAKLaDPD 410
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
26-493 |
2.23e-33 |
|
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: 132.21 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVv 105
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 asaaregvatiAQRHGAivETLDADGSGSLL--DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd17656 91 -----------TQRHLK--SKLSFNKSTILLedPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRV-TSDDRLIHALPIFHT--HGLFvatnVTLLAGASMVLLS---KFDADEVVSLMP-EATMLMGVPTFYVRLL 256
Cdd:cd17656 158 HFEREKTNInFSDKVLQFATCSFDVcyQEIF----STLLSGGTLYIIReetKRDVEQLFDLVKrHNIEVVFLPVAFLKFI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 QSPR-FGKEAAANIRLFIS-GSAPLLAETHTEFEARTGHAILERYGMTETN---MNTSNPYDGKRIAGTVGLPLPDVRVR 331
Cdd:cd17656 234 FSEReFINRFPTCVKHIITaGEQLVITNEFKEMLHEHNVHLHNHYGPSETHvvtTYTINPEAEIPELPPIGKPISNTWIY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 332 VTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGG 405
Cdd:cd17656 314 ILDQEQQLQ-PQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 406 YNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVrkPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTM 485
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPN 470
|
....*...
gi 1037244487 486 GKVQKNIL 493
Cdd:cd17656 471 GKVDRKAL 478
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
25-497 |
2.95e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 135.08 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL 3159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAARegvatIAQRHGAIVETLDADGSgsllDLARDEPADFVDasrsADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK12316 3160 SQSHLR-----LPLAQGVQVLDLDRGDE----NYAEANPAIRTM----PENLAYVIYTSGSTGKPKGVGIRHSALSNHLC 3226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIHALPiFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMP-EATMLMGVPTFYVRLLQSPRFGK 263
Cdd:PRK12316 3227 WMQQAYGLGVGDRVLQFTT-FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVElINSEGVDVLHAYPSMLQAFLEEE 3305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 264 EAA--ANIRLFISGSAPLLAETHTEFEArtGHAILERYGMTETNMNTSNPYDGKRIAGT--VGLPLPDVRVRVTDpATGL 339
Cdd:PRK12316 3306 DAHrcTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILD-GSLE 3382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 340 VLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF------FISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEV 413
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEI 3462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 414 ESEIDRIEGVVESAVIGVPhpdfGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLP--------RNTM 485
Cdd:PRK12316 3463 EARLLEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPltpngkldRKAL 3538
|
490
....*....|..
gi 1037244487 486 GKVQKNILRQQY 497
Cdd:PRK12316 3539 PRPDAALLQQDY 3550
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
26-474 |
5.36e-33 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 131.94 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAV---------YLPLNTAYTLAELDYFIG 96
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVpvlvdpgmgIKNLKQCLAEAQPDAFIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 97 DAEPRLVVV----ASAAREGVATIAQRH---GAIVETLDADGSGSLLDLARDEPadfvdasrsaDDLAAILYTSGTTGRS 169
Cdd:PRK09274 120 IPKAHLARRlfgwGKPSVRRLVTVGGRLlwgGTTLATLLRDGAAAPFPMADLAP----------DDMAAILFTSGSTGTP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 170 KGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFhthGLFvatnvTLLAGASMVlLSKFDADEVVSLMPEA------- 242
Cdd:PRK09274 190 KGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLF---ALF-----GPALGMTSV-IPDMDPTRPATVDPAKlfaaier 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 243 ---TMLMGVPTFYVRLLQSPRFGKEAAANIRLFISGSAPLLAETHTEFEA--RTGHAILERYGMTE----TNMNTSNPYD 313
Cdd:PRK09274 261 ygvTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAmlPPDAEILTPYGATEalpiSSIESREILF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 314 GKRI-----AGT-VGLPLPDVRVRVTDPATG--------LVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAE--FTGDGFF 377
Cdd:PRK09274 341 ATRAatdngAGIcVGRPVDGVEVRIIAISDApipewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGDV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 378 I--SGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPdfGEGVTAIVV-RKPGAVLDE 454
Cdd:PRK09274 421 WhrMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVLCVeLEPGVACSK 498
|
490 500
....*....|....*....|
gi 1037244487 455 KTIVGALQDRLARYKQPKRI 474
Cdd:PRK09274 499 SALYQELRALAAAHPHTAGI 518
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
26-451 |
1.30e-32 |
|
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: 131.01 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAAR-EGVATIAQR-------------------HGAIVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGT 165
Cdd:cd17641 90 EDEEQvDKLLEIADRipsvryviycdprgmrkydDPRLISFEDVVALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 166 TGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHThGLFVATnvtllAGASMVLLSKFDADEVVSLMPEATML 245
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWI-GEQMYS-----VGQALVCGFIVNFPEEPETMMEDLRE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 246 MGvPTFY---------------VRLLQSPRF-----------GKEAAA-------------------------------- 267
Cdd:cd17641 244 IG-PTFVllpprvwegiaadvrARMMDATPFkrfmfelgmklGLRALDrgkrgrpvslwlrlaswladallfrplrdrlg 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 268 --NIRLFISGSAPLLAETHTEFEArTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRVTDpatglvlppeq 345
Cdd:cd17641 323 fsRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE----------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 346 TGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDL-VISGGYNIYPKEVESEIDRIEGVV 424
Cdd:cd17641 391 VGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVgTTSDGTRFSPQFIENKLKFSPYIA 470
|
490 500
....*....|....*....|....*..
gi 1037244487 425 ESAVIGVPHPdfgeGVTAIVVRKPGAV 451
Cdd:cd17641 471 EAVVLGAGRP----YLTAFICIDYAIV 493
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
158-494 |
1.80e-32 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 130.73 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 158 AILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASmVLLSKFDADEVVS 237
Cdd:PLN02479 199 ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCGTN-ICLRQVTAKAIYS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 238 LMPEA--TMLMGVPTFYVRLLQSPrfgKEAAA-----NIRLFISGSAP---LLAEThtefeARTGHAILERYGMTETNMN 307
Cdd:PLN02479 278 AIANYgvTHFCAAPVVLNTIVNAP---KSETIlplprVVHVMTAGAAPppsVLFAM-----SEKGFRVTHTYGLSETYGP 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 308 TS-------------------NPYDGKRIAGTVGLPLPDVRVRVTDPATGLVLppeqtGMIEIKGPNVFKGYWRMPEKTA 368
Cdd:PLN02479 350 STvcawkpewdslppeeqarlNARQGVRYIGLEGLDVVDTKTMKPVPADGKTM-----GEIVMRGNMVMKGYLKNPKANE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 369 AEFTGdGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKP 448
Cdd:PLN02479 425 EAFAN-GWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKP 503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1037244487 449 GA-VLDEKTIVGAL----QDRLARYKQPKRIIFTEdLPRNTMGKVQKNILR 494
Cdd:PLN02479 504 GVdKSDEAALAEDImkfcRERLPAYWVPKSVVFGP-LPKTATGKIQKHVLR 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-493 |
2.37e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 132.21 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASA------AREGVATIAqrhgaiVETLDADG---SGSLLDLardepadfvdasrSADDLAAILYTSGTTGRSKGAMLT 175
Cdd:PRK05691 1234 TQSHllerlpQAEGVSAIA------LDSLHLDSwpsQAPGLHL-------------HGDNLAYVIYTSGSTGQPKGVGNT 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLLSNALTLRDYWRVTSDDRLIHALPIfhthglfvATNVT-------LLAGASMVLLS---KFDADEVVSLMPE--AT 243
Cdd:PRK05691 1295 HAALAERLQWMQATYALDDSDVLMQKAPI--------SFDVSvwecfwpLITGCRLVLAGpgeHRDPQRIAELVQQygVT 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 244 MLMGVPTFYVRLLQSPRFGkeAAANIRLFISGSAPLLAETHTEFEARTGHAILE-RYGMTETNMNTSNPY----DGKRia 318
Cdd:PRK05691 1367 TLHFVPPLLQLFIDEPLAA--ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHnRYGPTETAINVTHWQcqaeDGER-- 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 GTVGLPLPDVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYV 391
Cdd:PRK05691 1443 SPIGRPLGNVLCRVLDAELNLL-PPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNADGAL 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 392 HIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIgVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQP 471
Cdd:PRK05691 1522 EYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVP 1600
|
490 500
....*....|....*....|..
gi 1037244487 472 KRIIFTEDLPRNTMGKVQKNIL 493
Cdd:PRK05691 1601 AQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
25-499 |
1.35e-31 |
|
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: 126.78 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLhDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVasaaregvatiaqrhgaivetldadgsgslldlarDEpadfvdasrsaDDLAAILYTSGTTGRSKGAMLTHGNLLSNA 183
Cdd:cd05937 83 IV-----------------------------------DP-----------DDPAILIYTSGTTGLPKAAAISWRRTLVTS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 184 LTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDA----DEVVSlmPEATMLMGVPTFYVRLLQSP 259
Cdd:cd05937 117 NLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSAsqfwKDVRD--SGATIIQYVGELCRYLLSTP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 260 RFGKEAAANIRL-FISGSAPllaETHTEFEARTG-HAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVR-------- 329
Cdd:cd05937 195 PSPYDRDHKVRVaWGNGLRP---DIWERFRERFNvPEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRwkfenqvv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 -VRVtDPATGLVLPPEQTGMIE-------------IKGPNV--FKGYWRMPEKTAAEFT------GDGFFISGDLGKIDS 387
Cdd:cd05937 272 lVKM-DPETDDPIRDPKTGFCVrapvgepgemlgrVPFKNReaFQGYLHNEDATESKLVrdvfrkGDIYFRTGDLLRQDA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 388 DGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGV--PHPDFGEGVTAIVVRKPGAVLDEKT---IVGALQ 462
Cdd:cd05937 351 DGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvPGHDGRAGCAAITLEESSAVPTEFTkslLASLAR 430
|
490 500 510
....*....|....*....|....*....|....*..
