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Conserved domains on  [gi|1517851394|gb|ROZ52336|]
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carboxylesterase/lipase family protein [Rhodococcus sp. WS1]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10006294)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate, and lipase, which hydrolyzes triglycerides into diglycerides and subsequently into monoglycerides and free fatty acids

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0052689|GO:0016298
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
12-511 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


:

Pssm-ID: 441873  Cd Length: 500  Bit Score: 567.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  12 DGTLVIRARGGEARGYPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQGQSPAVPIDRAfKIDED 91
Cdd:COG2272    10 AAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGGPA-PGSED 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  92 CLSINVWAPRP-DGTPRPVMVWIHGGAYCLGSAAQTIYDGRHLAETGdVVLVSFNYRVGALGFLDLSGFSTADPVFESNC 170
Cdd:COG2272    89 CLYLNVWTPALaAGAKLPVMVWIHGGGFVSGSGSEPLYDGAALARRG-VVVVTINYRLGALGFLALPALSGESYGASGNY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 171 GLRDQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQSPPATSVYGAERAKTVAERFLEL 250
Cdd:COG2272   168 GLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 251 LSIDPEDAGDLLTTDLELLVKASDDLVNeiptRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRIPLIIGSNKDEASIFK 330
Cdd:COG2272   248 LGVAPATLAALRALPAEELLAAQAALAA----EGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 331 FMKSPLMPVSAQSVEAMLQLLADDHPDisatklaEIMSAYPDHAKPSGALALSRDAAFRMPTLWIADAHCR-HSPTWVYR 409
Cdd:COG2272   324 ALLGDLGPLTAADYRAALRRRFGDDAD-------EVLAAYPAASPAEALAALATDRVFRCPARRLAEAHAAaGAPVYLYR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 410 FDHATPMLKAARIGAGHATELPYVFGNFgtlnvDPTFWLGGRKAAMEVAGRIQRRWLAFARHAVPAAlDGSKHWAPYEEE 489
Cdd:COG2272   397 FDWRSPPLRGFGLGAFHGAELPFVFGNL-----DAPALTGLTPADRALSDQMQAYWVNFARTGDPNG-PGLPEWPAYDPE 470
                         490       500
                  ....*....|....*....|..
gi 1517851394 490 RRSTLLIDSADTLVSDPDHGLR 511
Cdd:COG2272   471 DRAVMVFDAEPRVVNDPDAEER 492
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
12-511 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 567.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  12 DGTLVIRARGGEARGYPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQGQSPAVPIDRAfKIDED 91
Cdd:COG2272    10 AAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGGPA-PGSED 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  92 CLSINVWAPRP-DGTPRPVMVWIHGGAYCLGSAAQTIYDGRHLAETGdVVLVSFNYRVGALGFLDLSGFSTADPVFESNC 170
Cdd:COG2272    89 CLYLNVWTPALaAGAKLPVMVWIHGGGFVSGSGSEPLYDGAALARRG-VVVVTINYRLGALGFLALPALSGESYGASGNY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 171 GLRDQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQSPPATSVYGAERAKTVAERFLEL 250
Cdd:COG2272   168 GLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 251 LSIDPEDAGDLLTTDLELLVKASDDLVNeiptRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRIPLIIGSNKDEASIFK 330
Cdd:COG2272   248 LGVAPATLAALRALPAEELLAAQAALAA----EGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 331 FMKSPLMPVSAQSVEAMLQLLADDHPDisatklaEIMSAYPDHAKPSGALALSRDAAFRMPTLWIADAHCR-HSPTWVYR 409
Cdd:COG2272   324 ALLGDLGPLTAADYRAALRRRFGDDAD-------EVLAAYPAASPAEALAALATDRVFRCPARRLAEAHAAaGAPVYLYR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 410 FDHATPMLKAARIGAGHATELPYVFGNFgtlnvDPTFWLGGRKAAMEVAGRIQRRWLAFARHAVPAAlDGSKHWAPYEEE 489
Cdd:COG2272   397 FDWRSPPLRGFGLGAFHGAELPFVFGNL-----DAPALTGLTPADRALSDQMQAYWVNFARTGDPNG-PGLPEWPAYDPE 470
                         490       500
                  ....*....|....*....|..
gi 1517851394 490 RRSTLLIDSADTLVSDPDHGLR 511
Cdd:COG2272   471 DRAVMVFDAEPRVVNDPDAEER 492
COesterase pfam00135
Carboxylesterase family;
14-497 1.34e-131