gi 1037244487 463 DRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYAD 499
Cdd:cd05937 431 KNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGVD 467
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
22-497 |
2.19e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.13 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:PRK05691 2208 TFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIG 2287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASAAREGVATIAQrhGAIVETLDADGSGslLDLARDEPADFVDASRSaddLAAILYTSGTTGRSKGAMLTHGNLLS 181
Cdd:PRK05691 2288 LLLSDRALFEALGELPA--GVARWCLEDDAAA--LAAYSDAPLPFLSLPQH---QAYLIYTSGSTGKPKGVVVSHGEIAM 2360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NALTLRDYWRVTSDDRLIHalpiFHTHGLFVATN---VTLLAGASMVLLS--KFDADEVVSLMPE--ATMLMGVPTFYVR 254
Cdd:PRK05691 2361 HCQAVIERFGMRADDCELH----FYSINFDAASErllVPLLCGARVVLRAqgQWGAEEICQLIREqqVSILGFTPSYGSQ 2436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 255 LLQSpRFGKEAAANIRLFISGSAPLLAETHTEF-EARTGHAILERYGMTET-NMNTSNPYDGKRIAGTVGLPLPDV---R 329
Cdd:PRK05691 2437 LAQW-LAGQGEQLPVRMCITGGEALTGEHLQRIrQAFAPQLFFNAYGPTETvVMPLACLAPEQLEEGAASVPIGRVvgaR 2515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 330 VRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF-------FISGDLGKIDSDGYVHIVGRGKDLVI 402
Cdd:PRK05691 2516 VAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRADGLVEYVGRIDHQVK 2595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDfGEGVTAIVVRKPGAVLDE------KTIVGALQDRLARYKQPKRIIF 476
Cdd:PRK05691 2596 IRGFRIELGEIESRLLEHPAVREAVVLALDTPS-GKQLAGYLVSAVAGQDDEaqaalrEALKAHLKQQLPDYMVPAHLIL 2674
|
490 500
....*....|....*....|....*....
gi 1037244487 477 TEDLPRNTMGKVQKNIL--------RQQY 497
Cdd:PRK05691 2675 LDSLPLTANGKLDRRALpapdpelnRQAY 2703
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
25-474 |
2.33e-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: 127.02 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGAL-DTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLV 103
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALlAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATI--AQRHGAIV-----ETLDADGSGSLLDLARDEPADFVDASRSAD----DLAAILYTSGTTGRSKGA 172
Cdd:cd05938 83 VVAPELQEAVEEVlpALRADGVSvwylsHTSNTEGVISLLDKVDAASDEPVPASLRAHvtikSPALYIYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 173 MLTHGNLL--SNALTLRDywrVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDAdevvSLMPEATMLMGVPT 250
Cdd:cd05938 163 RISHLRVLqcSGFLSLCG---VTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSA----SQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 F-YV-----RLLQSPRFGKEAAANIRLFIsGSApLLAETHTEFEARTGH-AILERYGMTETNMNTSNpYDGKRiaGTVG- 322
Cdd:cd05938 236 IqYIgellrYLCNQPQSPNDRDHKVRLAI-GNG-LRADVWREFLRRFGPiRIREFYGSTEGNIGFFN-YTGKI--GAVGr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 323 --------LPLPDVRVRVT--DP---ATGLVLP--PEQTGMI--EIKGPNVFKGYWRMPEKTAAEF------TGDGFFIS 379
Cdd:cd05938 311 vsylykllFPFELIKFDVEkeEPvrdAQGFCIPvaKGEPGLLvaKITQQSPFLGYAGDKEQTEKKLlrdvfkKGDVYFNT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 380 GDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDF-GEGVTAIVVRKPGAVLDEKTIV 458
Cdd:cd05938 391 GDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHeGRIGMAAVKLKPGHEFDGKKLY 470
|
490
....*....|....*...
gi 1037244487 459 GALQDRLARYKQPK--RI 474
Cdd:cd05938 471 QHVREYLPAYARPRflRI 488
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
25-488 |
6.73e-30 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 122.31 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLII 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVATIaqrhgaivETLDADgsgSLLD-LARDEPADFvDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLS-- 181
Cdd:PRK04813 105 ATEELPLEILGI--------PVITLD---ELKDiFATGNPYDF-DHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSft 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 182 NaltlrdyWrVTSDDRLIHAlPIFHTHGLF------VATNVTLLAGASMVLLSKfdadEVVS---LMPEA--TMLMGV-- 248
Cdd:PRK04813 173 N-------W-MLEDFALPEG-PQFLNQAPYsfdlsvMDLYPTLASGGTLVALPK----DMTAnfkQLFETlpQLPINVwv 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 249 --PTFYVRLLQSPRFGKEAAANIRLFIsgsapLLAEthtEFEARTGHAILER---------YGMTETNMNTS-------- 309
Cdd:PRK04813 240 stPSFADMCLLDPSFNEEHLPNLTHFL-----FCGE---ELPHKTAKKLLERfpsatiyntYGPTEATVAVTsieitdem 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 310 -NPYDgkRIAgtVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEF-TGDG--FFISGDLGKI 385
Cdd:PRK04813 312 lDQYK--RLP--IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGqpAYHTGDAGYL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 386 DsDGYVHIVGRgKDLVIS-GGYNIYPKEVESEIDRIEGvVESAVIgVPHPDfGEGVT---AIVVRKPGAVLDE----KTI 457
Cdd:PRK04813 387 E-DGLLFYQGR-IDFQIKlNGYRIELEEIEQNLRQSSY-VESAVV-VPYNK-DHKVQyliAYVVPKEEDFEREfeltKAI 461
|
490 500 510
....*....|....*....|....*....|.
gi 1037244487 458 VGALQDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKI 492
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
25-493 |
8.96e-30 |
|
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: 121.39 E-value: 8.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVV 104
Cdd:cd17644 23 DQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VasaaregvatiaqrhgaivetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:cd17644 103 T----------------------------------------------QPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSDDRLIhalpIFHTHGLFVATN---VTLLAGASMVL---LSKFDADEVVSLMPEATM-LMGVPTFYVRLLQ 257
Cdd:cd17644 137 GLIKEYGITSSDRVL----QFASIAFDVAAEeiyVTLLSGATLVLrpeEMRSSLEDFVQYIQQWQLtVLSLPPAYWHLLV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 SPRFGKEAA--ANIRLFISGSAPLLAETHTEFEARTGHAI--LERYGMTE-----TNMNTSNPYDGKRIAGTVGLPLPDV 328
Cdd:cd17644 213 LELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEatiaaTVCRLTQLTERNITSVPIGRPIANT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 329 RVRVTDpATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFIS--------GDLGKIDSDGYVHIVGRGKDL 400
Cdd:cd17644 293 QVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSeserlyktGDLARYLPDGNIEYLGRIDNQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 401 VISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDL 480
Cdd:cd17644 372 VKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEEL 451
|
490
....*....|...