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 392.06  E-value: 1.34e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  14 TLVIRARGGEARG-----YPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQGQSPAVPIDRAFKI 88
Cdd:pfam00135   2 SPVVTTSLGRVRGkrlkvDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSGLEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  89 DEDCLSINVWAPRPD---GTPRPVMVWIHGGAYCLGSAAQtiYDGRHLAETGDVVLVSFNYRVGALGFLdlsgfSTADPV 165
Cdd:pfam00135  82 SEDCLYLNVYTPKELkenKNKLPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFL-----STGDDE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 166 FESNCGLRDQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQSPPATSVYG-AERAKTVA 244
Cdd:pfam00135 155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAiQSNARQRA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 245 ERFLELLSIDPEDAGdllttdleLLV-----KASDDLV----NEIPTRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRI 315
Cdd:pfam00135 235 KELAKLVGCPTSDSA--------ELVeclrsKPAEELLdaqlKLLVYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKV 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 316 PLIIGSNKDEASIF--KFMKSPLMP-------VSAQSVEAMLQLLADDHPDISATKLAEIMSAYPDHAKPS---GALALS 383
Cdd:pfam00135 307 PLLIGVTKDEGLLFaaYILDNVDILkaleeklLRSLLIDLLYLLLVDLPEEISAALREEYLDWGDRDDPETsrrALVELL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 384 RDAAFRMPTLWIADAH-CRHSPTWVYRFDHATPMLKA-ARIGAGHATELPYVFGN-FGTLNVDptfwlggRKAAMEVAGR 460
Cdd:pfam00135 387 TDYLFNCPVIRFADLHaSRGTPVYMYSFDYRGSSLRYpKWVGVDHGDELPYVFGTpFVGALLF-------TEEDEKLSRK 459
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1517851394 461 IQRRWLAFARHAVPAALDGSKHWAPYEEERRSTLLID 497
Cdd:pfam00135 460 MMTYWTNFAKTGNPNGPEGLPKWPPYTDENGQYLSID 496
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
21-505 4.10e-115

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 349.32  E-value: 4.10e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  21 GGEARGYPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQgqsPAVPIDRAF----KIDEDCLSIN 96
Cdd:cd00312     6 NGKVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQ---WDQLGGGLWnaklPGSEDCLYLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  97 VWAPRPD--GTPRPVMVWIHGGAYCLGSAaqTIYDGRHLAETGD-VVLVSFNYRVGALGFLdlsgfSTADPVFESNCGLR 173
Cdd:cd00312    83 VYTPKNTkpGNSLPVMVWIHGGGFMFGSG--SLYPGDGLAREGDnVIVVSINYRLGVLGFL-----STGDIELPGNYGLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 174 DQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQS-----PPATSVYGAERAKtvaeRFL 248
Cdd:cd00312   156 DQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSgsalsPWAIQENARGRAK----RLA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 249 ELLSIDPEDAgdlLTTDLELLVKASDDLV----NEIPTRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRIPLIIGSNKD 324
Cdd:cd00312   232 RLLGCNDTSS---AELLDCLRSKSAEELLdatrKLLLFSYSPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 325 EASIFKFM----KSPLMPVSAQSVEAMLQLLADDHPDISATKlaeIMSAYPDHAKPSGAL--ALSR---DAAFRMPTLWI 395
Cdd:cd00312   309 EGGYFAAMllnfDAKLIIETNDRWLELLPYLLFYADDALADK---VLEKYPGDVDDSVESrkNLSDmltDLLFKCPARYF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 396 ADAHCRH--SPTWVYRFDHATPMLKAARI---GAGHATELPYVFGNfgtlnvdPTFWLGGRKAAMEVAGRIQRRWLAFAR 470
Cdd:cd00312   386 LAQHRKAggSPVYAYVFDHRSSLSVGRWPpwlGTVHGDEIFFVFGN-------PLLKEGLREEEEKLSRTMMKYWANFAK 458
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1517851394 471 HAVPAALDGSKHWAPYEEERRSTLLIDSADTLVSD 505
Cdd:cd00312   459 TGNPNTEGNLVVWPAYTSESEKYLDINIEGTEIKQ 493
 
Name Accession Description Interval E-value
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
12-511 0e+00