gi 1037244487 481 PRNTMGKVQKNIL 493
Cdd:cd17644 452 PLTPNGKIDRRAL 464
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
32-414 |
3.42e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 120.88 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 32 DAFALSGRIAGaldtLGIRPGDRVAVQVEKSAEALILYLACLRSG--AVYLPLNTAYT-----LAELDYFIGDAEPRLVV 104
Cdd:PRK09192 58 RAEAGARRLLA----LGLKPGDRVALIAETDGDFVEAFFACQYAGlvPVPLPLPMGFGgresyIAQLRGMLASAQPAAII 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 105 VASAAREGVAtiaqrhgAIVETLDADGSGSLLDLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK09192 134 TPDELLPWVN-------EATHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TL-RDYWRVTSDDRLIHALPIFHTHGL--FVATNVTllAGASMVLLskfdadevvslmpeatmlmgvPT--FYVRLLQ-- 257
Cdd:PRK09192 207 AIsHDGLKVRPGDRCVSWLPFYHDMGLvgFLLTPVA--TQLSVDYL---------------------PTrdFARRPLQwl 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 ------------SPRFGKEAAA--------------NIRLFISGSAPLLAETHTEFEAR------TGHAILERYGMTETN 305
Cdd:PRK09192 264 dlisrnrgtisySPPFGYELCArrvnskdlaeldlsCWRVAGIGADMIRPDVLHQFAEAfapagfDDKAFMPSYGLAEAT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 306 MNTSNP-----------------YDGKRIAGTV-----------GLPLPDVRVRVTDPAtGLVLPPEQTGMIEIKGPNVF 357
Cdd:PRK09192 344 LAVSFSplgsgivveevdrdrleYQGKAVAPGAetrrvrtfvncGKALPGHEIEIRNEA-GMPLPERVVGHICVRGPSLM 422
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 358 KGYWRMPEkTAAEFTGDGFFISGDLGKIdSDGYVHIVGRGKDLVISGGYNIYPKEVE 414
Cdd:PRK09192 423 SGYFRDEE-SQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIE 477
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
29-493 |
3.75e-29 |
|
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: 119.43 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLG-IRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAS 107
Cdd:cd17648 14 TYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVITNS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 108 AaregvatiaqrhgaivetldadgsgslldlardepadfvdasrsadDLAAILYTSGTTGRSKGAMLTHGNLLS--NALT 185
Cdd:cd17648 94 T----------------------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVNlrTSLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRLihalpifhthgLFVATNV----------TLLAGASMVLLS---KFDADEVVSLMPE--ATMLMGVPT 250
Cdd:cd17648 128 ERYFGRDNGDEAV-----------LFFSNYVfdffveqmtlALLNGQKLVVPPdemRFDPDRFYAYINRekVTYLSGTPS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 fyvrLLQSPRFGKEAAANiRLFISG---SAPLLAETHTEFEARtghaILERYGMTETNM-NTSNPYDG-KRIAGTVGLPL 325
Cdd:cd17648 197 ----VLQQYDLARLPHLK-RVDAAGeefTAPVFEKLRSRFAGL----IINAYGPTETTVtNHKRFFPGdQRFDKSLGRPV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 326 PDVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGF--------------FISGDLGKIDSDGYV 391
Cdd:cd17648 268 RNTKCYVLNDAMKRV-PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 392 HIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGE--GVTAIV---VRKPGAVlDEKTIVGALQDRLA 466
Cdd:cd17648 347 EYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQsrIQKYLVgyyLPEPGHV-PESDLLSFLRAKLP 425
|
490 500
....*....|....*....|....*..
gi 1037244487 467 RYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd17648 426 RYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
51-449 |
4.19e-29 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 120.31 E-value: 4.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 51 PGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVAsaaREGVATIAQRHGAIVE----- 125
Cdd:PRK06334 66 PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTS---KQLMQHLAQTHGEDAEypfsl 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 126 --TLDADGSGSLLDLAR-----DEPAD-----FVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVT 193
Cdd:PRK06334 143 iyMEEVRKELSFWEKCRigiymSIPFEwlmrwFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 194 SDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK-FDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIR 270
Cdd:PRK06334 223 EDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAYNpLYPKKIVEMIDEakVTFLGSTPVFFDYILKTAKKQESCLPSLR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 271 LFISGSAPLLAETHTEFEARTGHAILER-YGMTETN-MNTSNPYDGKRIAGTVGLPLPDVRVRVTDPATGLVLPPEQTGM 348
Cdd:PRK06334 303 FVVIGGDAFKDSLYQEALKTFPHIQLRQgYGTTECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPVSSGETGL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 349 IEIKGPNVFKGYW-RMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIdrIEGVVEsa 427
Cdd:PRK06334 383 VLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL--MEGFGQ-- 458
|
410 420
....*....|....*....|..
gi 1037244487 428 vigvphPDFGEGVTAIVVRKPG 449
Cdd:PRK06334 459 ------NAADHAGPLVVCGLPG 474
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
50-458 |
4.57e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.82 E-value: 4.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 50 RPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIG---DAEPRLVVVASAAREGVATIAQRHG----- 121
Cdd:PRK05850 57 STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAHDERVSAvlrDTSPSVVLTTSAVVDDVTEYVAPQPgqsap 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 122 AIVEtLDadgsgsLLDLarDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTL-RDYWRVT-----SD 195
Cdd:PRK05850 137 PVIE-VD------LLDL--DSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLmSDYFGDTggvppPD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 196 DRLIHALPIFHTHGLFVATNVTLLAGASMVLLSkfdadevvslmPEAtmLMGVPTFYVRLLQS--------PRFGKEAAA 267
Cdd:PRK05850 208 TTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTS-----------PVA--FLQRPARWMQLLASnphafsaaPNFAFELAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 268 --------------NIRLFISGSAPLLAETHTEFEARTGH------AILERYGMTETNM--NTSNP----------YDG- 314
Cdd:PRK05850 275 rktsdddmagldlgGVLGIISGSERVHPATLKRFADRFAPfnlretAIRPSYGLAEATVyvATREPgqppesvrfdYEKl 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 315 -----KRIAGTVGLPLpdVR--------VRVTDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEF---------- 371
Cdd:PRK05850 355 saghaKRCETGGGTPL--VSygsprsptVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspg 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 372 TGDGFFI-SGDLGKIdSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEG--VvesAVIGVPHPDFGEGVTAIVVRKP 448
Cdd:PRK05850 433 TPEGPWLrTGDLGFI-SEGELFIVGRIKDLLIVDGRNHYPDDIEATIQEITGgrV---AAISVPDDGTEKLVAIIELKKR 508
|
490
....*....|
gi 1037244487 449 GAvLDEKTIV 458
Cdd:PRK05850 509 GD-SDEEAMD 517
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
21-417 |
2.00e-28 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 119.00 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEP 100
Cdd:cd05933 2 RGDKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RLVVVASAAR-----------EGVATIAQRHGAIVETLDADGSGS-LLDLARDEPADFVDA---SRSADDLAAILYTSGT 165
Cdd:cd05933 82 NILVVENQKQlqkilqiqdklPHLKAIIQYKEPLKEKEPNLYSWDeFMELGRSIPDEQLDAiisSQKPNQCCTLIYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 166 TGRSKGAMLTHGNLLSNALTL-RDYWRVTSDDR---LIHALPIFHTHGLFVATNVTLLAGASMVLLSKfDA--DEVVSLM 239
Cdd:cd05933 162 TGMPKGVMLSHDNITWTAKAAsQHMDLRPATVGqesVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQP-DAlkGTLVKTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 240 PEA--TMLMGVP-----------------TFYVRLL--------------------QSPRFGKEAA-------------A 267
Cdd:cd05933 241 REVrpTAFMGVPrvwekiqekmkavgaksGTLKRKIaswakgvgletnlklmggesPSPLFYRLAKklvfkkvrkalglD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 268 NIRLFISGSAPLLAEThTEFEARTGHAILERYGMTETN----MNTSNPYdgkRIaGTVGLPLPDVRVRVTDP-ATGLvlp 342
Cdd:cd05933 321 RCQKFFTGAAPISRET-LEFFLSLNIPIMELYGMSETSgphtISNPQAY---RL-LSCGKALPGCKTKIHNPdADGI--- 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037244487 343 peqtGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVI-SGGYNIYPKEVESEI 417
Cdd:cd05933 393 ----GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVPIEDAV 464
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
39-495 |
8.56e-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: 116.38 E-value: 8.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV----ASAAREGVA 114
Cdd:cd05915 36 RLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFdpnlLPLVEAIRG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 115 TIAQRHGAIVETLDADGSGSLLDLARD--EPADFVDASrsadDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRV 192
Cdd:cd05915 116 ELKTVQHFVVMDEKAPEGYLAYEEALGeeADPVRVPER----AACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 193 TSDDRLIH--ALPIFHTHGLFVATNVTLLAGAsMVLLSKFDADEVV--SLMPEATMLMGVPTFYVRLLQSPR--FGKEAA 266
Cdd:cd05915 192 ALSEKDVVlpVVPMFHVNAWCLPYAATLVGAK-QVLPGPRLDPASLveLFDGEGVTFTAGVPTVWLALADYLesTGHRLK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 ANIRLFISGSAP----LLAETHTEFEARTGHAILERYGMTETNM-----NTSNPYDGKRIAGTVGLPLPDVRVRVTDPAT 337
Cdd:cd05915 271 TLRRLVVGGSAAprslIARFERMGVEVRQGYGLTETSPVVVQNFvkshlESLSEEEKLTLKAKTGLPIPLVRLRVADEEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 338 GLVLPPEQT-GMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESE 416
Cdd:cd05915 351 RPVPKDGKAlGEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 417 IDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKtIVGALQDRLARYKQ-PKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd05915 431 LMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEE-LNEHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
26-474 |
8.95e-27 |
|
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: 112.55 E-value: 8.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPrlvvv 105
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEP----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 asaaregvatiaqrhgaivetlDAdgsgslldlardepadFVDASRsADDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:cd05910 76 ----------------------DA----------------FIGIPK-ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRLIHALPIFhthGLF-VATNVTLLAGAsMVLLSKFDAD--EVVSLMPE--ATMLMGVPTFYVRLLQSPR 260
Cdd:cd05910 117 LRQLYGIRPGEVDLATFPLF---ALFgPALGLTSVIPD-MDPTRPARADpqKLVGAIRQygVSIVFGSPALLERVARYCA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 261 FGKEAAANIRLFISGSAPLLAETHTEFEA--RTGHAILERYGMTET---------NMNTSNPYDGKRIAGT-VGLPLPDV 328
Cdd:cd05910 193 QHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEAlpvssigsrELLATTTAATSGGAGTcVGRPIPGV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 329 RVRV---TD---PATG--LVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAE--FTGDGFFI--SGDLGKIDSDGYVHIVGR 396
Cdd:cd05910 273 RVRIieiDDepiAEWDdtLELPRGEIGEITVTGPTVTPTYVNRPVATALAkiDDNSEGFWhrMGDLGYLDDEGRLWFCGR 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037244487 397 GKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVtAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRI 474
Cdd:cd05910 353 KAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPV-LCVEPLPGTITPRARLEQELRALAKDYPHTQRI 429
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
150-398 |
3.32e-25 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 109.41 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 150 SRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSK 229
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 230 FDADEVVslmPE------ATMLMGVPTF---YVRLLQSPRFgkeaaANIRLFISGSAPLLAETHTEFEARTGHAILERYG 300
Cdd:PRK08043 441 PLHYRIV---PElvydrnCTVLFGTSTFlgnYARFANPYDF-----ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYG 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 301 MTE----TNMNTsnPYDGKriAGTVGLPLPDVRVRVTdPATGLvlppEQTGMIEIKGPNVFKGYWRMP-----EKTAAEF 371
Cdd:PRK08043 513 VTEcapvVSINV--PMAAK--PGTVGRILPGMDARLL-SVPGI----EQGGRLQLKGPNIMNGYLRVEkpgvlEVPTAEN 583
|
250 260 270
....*....|....*....|....*....|.
gi 1037244487 372 T-GD---GFFISGDLGKIDSDGYVHIVGRGK 398
Cdd:PRK08043 584 ArGEmerGWYDTGDIVRFDEQGFVQIQGRAK 614
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
25-401 |
2.19e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 106.98 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFalsGRiagALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVylpLNTAY-TLAE--LDYFIGDAEPR 101
Cdd:PTZ00216 125 AELWERIVNF---GR---GLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMV---AATVYaNLGEdaLAYALRETECK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASAA--------REGVAtiaqrHGAIVETLDA-----DGSG-------SLLDLARDEPADF-VDASRSADDLAAIL 160
Cdd:PTZ00216 196 AIVCNGKNvpnllrlmKSGGM-----PNTTIIYLDSlpasvDTEGcrlvawtDVVAKGHSAGSHHpLNIPENNDDLALIM 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 161 YTSGTTGRSKGAMLTHGNLLSNALTLRDywRVTS-------DDRLIHALPIFHTHGlFVATNVTLLAGASM------VLL 227
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLTAGILALED--RLNDligppeeDETYCSYLPLAHIME-FGVTNIFLARGALIgfgsprTLT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 228 SKF-----DADEVvslmpEATMLMGVPTFY--------VRL------------------LQSPRFGKEA----------- 265
Cdd:PTZ00216 348 DTFarphgDLTEF-----RPVFLIGVPRIFdtikkaveAKLppvgslkrrvfdhayqsrLRALKEGKDTpywnekvfsap 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 266 ----AANIRLFISGSAPLLAETHtEFEARTGHAILERYGMTETNMNTSNPYDGKRIAGTVGLPLPDVRVRV--------T 333
Cdd:PTZ00216 423 ravlGGRVRAMLSGGGPLSAATQ-EFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMKLldteeykhT 501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1037244487 334 DPatglvlpPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:PTZ00216 502 DT-------PEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALA 562
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
50-414 |
6.47e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 105.20 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 50 RPGDRVAVQVEKSAEALILYLACLRSGAVYLPL---NTAYTLAELDYFIGDAEPRLVVVASAAREGVATI------AQRH 120
Cdd:PRK07769 77 KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpAEPGHVGRLHAVLDDCTPSAILTTTDSAEGVRKFfrarpaKERP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 121 GAIveTLDA--DGSGSLldlardepadFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTSDDRL 198
Cdd:PRK07769 157 RVI--AVDAvpDEVGAT----------WVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 199 IHALPIFHTHGLFvatnvtllagasMVLLSKFDADEVVSLMPEAtmLMGVPTFYVRLLQ------------SPRFGKEAA 266
Cdd:PRK07769 225 VSWLPFFHDMGLI------------TVLLPALLGHYITFMSPAA--FVRRPGRWIRELArkpggtggtfsaAPNFAFEHA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 A---------------NIRLFISGSAPLLAETHTEF-EARTGH-----AILERYGMTE-------TNMNTS--------- 309
Cdd:PRK07769 291 AarglpkdgeppldlsNVKGLLNGSEPVSPASMRKFnEAFAPYglpptAIKPSYGMAEatlfvstTPMDEEptviyvdrd 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 310 ----------NPYDGKRIA----GTVGLPLPDVRVrvtDPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKTAAEF---- 371
Cdd:PRK07769 371 elnagrfvevPADAPNAVAqvsaGKVGVSEWAVIV---DPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnil 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1037244487 372 -------------TGDGFFISGDLGkIDSDGYVHIVGRGKDLVISGGYNIYPKEVE 414
Cdd:PRK07769 448 ksrlseshaegapDDALWVRTGDYG-VYFDGELYITGRVKDLVIIDGRNHYPQDLE 502
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-488 |
3.84e-23 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 103.10 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPR 101
Cdd:PRK10524 79 TDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDAKPV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 102 LVVVASA-AREGVA-----------TIAQRHGAIVETLD------ADGSGSLLDLArDEPADFVDASRSADDLAA----- 158
Cdd:PRK10524 159 LIVSADAgSRGGKVvpykplldeaiALAQHKPRHVLLVDrglapmARVAGRDVDYA-TLRAQHLGARVPVEWLESnepsy 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTHGNLlsnALTLRdywrvTSDDRlihalpIFHTHG---LFVATNV------------TLLAGAS 223
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGY---AVALA-----TSMDT------IFGGKAgetFFCASDIgwvvghsyivyaPLLAGMA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 224 MVLLskfdadEVVSLMPEA------------TMLMGVPTfYVRLLQsprfgKEAAANIR---------LFISGSaPLLAE 282
Cdd:PRK10524 304 TIMY------EGLPTRPDAgiwwrivekykvNRMFSAPT-AIRVLK-----KQDPALLRkhdlsslraLFLAGE-PLDEP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 283 THTEFEARTGHAILERYGMTETN---MNTSNPYDGKRI-AGTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGP---- 354
Cdd:PRK10524 371 TASWISEALGVPVIDNYWQTETGwpiLAIARGVEDRPTrLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGPlppg 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 355 ----------NVFKGYWR-MPEKTAAEFtgdgffisgDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGV 423
Cdd:PRK10524 451 cmqtvwgdddRFVKTYWSlFGRQVYSTF---------DWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAV 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 424 VESAVIGVPHPDFGEGVTAIVVRKPGAVLD--------EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:PRK10524 522 AEVAVVGVKDALKGQVAVAFVVPKDSDSLAdrearlalEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKL 594
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
50-499 |
8.47e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 101.74 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 50 RPGDRVAVQVEKSAEALILYLACLRSGAVYLPLnTAYTLA----ELDYFIGDAEPRLVVVASAAREGVatiaqrhGAIVE 125
Cdd:PRK12476 90 GPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPL-FAPELPghaeRLDTALRDAEPTVVLTTTAAAEAV-------EGFLR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 126 TLDADGSGSLL---DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLrdYWRVTSDDRLIHA- 201
Cdd:PRK12476 162 NLPRLRRPRVIaidAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQM--ILSIDLLDRNTHGv 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 202 --LPIFHTHGL----FVAtnvtlLAGASMVLLSkfdadevvslmpeatmlmgvPTFYVRLLQ------------------ 257
Cdd:PRK12476 240 swLPLYHDMGLsmigFPA-----VYGGHSTLMS--------------------PTAFVRRPQrwikalsegsrtgrvvta 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 258 SPRFGKEAAA--------------NIRLfISGSAPLLAETHTEFEA--------RTghAILERYGMTETNMNTSN--P-- 311
Cdd:PRK12476 295 APNFAYEWAAqrglpaegddidlsNVVL-IIGSEPVSIDAVTTFNKafapyglpRT--AFKPSYGIAEATLFVATiaPda 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 312 ------YDGKRIAGTVGLPL----PDVRVRVT-------------DPATGLVLPPEQTGMIEIKGPNVFKGYWRMPEKT- 367
Cdd:PRK12476 372 epsvvyLDREQLGAGRAVRVaadaPNAVAHVScgqvarsqwavivDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETe 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 368 ----------------AAEFTGDG-FFISGDLGkIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVES---A 427
Cdd:PRK12476 452 rtfgaklqsrlaegshADGAADDGtWLRTGDLG-VYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRgyvT 530
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 428 VIGVPHPDfGEGVTAIVVRKPGAV-LDEKTIVGALQDRLARYKQPK----RIIFTEDLPRNTMGKVQKNILRQQYAD 499
Cdd:PRK12476 531 AFTVPAED-NERLVIVAERAAGTSrADPAPAIDAIRAAVSRRHGLAvadvRLVPAGAIPRTTSGKLARRACRAQYLD 606
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
28-401 |
2.93e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 100.58 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 W-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGavyLPLNTAY-TLAE--LDYFIGDAEPRLV 103
Cdd:PLN02387 106 WiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQN---ITVVTIYaSLGEeaLCHSLNETEVTTV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGAI--VETLDADGSGSLL-----------------DLARDEPadfVDASR-SADDLAAILYTS 163
Cdd:PLN02387 183 ICDSKQLKKLIDISSQLETVkrVIYMDDEGVDSDSslsgssnwtvssfseveKLGKENP---VDPDLpSPNDIAVIMYTS 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 164 GTTGRSKGAMLTHGNLLSNALTLRDYW-RVTSDDRLIHALPIFHTHGLfVATNVTLLAGAS------MVLL--------- 227
Cdd:PLN02387 260 GSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDVYLAYLPLAHILEL-AAESVMAAVGAAigygspLTLTdtsnkikkg 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 228 SKFDADEvvsLMPeaTMLMGVPTFYVRLLQSPR-----------------------------FGKEAA------------ 266
Cdd:PLN02387 339 TKGDASA---LKP--TLMTAVPAILDRVRDGVRkkvdakgglakklfdiaykrrlaaiegswFGAWGLekllwdalvfkk 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 267 ------ANIRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMN-TSNPYDGKRIaGTVGLPLPDVRVRVTDPATGL 339
Cdd:PLN02387 414 iravlgGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGaTFSEWDDTSV-GRVGPPLPCCYVKLVSWEEGG 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1037244487 340 VL---PPEQTGMIEIKGPNVFKGYWRMPEKTAAEFTGDG----FFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:PLN02387 493 YLisdKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFYTGDIGQFHPDGCLEIIDRKKDIV 561
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
27-382 |
4.66e-22 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 99.45 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TWSYGDAFALSGRIAGALDTLG-IRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd17632 67 TITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAA-----------------------------REGVATIAQRHGAI-----VETLDADGSGSLLDLARDEPADfvdasr 151
Cdd:cd17632 147 SAEHldlaveavleggtpprlvvfdhrpevdahRAALESARERLAAVgipvtTLTLIAVRGRDLPPAPLFRPEP------ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 152 SADDLAAILYTSGTTGRSKGAMLTHGNllsnaltLRDYWRVTS---DDR-----LIHALPIFHTHGLFVATNvTLLAGAS 223
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERL-------VATFWLKVSsiqDIRppasiTLNFMPMSHIAGRISLYG-TLARGGT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 224 MVLLSKFDA----DEVVSLMPeaTMLMGVPTFYVRLLQspRFGKE-----------------AAANIR---------LFI 273
Cdd:cd17632 293 AYFAAASDMstlfDDLALVRP--TELFLVPRVCDMLFQ--RYQAEldrrsvagadaetlaerVKAELRervlggrllAAV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 274 SGSAPLLAETHTEFEARTGHAILERYGMTEtnmntsnpydgkriAGTVGLPLPDVRVRVTD------PATGLVLP--PEQ 345
Cdd:cd17632 369 CGSAPLSAEMKAFMESLLDLDLHDGYGSTE--------------AGAVILDGVIVRPPVLDyklvdvPELGYFRTdrPHP 434
|
410 420 430
....*....|....*....|....*....|....*..