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 567.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  12 DGTLVIRARGGEARGYPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQGQSPAVPIDRAfKIDED 91
Cdd:COG2272    10 AAAPVVRTEAGRVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGGPA-PGSED 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  92 CLSINVWAPRP-DGTPRPVMVWIHGGAYCLGSAAQTIYDGRHLAETGdVVLVSFNYRVGALGFLDLSGFSTADPVFESNC 170
Cdd:COG2272    89 CLYLNVWTPALaAGAKLPVMVWIHGGGFVSGSGSEPLYDGAALARRG-VVVVTINYRLGALGFLALPALSGESYGASGNY 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 171 GLRDQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQSPPATSVYGAERAKTVAERFLEL 250
Cdd:COG2272   168 GLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTLAEAEAVGAAFAAA 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 251 LSIDPEDAGDLLTTDLELLVKASDDLVNeiptRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRIPLIIGSNKDEASIFK 330
Cdd:COG2272   248 LGVAPATLAALRALPAEELLAAQAALAA----EGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEGRLFA 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 331 FMKSPLMPVSAQSVEAMLQLLADDHPDisatklaEIMSAYPDHAKPSGALALSRDAAFRMPTLWIADAHCR-HSPTWVYR 409
Cdd:COG2272   324 ALLGDLGPLTAADYRAALRRRFGDDAD-------EVLAAYPAASPAEALAALATDRVFRCPARRLAEAHAAaGAPVYLYR 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 410 FDHATPMLKAARIGAGHATELPYVFGNFgtlnvDPTFWLGGRKAAMEVAGRIQRRWLAFARHAVPAAlDGSKHWAPYEEE 489
Cdd:COG2272   397 FDWRSPPLRGFGLGAFHGAELPFVFGNL-----DAPALTGLTPADRALSDQMQAYWVNFARTGDPNG-PGLPEWPAYDPE 470
                         490       500
                  ....*....|....*....|..
gi 1517851394 490 RRSTLLIDSADTLVSDPDHGLR 511
Cdd:COG2272   471 DRAVMVFDAEPRVVNDPDAEER 492
COesterase pfam00135
Carboxylesterase family;
14-497 1.34e-131

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 392.06  E-value: 1.34e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  14 TLVIRARGGEARG-----YPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQGQSPAVPIDRAFKI 88
Cdd:pfam00135   2 SPVVTTSLGRVRGkrlkvDGGKPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSPGSSGLEG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  89 DEDCLSINVWAPRPD---GTPRPVMVWIHGGAYCLGSAAQtiYDGRHLAETGDVVLVSFNYRVGALGFLdlsgfSTADPV 165
Cdd:pfam00135  82 SEDCLYLNVYTPKELkenKNKLPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFL-----STGDDE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 166 FESNCGLRDQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQSPPATSVYG-AERAKTVA 244
Cdd:pfam00135 155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAiQSNARQRA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 245 ERFLELLSIDPEDAGdllttdleLLV-----KASDDLV----NEIPTRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRI 315
Cdd:pfam00135 235 KELAKLVGCPTSDSA--------ELVeclrsKPAEELLdaqlKLLVYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKV 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 316 PLIIGSNKDEASIF--KFMKSPLMP-------VSAQSVEAMLQLLADDHPDISATKLAEIMSAYPDHAKPS---GALALS 383
Cdd:pfam00135 307 PLLIGVTKDEGLLFaaYILDNVDILkaleeklLRSLLIDLLYLLLVDLPEEISAALREEYLDWGDRDDPETsrrALVELL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 384 RDAAFRMPTLWIADAH-CRHSPTWVYRFDHATPMLKA-ARIGAGHATELPYVFGN-FGTLNVDptfwlggRKAAMEVAGR 460
Cdd:pfam00135 387 TDYLFNCPVIRFADLHaSRGTPVYMYSFDYRGSSLRYpKWVGVDHGDELPYVFGTpFVGALLF-------TEEDEKLSRK 459
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1517851394 461 IQRRWLAFARHAVPAALDGSKHWAPYEEERRSTLLID 497
Cdd:pfam00135 460 MMTYWTNFAKTGNPNGPEGLPKWPPYTDENGQYLSID 496
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
21-505 4.10e-115

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 349.32  E-value: 4.10e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  21 GGEARGYPDGGVFAWKGMPYAAAPVGERRFRAPQPAEPWDGVRDCREFGPIAPQgqsPAVPIDRAF----KIDEDCLSIN 96
Cdd:cd00312     6 NGKVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQ---WDQLGGGLWnaklPGSEDCLYLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  97 VWAPRPD--GTPRPVMVWIHGGAYCLGSAaqTIYDGRHLAETGD-VVLVSFNYRVGALGFLdlsgfSTADPVFESNCGLR 173
Cdd:cd00312    83 VYTPKNTkpGNSLPVMVWIHGGGFMFGSG--SLYPGDGLAREGDnVIVVSINYRLGVLGFL-----STGDIELPGNYGLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 174 DQIAALEWVRDNIDAFGGDPSAVTVFGESSGAGSITTLMTCPSAEGLFHRAIAQS-----PPATSVYGAERAKtvaeRFL 248
Cdd:cd00312   156 DQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSgsalsPWAIQENARGRAK----RLA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 249 ELLSIDPEDAgdlLTTDLELLVKASDDLV----NEIPTRIPGTLAMAPVVDRDLVPHYPVAAFQKGYAHRIPLIIGSNKD 324
Cdd:cd00312   232 RLLGCNDTSS---AELLDCLRSKSAEELLdatrKLLLFSYSPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 325 EASIFKFM----KSPLMPVSAQSVEAMLQLLADDHPDISATKlaeIMSAYPDHAKPSGAL--ALSR---DAAFRMPTLWI 395
Cdd:cd00312   309 EGGYFAAMllnfDAKLIIETNDRWLELLPYLLFYADDALADK---VLEKYPGDVDDSVESrkNLSDmltDLLFKCPARYF 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 396 ADAHCRH--SPTWVYRFDHATPMLKAARI---GAGHATELPYVFGNfgtlnvdPTFWLGGRKAAMEVAGRIQRRWLAFAR 470
Cdd:cd00312   386 LAQHRKAggSPVYAYVFDHRSSLSVGRWPpwlGTVHGDEIFFVFGN-------PLLKEGLREEEEKLSRTMMKYWANFAK 458
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1517851394 471 HAVPAALDGSKHWAPYEEERRSTLLIDSADTLVSD 505
Cdd:cd00312   459 TGNPNTEGNLVVWPAYTSESEKYLDINIEGTEIKQ 493
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
97-230 1.82e-15