gi 1037244487 346 TGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDL 382
Cdd:cd17632 435 RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDV 471
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
27-400 |
1.01e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 98.76 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 27 TW-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:PLN02861 76 VWlTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAAREGVATIAQRHGAIVETLDADGSGSLLdlaRDEPADFVDAS-------------------RSADDLAAILYTSGTT 166
Cdd:PLN02861 156 QESKISSILSCLPKCSSNLKTIVSFGDVSSE---QKEEAEELGVScfsweefslmgsldcelppKQKTDICTIMYTSGTT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 167 GRSKGAMLTHGNLLSNALTLRDYWRVT-----SDDRLIHALPIFHTHGLfVATNVTLLAGASMVLLS---KFDADEVVSL 238
Cdd:PLN02861 233 GEPKGVILTNRAIIAEVLSTDHLLKVTdrvatEEDSYFSYLPLAHVYDQ-VIETYCISKGASIGFWQgdiRYLMEDVQAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 239 MPeaTMLMGVPTFYVRLL-------------------------------------QSPRFG-------KEA-AANIRLFI 273
Cdd:PLN02861 312 KP--TIFCGVPRVYDRIYtgimqkissggmlrkklfdfaynyklgnlrkglkqeeASPRLDrlvfdkiKEGlGGRVRLLL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 274 SGSAPLLAETHtEFEARTGHAILER-YGMTETN----MNTSNPYDgkrIAGTVGLPLPDVRVRVTD-PATGL-VLPPEQT 346
Cdd:PLN02861 390 SGAAPLPRHVE-EFLRVTSCSVLSQgYGLTESCggcfTSIANVFS---MVGTVGVPMTTIEARLESvPEMGYdALSDVPR 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1037244487 347 GMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDL 400
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNGAMKIIDRKKNI 518
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
25-493 |
2.40e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 98.32 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 25 GQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIG-DAEPRLV 103
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIElSRTPVLV 3822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 104 VVASAAREGVATIAQRHGA------IVETLDADGSgslldlARDEPADFvdasRSADDLAAILYTSGTTGRSKGAMLTHG 177
Cdd:PRK05691 3823 CSAACREQARALLDELGCAnrprllVWEEVQAGEV------ASHNPGIY----SGPDNLAYVIYTSGSTGLPKGVMVEQR 3892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 178 NLLSNALTLRDYWRVTSDDRLIH--------------ALPIFhthGLFVATNVTLLAGASMVLLSKFDADEVvslmpeaT 243
Cdd:PRK05691 3893 GMLNNQLSKVPYLALSEADVIAQtasqsfdisvwqflAAPLF---GARVEIVPNAIAHDPQGLLAHVQAQGI-------T 3962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 244 MLMGVPTFYVRLLQSPRfgkEAAANIR-LFISGSA--PLLAETHTEFEARTGhaILERYGMTETNMNTS-NPYDGKRIAG 319
Cdd:PRK05691 3963 VLESVPSLIQGMLAEDR---QALDGLRwMLPTGEAmpPELARQWLQRYPQIG--LVNAYGPAECSDDVAfFRVDLASTRG 4037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 320 T---VGLPLPDVRVRVTDPATGLVlPPEQTGMIEIKGPNVFKGYWRMPEKTAAEFT-------GDGFFISGDLGKIDSDG 389
Cdd:PRK05691 4038 SylpIGSPTDNNRLYLLDEALELV-PLGAVGELCVAGTGVGRGYVGDPLRTALAFVphpfgapGERLYRTGDLARRRSDG 4116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 390 YVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPD----FGEGVTAIVVRKPGAVLDEktIVGALQDRL 465
Cdd:PRK05691 4117 VLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNgkhlVGYLVPHQTVLAQGALLER--IKQRLRAEL 4194
|
490 500
....*....|....*....|....*...
gi 1037244487 466 ARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:PRK05691 4195 PDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
28-401 |
2.80e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 97.19 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 W-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVA 106
Cdd:PLN02430 76 WkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 107 SAAREGV----ATIAQRHGAIV--------ETLDADGSG-------SLLDLARDEPADFvdASRSADDLAAILYTSGTTG 167
Cdd:PLN02430 156 DKKIKELlepdCKSAKRLKAIVsftsvteeESDKASQIGvktyswiDFLHMGKENPSET--NPPKPLDICTIMYTSGTSG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 168 RSKGAMLTHGNLLSNALTLRDYW-----RVTSDDRLIHALPIFHTHGLFV-------ATNVTLLAGASMVLlskfdADEV 235
Cdd:PLN02430 234 DPKGVVLTHEAVATFVRGVDLFMeqfedKMTHDDVYLSFLPLAHILDRMIeeyffrkGASVGYYHGDLNAL-----RDDL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 236 VSLMPeaTMLMGVPTFYVRL-------LQ--SPR----FG----------------KEAA----------------ANIR 270
Cdd:PLN02430 309 MELKP--TLLAGVPRVFERIhegiqkaLQelNPRrrliFNalykyklawmnrgyshKKASpmadflafrkvkaklgGRLR 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 271 LFISGSAPLLAETHtEFEARTGHA-ILERYGMTETNMNTSNPY-DGKRIAGTVGLPLPDVRVRVTD-PATG---LVLPPE 344
Cdd:PLN02430 387 LLISGGAPLSTEIE-EFLRVTSCAfVVQGYGLTETLGPTTLGFpDEMCMLGTVGAPAVYNELRLEEvPEMGydpLGEPPR 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1037244487 345 qtGMIEIKGPNVFKGYWRMPEKTAaEFTGDGFFISGDLGKIDSDGYVHIVGRGKDLV 401
Cdd:PLN02430 466 --GEICVRGKCLFSGYYKNPELTE-EVMKDGWFHTGDIGEILPNGVLKIIDRKKNLI 519
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
29-495 |
9.86e-20 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 92.51 E-value: 9.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYlplN------TAYTLAELdyfIGDAEPRL 102
Cdd:PRK00174 100 TYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVH---SvvfggfSAEALADR---IIDAGAKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 103 VVVASAAREGVATIA---------------------QRHGAIVETLDadgsG------SLLDLARDE-PADFVDAsrsaD 154
Cdd:PRK00174 174 VITADEGVRGGKPIPlkanvdealancpsvekvivvRRTGGDVDWVE----GrdlwwhELVAGASDEcEPEPMDA----E 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 155 DLAAILYTSGTTGRSKGAM-LTHGNLLSNALT------LRD---YWrVTSDdrlihalpifhthglfvatnVTLLAGASM 224
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLhTTGGYLVYAAMTmkyvfdYKDgdvYW-CTAD--------------------VGWVTGHSY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 225 VLLSkfdadevvSLMPEATMLM--GVPT------------------FY-----VRLLQspRFGKEAAAN-----IRLFIS 274
Cdd:PRK00174 305 IVYG--------PLANGATTLMfeGVPNypdpgrfwevidkhkvtiFYtaptaIRALM--KEGDEHPKKydlssLRLLGS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 275 GSAPLLAET-----HTEFEARTghAILERYGMTET--NMNTSNP--YDGKriAGTVGLPLPDVRVRVTDpATGLVLPPEQ 345
Cdd:PRK00174 375 VGEPINPEAwewyyKVVGGERC--PIVDTWWQTETggIMITPLPgaTPLK--PGSATRPLPGIQPAVVD-EEGNPLEGGE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 346 TGMIEIKGP------NVF-------KGYW-RMPEKTaaeFTGDGffisgdlGKIDSDGYVHIVGRGKDLVISGGYNIYPK 411
Cdd:PRK00174 450 GGNLVIKDPwpgmmrTIYgdherfvKTYFsTFKGMY---FTGDG-------ARRDEDGYYWITGRVDDVLNVSGHRLGTA 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 412 EVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKtIVGALQDRLAR----YKQPKRIIFTEDLPRNTMGK 487
Cdd:PRK00174 520 EIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDE-LRKELRNWVRKeigpIAKPDVIQFAPGLPKTRSGK 598
|
....*...
gi 1037244487 488 VQKNILRQ 495
Cdd:PRK00174 599 IMRRILRK 606
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
39-495 |
9.98e-20 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 92.65 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAAREGVATIAQ 118
Cdd:PLN02654 132 QLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAVKRGPKTINL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 119 RH---GAIVET----------LDADGSGSL---------------LDLARDEPAD----FVDAsrsaDDLAAILYTSGTT 166
Cdd:PLN02654 212 KDivdAALDESakngvsvgicLTYENQLAMkredtkwqegrdvwwQDVVPNYPTKceveWVDA----EDPLFLLYTSGST 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 167 GRSKGAMLTHGN-LLSNALTLRD---------YWrVTSDDRLIHAlpifHTHglfvATNVTLLAGASMVLLskfdadEVV 236
Cdd:PLN02654 288 GKPKGVLHTTGGyMVYTATTFKYafdykptdvYW-CTADCGWITG----HSY----VTYGPMLNGATVLVF------EGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 237 SLMPEA------------TMLMGVPTFYVRLLqspRFGKEAAA-----NIRLFISGSAPLLAETHTEFEARTGHA---IL 296
Cdd:PLN02654 353 PNYPDSgrcwdivdkykvTIFYTAPTLVRSLM---RDGDEYVTrhsrkSLRVLGSVGEPINPSAWRWFFNVVGDSrcpIS 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 297 ERYGMTETN--MNTSNPYDGKRIAGTVGLPLPDVRVRVTDpATGLVLPPEQTGMIEIKG--PNVFKGYWRMPEKTAAEFT 372
Cdd:PLN02654 430 DTWWQTETGgfMITPLPGAWPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKKswPGAFRTLYGDHERYETTYF 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 373 G--DGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGA 450
Cdd:PLN02654 509 KpfAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGV 588
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1037244487 451 VLDE---KTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:PLN02654 589 PYSEelrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
112-496 |
2.57e-19 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 90.98 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 112 GVATIAQrHGAIVETLDA-DGSGSLLDLA------RDEPADFVDASrsadDLAAILYTSGTTGRSKGAMLTHGNLLSNAL 184
Cdd:PRK05851 108 GVRTVLS-HGSHLERLRAvDSSVTVHDLAtaahtnRSASLTPPDSG----GPAVLQGTAGSTGTPRTAILSPGAVLSNLR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 185 TLRDYWRVTSD-DRLIHALPIFHTHGL-FVATNVtlLAGASMVL--LSKFDADEV--VSLMPE--ATMLMGvPTFYVRLL 256
Cdd:PRK05851 183 GLNARVGLDAAtDVGCSWLPLYHDMGLaFLLTAA--LAGAPLWLapTTAFSASPFrwLSWLSDsrATLTAA-PNFAYNLI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 257 qsprfGKEAA-------ANIRLFISGSAPLLAETHTEFE---ARTGH---AILERYGMTETN--MNTSNPYDGKRIA--- 318
Cdd:PRK05851 260 -----GKYARrvsdvdlGALRVALNGGEPVDCDGFERFAtamAPFGFdagAAAPSYGLAESTcaVTVPVPGIGLRVDevt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 319 ----------GTVGLPLPDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYwrmpeKTAAEFTGDGFFISGDLGKIDSD 388
Cdd:PRK05851 335 tddgsgarrhAVLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY-----LGQAPIDPDDWFPTGDLGYLVDG 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 389 GYVhIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVphpdfGEGVTAIvvrKPGAVL-------DEKTIVGAL 461
Cdd:PRK05851 410 GLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAV-----GTGEGSA---RPGLVIaaefrgpDEAGARSEV 480
|
410 420 430
....*....|....*....|....*....|....*....
gi 1037244487 462 QDRLARY--KQPKRIIFTE--DLPRNTMGKVQKNILRQQ 496
Cdd:PRK05851 481 VQRVASEcgVVPSDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
50-488 |
5.44e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.94 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 50 RPGDRVAVQVEKSAEALILYLACLRSGAVYLPlntaytlaeldyfIGDAEPRlvvvaSAAREgVATIAQRHGAIVETLD- 128
Cdd:PRK08308 30 AAGNRFAVCLKDPFDIITLVFFLKEKGASVLP-------------IHPDTPK-----EAAIR-MAKRAGCHGLLYGESDf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 129 --------ADGSGSLLDlardepadfvdasrsaddlaailYTSGTTGRSKgamlthgnllsnalTLRDYWrvTSDDRLIH 200
Cdd:PRK08308 91 tkleavnyLAEEPSLLQ-----------------------YSSGTTGEPK--------------LIRRSW--TEIDREIE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 201 ----------------ALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPEAT--MLMGVPTFY---VRLLQ-S 258
Cdd:PRK08308 132 aynealnceqdetpivACPVTHSYGLICGVLAALTRGSKPVIITNKNPKFALNILRNTPqhILYAVPLMLhilGRLLPgT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 259 PRFGkeaaaniRLFISGsAPLLAETHTEFEARTGHaILERYGMTET-----NMNTSNPYDgkriagtVGLPLPDVRVRvt 333
Cdd:PRK08308 212 FQFH-------AVMTSG-TPLPEAWFYKLRERTTY-MMQQYGCSEAgcvsiCPDMKSHLD-------LGNPLPHVSVS-- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 334 dpaTGLvlPPEQTGMIEIKgpnvfkgywrmpektaaefTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEV 413
Cdd:PRK08308 274 ---AGS--DENAPEEIVVK-------------------MGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEV 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1037244487 414 ESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEktIVGALQDRLARYKQPKRIIFTEDLPRNTMGKV 488
Cdd:PRK08308 330 EDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQ--LREWCIQHLAPYQVPHEIESVTEIPKNANGKV 402
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
412-487 |
1.33e-18 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 79.90 E-value: 1.33e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037244487 412 EVESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDEKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGK 487
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
29-435 |
2.91e-16 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 81.61 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 29 SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAE--------- 99
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEvsivfveek 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 100 --PRLVVVASAAREGVATI-------------AQRHGAIVETLDAD---GSGSLLDLARDEPADfvdasrsaddLAAILY 161
Cdd:PLN02614 161 kiSELFKTCPNSTEYMKTVvsfggvsreqkeeAETFGLVIYAWDEFlklGEGKQYDLPIKKKSD----------ICTIMY 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 162 TSGTTGRSKGAMLTHGNLLSNALTLRDYWR-----VTSDDRLIHALPIFHTHGLfVATNVTLLAGASMVLLS---KFDAD 233
Cdd:PLN02614 231 TSGTTGDPKGVMISNESIVTLIAGVIRLLKsanaaLTVKDVYLSYLPLAHIFDR-VIEECFIQHGAAIGFWRgdvKLLIE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 234 EVVSLMPeaTMLMGVPTFYVRL---LQ----------------------------------SPRFGKEA--------AAN 268
Cdd:PLN02614 310 DLGELKP--TIFCAVPRVLDRVysgLQkklsdggflkkfvfdsafsykfgnmkkgqshveaSPLCDKLVfnkvkqglGGN 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 269 IRLFISGSAPLLAETHTEFEARTGHAILERYGMTETNMNTSNPY-DGKRIAGTVGLPLPDVRVRVTD-PATGL-VLPPEQ 345
Cdd:PLN02614 388 VRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLpDELDMLGTVGPPVPNVDIRLESvPEMEYdALASTP 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 346 TGMIEIKGPNVFKGYWRMPEKTAAEFTgDGFFISGDLGKIDSDGYVHIVGRGKDLV-ISGGYNIYPKEVE---SEIDRIE 421
Cdd:PLN02614 468 RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIEniyGEVQAVD 546
|
490 500
....*....|....*....|
gi 1037244487 422 GV------VESAVIGVPHPD 435
Cdd:PLN02614 547 SVwvygnsFESFLVAIANPN 566
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
19-493 |
1.66e-13 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 72.50 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 19 FMRTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYtlaeldyfigdA 98
Cdd:cd17654 8 IDQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPAS-----------P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 99 EPRLVVVASAAreGVATIAQRHGAIVETLDADGSGSLLDLARDEPadfvdasrsaddLAAILYTSGTTGRSKGAMLTHGN 178
Cdd:cd17654 77 EQRSLTVMKKC--HVSYLLQNKELDNAPLSFTPEHRHFNIRTDEC------------LAYVIHTSGTTGTPKIVAVPHKC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 179 LLSNALTLRDYWRVTSDDRLIHAlPIFHTHGLFVATNVTLLAGASM--------VLLSKFdaDEVVSLMPEATMLMGVPT 250
Cdd:cd17654 143 ILPNIQHFRSLFNITSEDILFLT-SPLTFDPSVVEIFLSLSSGATLlivptsvkVLPSKL--ADILFKRHRITVLQATPT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 251 FYVRLLQS--PRFGKEAAANIRLFISGSAPL----LAETHTEFEARTghAILERYGMTETNMnTSNPYDGKRIAGTV--G 322
Cdd:cd17654 220 LFRRFGSQsiKSTVLSATSSLRVLALGGEPFpslvILSSWRGKGNRT--RIFNIYGITEVSC-WALAYKVPEEDSPVqlG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 323 LPLPDVRVRVTDPATGlvlppEQTGMIEIKGPNvfKGYWRMPEKTAAEFTgdgFFISGDLGKIdSDGYVHIVGRGKDLVI 402
Cdd:cd17654 297 SPLLGTVIEVRDQNGS-----EGTGQVFLGGLN--RVCILDDEVTVPKGT---MRATGDFVTV-KDGELFFLGRKDSQIK 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 403 SGGYNIYPKEVESEIDRIEGVVESAVIGVPHpdfgEGVTAIVVRKPGAVLDEKTIVgalQDRLARYKQPKRIIFTEDLPR 482
Cdd:cd17654 366 RRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLIAFIVGESSSSRIHKELQ---LTLLSSHAIPDTFVQIDKLPL 438
|
490
....*....|.