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 75.29  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  97 VWAPRPDGTPRPVMVWIHGGAYCLGSAAQTIYDGRHLAETGDVVLVSFNYRvgalgfldLS---GFSTAdpvfesncgLR 173
Cdd:COG0657     3 VYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYR--------LApehPFPAA---------LE 65
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1517851394 174 DQIAALEWVRDNIDAFGGDPSAVTVFGESSGAG--SITTLMTCPSAEGLFHRAIAQSPP 230
Cdd:COG0657    66 DAYAALRWLRANAAELGIDPDRIAVAGDSAGGHlaAALALRARDRGGPRPAAQVLIYPV 124
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
110-206 2.95e-10

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 59.92  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 110 MVWIHGGAYCLGSAAQtiYDG--RHLAETGDVVLVSFNYRvgalgfldLS---GFSTAdpvfesncgLRDQIAALEWVRD 184
Cdd:pfam07859   1 LVYFHGGGFVLGSADT--HDRlcRRLAAEAGAVVVSVDYR--------LApehPFPAA---------YDDAYAALRWLAE 61
                          90       100
                  ....*....|....*....|..
gi 1517851394 185 NIDAFGGDPSAVTVFGESSGAG 206
Cdd:pfam07859  62 QAAELGADPSRIAVAGDSAGGN 83
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
100-205 9.68e-09

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 55.65  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 100 PRPDGTPRPVMVWIHGGAYCLGS-AAQTIYD---GRHLAETGDVVlVSFNYRvgalgfldlsgfSTADPVFESncglrdQ 175
Cdd:pfam20434   6 PKNAKGPYPVVIWIHGGGWNSGDkEADMGFMtntVKALLKAGYAV-ASINYR------------LSTDAKFPA------Q 66
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1517851394 176 I----AALEWVRDNIDAFGGDPSAVTVFGESSGA 205
Cdd:pfam20434  67 IqdvkAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
90-257 1.90e-07

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 51.94  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  90 EDCLSINVWAPRP-DGTPRPVMVWIHGGayclGSAAQTIYDGRH--LAETGDVVLvSFNYR-----VGALGFLDlsgfst 161
Cdd:COG1506     5 ADGTTLPGWLYLPaDGKKYPVVVYVHGG----PGSRDDSFLPLAqaLASRGYAVL-APDYRgygesAGDWGGDE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 162 adpvfesncgLRDQIAALEWVRDNIDAfggDPSAVTVFGESSGAGsiTTLMTCPSAEGLFHRAIAQSPPATSVYGAERAK 241
Cdd:COG1506    74 ----------VDDVLAAIDYLAARPYV---DPDRIGIYGHSYGGY--MALLAAARHPDRFKAAVALAGVSDLRSYYGTTR 138
                         170
                  ....*....|....*.
gi 1517851394 242 TVAERFLELLSIDPED 257
Cdd:COG1506   139 EYTERLMGGPWEDPEA 154
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
96-255 5.70e-04

Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 41.82  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394  96 NVWAPRPDGTPRPVMVWIHGGAyclGSAAQTIYDGRHLAETGDVVLVsFNYRvgalGFldlsGFSTADPVFESNCGLRDQ 175
Cdd:COG1073    26 DLYLPAGASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLA-FDYR----GY----GESEGEPREEGSPERRDA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517851394 176 IAALEWVRDNIdafGGDPSAVTVFGESSGAG-SITTLMTCPSAEGLfhraIAQSPPaTSVY--GAERAKTVAERFLELLS 252
Cdd:COG1073    94 RAAVDYLRTLP---GVDPERIGLLGISLGGGyALNAAATDPRVKAV----ILDSPF-TSLEdlAAQRAKEARGAYLPGVP 165

                  ...
gi 1517851394 253 IDP 255
Cdd:COG1073   166 YLP 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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