gi 1037244487 483 NTMGKVQKNIL 493
Cdd:cd17654 439 TSHGKVDKSEL 449
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
137-420 |
1.94e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 72.83 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 137 DLARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALTLRDyWRVT---SDDRLIHALPIFHthgLFVA 213
Cdd:PTZ00342 287 DMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCK-HSIFkkyNPKTHLSYLPISH---IYER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 214 TNV--TLLAGASMVLLSK----FDADEVVSlmpEATMLMGVPTFYVRLLQS--------PRFGK---------------- 263
Cdd:PTZ00342 363 VIAylSFMLGGTINIWSKdinyFSKDIYNS---KGNILAGVPKVFNRIYTNimteinnlPPLKRflvkkilslrksnnng 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 264 ------EAAANI------------RLFISGSAPLLAETHTEFEARTGHAILERYGMTETN----MNTSNPYDGKRIAGTV 321
Cdd:PTZ00342 440 gfskflEGITHIsskikdkvnpnlEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTgpifVQHADDNNTESIGGPI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 322 GlplPDVRVRV----TDPATGLvlPPEqtGMIEIKGPNVFKGYWRMPEKTAAEFTGDGFFISGDLGKIDSDGYVHIVGRG 397
Cdd:PTZ00342 520 S---PNTKYKVrtweTYKATDT--LPK--GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRS 592
|
330 340 350
....*....|....*....|....*....|..
gi 1037244487 398 KDLV-ISGG-Y-------NIYpkeveSEIDRI 420
Cdd:PTZ00342 593 KGLVkLSQGeYietdmlnNLY-----SQISFI 619
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
39-504 |
6.68e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 71.26 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 39 RIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVVASAAREGVATI-- 116
Cdd:PLN03052 220 RVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQDVIVRGGKSIpl 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 117 ------AQRHGAIVetLDADGSGSLLDL---------------ARDEPADFVDASRSADDLAAILYTSGTTGRSKGAMLT 175
Cdd:PLN03052 300 ysrvveAKAPKAIV--LPADGKSVRVKLregdmswddflaranGLRRPDEYKAVEQPVEAFTNILFSSGTTGEPKAIPWT 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 176 HGNLLSNAltlRDYWrVTSDDRlihalpifhtHGLFVA--TNV-----------TLLAGASMVLLS---------KFDAD 233
Cdd:PLN03052 378 QLTPLRAA---ADAW-AHLDIR----------KGDIVCwpTNLgwmmgpwlvyaSLLNGATLALYNgsplgrgfaKFVQD 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 234 EVVslmpeaTMLMGVPTFyVRLLQSprfgkeaaanirlfiSGSAPLLAETHTEFEARTGHA-----------------IL 296
Cdd:PLN03052 444 AKV------TMLGTVPSI-VKTWKN---------------TNCMAGLDWSSIRCFGSTGEAssvddylwlmsragykpII 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 297 ERYGMTE--------------TNMNTSNPYDGKR--IAGTVGLPLPDvrvrvTDPATG-LVLPPEQTG----MIEIKGPN 355
Cdd:PLN03052 502 EYCGGTElgggfvtgsllqpqAFAAFSTPAMGCKlfILDDSGNPYPD-----DAPCTGeLALFPLMFGasstLLNADHYK 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 356 V-FKGywrMPEktaaeFTGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYniypKEVESEIDRI-----EGVVESAVI 429
Cdd:PLN03052 577 VyFKG---MPV-----FNGKILRRHGDIFERTSGGYYRAHGRADDTMNLGGI----KVSSVEIERVcnaadESVLETAAI 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 430 GVPHPDFG-EGVTAIVVRK--PGAVLD----EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQQYADLYT 502
Cdd:PLN03052 645 GVPPPGGGpEQLVIAAVLKdpPGSNPDlnelKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQLAQELS 724
|
..
gi 1037244487 503 RT 504
Cdd:PLN03052 725 RS 726
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
159-493 |
6.88e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 70.93 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 159 ILYTSGTTGRSKGAMLTHGnllSNALTLRDYWR--VTSDDRLIHalpIFHT-------HGLFVATnvtLLAGASMVLlsk 229
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNG---PHLVGLKYYWRsiIEKDIPTVV---FSHSsigwvsfHGFLYGS---LSLGNTFVM--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 230 FDADEVVSLMPE-----------ATMLMGVPTFYVRLLQSPRFG-----KEAAANIRLFISGSAPLLAETHTEFEARTGH 293
Cdd:PTZ00237 327 FEGGIIKNKHIEddlwntiekhkVTHTLTLPKTIRYLIKTDPEAtiirsKYDLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 294 AILERYGMTETNM-------NTSNPYDgkriagTVGLPLPDVRVRVTDPaTGLVLPPEQTGMIEIKGPnvfkgywrMPEK 366
Cdd:PTZ00237 407 KSSRGYGQTEIGItylycygHINIPYN------ATGVPSIFIKPSILSE-DGKELNVNEIGEVAFKLP--------MPPS 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 367 TAAEFTGD------------GFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIGVPHP 434
Cdd:PTZ00237 472 FATTFYKNdekfkqlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037244487 435 DFGEGVTAIVVRKPG---AVLD----EKTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:PTZ00237 552 DCYNVPIGLLVLKQDqsnQSIDlnklKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
21-495 |
1.16e-12 |
|
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: 70.38 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 21 RTGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL-AELDYFiGDAE 99
Cdd:cd05943 92 EDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVpGVLDRF-GQIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 100 PRLVVVASAA---------REGVATIAQRHGAIVET--LDADGSGSLLDLARDEP----ADFVDASRSA---------DD 155
Cdd:cd05943 171 PKVLFAVDAYtyngkrhdvREKVAELVKGLPSLLAVvvVPYTVAAGQPDLSKIAKaltlEDFLATGAAGelefeplpfDH 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 156 LAAILYTSGTTGRSKGAMLTHGNLLSNALT-LRDYWRVTSDDRLIHalpiFHTHGL----FVATNvtLLAGASMVLL--S 228
Cdd:cd05943 251 PLYILYSSGTTGLPKCIVHGAGGTLLQHLKeHILHCDLRPGDRLFY----YTTCGWmmwnWLVSG--LAVGATIVLYdgS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 229 KFDADEVVslMPE------ATMLMGVPTFYVRLLqspRFGKEAAAN-----IRLFISGSAPLLAET----HTEFEARtgh 293
Cdd:cd05943 325 PFYPDTNA--LWDladeegITVFGTSAKYLDALE---KAGLKPAEThdlssLRTILSTGSPLKPESfdyvYDHIKPD--- 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 294 AILERY-GMTETN-----MNTSNP-YDG---KRIAGtvglplpdVRVRVTDPATGLVlpPEQTGMIEIKGPnvFK----G 359
Cdd:cd05943 397 VLLASIsGGTDIIscfvgGNPLLPvYRGeiqCRGLG--------MAVEAFDEEGKPV--WGEKGELVCTKP--FPsmpvG 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 360 YWRMPEKT---AAEF-TGDGFFISGDLGKIDSDGYVHIVGRgKDLVIS-GGYNIYPKEVESEIDRIEGVVESAVIGVPHP 434
Cdd:cd05943 465 FWNDPDGSryrAAYFaKYPGVWAHGDWIEITPRGGVVILGR-SDGTLNpGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWK 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1037244487 435 DFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNILRQ 495
Cdd:cd05943 544 DGDERVILFVKLREGVELDDelrKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVKK 607
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
137-465 |
3.78e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 64.79 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 137 DLARDEPADFVDASRSadDLAAILYTSGTTGRSKGAMLTHGNLLSNA-LTLRDYW--RVTSDDRLIHALPifhtHGLFVA 213
Cdd:COG1541 68 DLRDNYPFGLFAVPLE--EIVRIHASSGTTGKPTVVGYTRKDLDRWAeLFARSLRaaGVRPGDRVQNAFG----YGLFTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 214 TNVTLLA----GASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLqspRFGKE-----AAANIRLFISGSAPLLAE 282
Cdd:COG1541 142 GLGLHYGaerlGATVIPAGGGNTERQLRLMQDfgPTVLVGTPSYLLYLA---EVAEEegidpRDLSLKKGIFGGEPWSEE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 283 THTEFEARTGHAILERYGMTETNMNTSN--PYDGkriagtvGLPLP--DVRVRVTDPATGLVLPPEQTGmiEIkgpnVFk 358
Cdd:COG1541 219 MRKEIEERWGIKAYDIYGLTEVGPGVAYecEAQD-------GLHIWedHFLVEIIDPETGEPVPEGEEG--EL----VV- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 359 gywrmpekTAaeFTGDGF----FISGDLGKIDSD----GYVH-----IVGRGKDLVISGGYNIYPKEVESEIDRIEGVVE 425
Cdd:COG1541 285 --------TT--LTKEAMplirYRTGDLTRLLPEpcpcGRTHprigrILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1037244487 426 SAVIGVPHPDFGEGVTAIVVRKPGAVLD--EKTIVGALQDRL 465
Cdd:COG1541 355 EYQIVVDREGGLDELTVRVELAPGASLEalAEAIAAALKAVL 396
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
22-493 |
8.09e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 61.35 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 22 TGSGQTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTL-AELDYFiGDAEP 100
Cdd:PRK03584 109 DGPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGVqGVLDRF-GQIEP 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 101 RlVVVASAA----------REGVATIAQ-----RHGAIVETLDADGSGSLLDLARDEpADFVDASRSA---------DDL 156
Cdd:PRK03584 188 K-VLIAVDGyryggkafdrRAKVAELRAalpslEHVVVVPYLGPAAAAAALPGALLW-EDFLAPAEAAelefepvpfDHP 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 157 AAILYTSGTTGRSKGAMLTHGNLLSNAL-TLRDYWRVTSDDRLIhalpIFHTHG-----LFVATnvtLLAGASMVLlskF 230
Cdd:PRK03584 266 LWILYSSGTTGLPKCIVHGHGGILLEHLkELGLHCDLGPGDRFF----WYTTCGwmmwnWLVSG---LLVGATLVL---Y 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 231 DadevvslmpeatmlmGVPTFyvrllqsPRFGK----EAAANIRLFISGSAPLLAETHTEFEARTGHAiLERYgmtetnm 306
Cdd:PRK03584 336 D---------------GSPFY-------PDPNVlwdlAAEEGVTVFGTSAKYLDACEKAGLVPGETHD-LSAL------- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 307 ntsnpydgkRIAGTVGLPLP---------DVRVRV--------TDPATGLVL--P--PEQTGMIEIKG------------ 353
Cdd:PRK03584 386 ---------RTIGSTGSPLPpegfdwvyeHVKADVwlasisggTDICSCFVGgnPllPVYRGEIQCRGlgmaveawdedg 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 354 ----------------PNVFKGYWRMPEKT---AAEF-TGDGFFISGDLGKIDSDGYVHIVGRGkDLVIS-GGYNIYPKE 412
Cdd:PRK03584 457 rpvvgevgelvctkpfPSMPLGFWNDPDGSryrDAYFdTFPGVWRHGDWIEITEHGGVVIYGRS-DATLNrGGVRIGTAE 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 413 VESEIDRIEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVLDE---KTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQ 489
Cdd:PRK03584 536 IYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDalrARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
....*...
gi 1037244487 490 ----KNIL 493
Cdd:PRK03584 616 elpvKKLL 623
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
48-464 |
2.20e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 60.12 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 48 GIRPGDRVAVQVEKSAEALILYLACLRSGA--VYLP----LNTAYTLAELDYFIGDAEPrlvvvASAAREGVATIAQRHG 121
Cdd:PRK07868 493 GVRQGDRVGVLMETRPSALVAIAALSRLGAvaVLMPpdtdLAAAVRLGGVTEIITDPTN-----LEAARQLPGRVLVLGG 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 122 AIVETLDADGSGSLLDLARDEPaDFVDASR-------SADDLAAILYtSGTTGRSKGAMLTHGNLLSNALTLRDYWRVTS 194
Cdd:PRK07868 568 GESRDLDLPDDADVIDMEKIDP-DAVELPGwyrpnpgLARDLAFIAF-STAGGELVAKQITNYRWALSAFGTASAAALDR 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 195 DDRLIHALPIFHTHGLFVATNVTLLAGASMVLLSKFDADEVVSLMPE--ATMLMGVPTFYVRLLQSPRFGKEAAANIRLF 272
Cdd:PRK07868 646 RDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQEVRQygVTVVSYTWAMLREVVDDPAFVLHGNHPVRLF 725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 273 I-SGSAPLLAETHTE-FE-ARtghaILERYGMTETNMNTSNPYDGKriAGTVGLPLP---DVRVRVTDPATGLVLPPEQt 346
Cdd:PRK07868 726 IgSGMPTGLWERVVEaFApAH----VVEFFATTDGQAVLANVSGAK--IGSKGRPLPgagRVELAAYDPEHDLILEDDR- 798
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 347 GMIEIKGPN---VFKGYWRMPEKTAAEF------TGDGFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEI 417
Cdd:PRK07868 799 GFVRRAEVNevgVLLARARGPIDPTASVkrgvfaPADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDAL 878
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1037244487 418 DRIEGVVESAVIGVPHPDFGEGVTAIVVRkPGAVLDEKTIVGALQDR 464
Cdd:PRK07868 879 GRIGGVDLAVTYGVEVGGRQLAVAAVTLR-PGAAITAADLTEALASL 924
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
26-493 |
3.27e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 46.36 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 26 QTWSYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPLNTAYTLAELDYFIGDAEPRLVVV 105
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 106 ASAAregvatiaqrhGAIVetldadgsgslldlardepadfvdasrSADDLAAILYTSGTTGRSKGAMLTHGNLLSNALT 185
Cdd:cd17647 99 IRAA-----------GVVV---------------------------GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 186 LRDYWRVTSDDRLIHALPIFH---THGLFVAtnvtLLAGASMVL---------------LSKFDAdEVVSLMPEATMLM- 246
Cdd:cd17647 141 MAKRFNLSENDKFTMLSGIAHdpiQRDMFTP----LFLGAQLLVptqddigtpgrlaewMAKYGA-TVTHLTPAMGQLLt 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 247 -GVPTFYVRLLQSPRFGKEAAANIRLFISGSAP------LLAETHTE-----FEARTGHA-----------ILERYGMTE 303
Cdd:cd17647 216 aQATTPFPKLHHAFFVGDILTKRDCLRLQTLAEnvrivnMYGTTETQravsyFEVPSRSSdptflknlkdvMPAGRGMLN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 304 TNMNTSNPYDGKRIA--GTVGlplpDVRVRVTDPATGLVLPPEQTGMIEIKGPNVFKGYW-------RMPEKTAAEFTGD 374
Cdd:cd17647 296 VQLLVVNRNDRTQICgiGEVG----EIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHWnyldkdnNEPWRQFWLGPRD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 375 GFFISGDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDRIEGVVESAVIG--------------VPHPDFGEGV 440
Cdd:cd17647 372 RLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrrdkdeeptlvsyiVPRFDKPDDE 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1037244487 441 TAIVVRKPGAVLDE-------------KTIVGALQDRLARYKQPKRIIFTEDLPRNTMGKVQKNIL 493
Cdd:cd17647 452 SFAQEDVPKEVSTDpivkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
380-502 |
2.20e-04 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 43.65 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 380 GDLGKIDSDGYVHIVGRGKDLVISGGYNIYPKEVESEIDR-IEGVVESAVIGVPHPDFGEGVTAIVVRKPGAVL-----D 453
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPELLVIFLVLGEEKKgfdqaR 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1037244487 454 EKTIVGALQDRLARYKQP----KRIIFTEDLPRNTMGKVQKNILRQQYADLYT 502
Cdd:PLN03051 442 PEALQKKFQEAIQTNLNPlfkvSRVKIVPELPRNASNKLLRRVLRDQLKKELS 494
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
28-116 |
1.05e-03 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 41.76 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1037244487 28 W-SYGDAFALSGRIAGALDTLGIRPGDRVAVQVEKSAEALILYLACLRSGAVYLPL----NTAYTLaeLDYFIgdaeprl 102
Cdd:PTZ00297 457 WlTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLvgkgSTMRTL--IDEHK------- 527
|
90
....*....|....
gi 1037244487 103 VVVASAAREGVATI 116
Cdd:PTZ00297 528 IKVVFADRNSVAAI 541
|
|
| |
