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Conserved domains on  [gi|1463570081|ref|NP_001352336|]
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cocaine esterase isoform 3 [Homo sapiens]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10444481)

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.-
PubMed:  8453375|3163407|8280778|9704093|11099800
SCOP:  3000102

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
1-445 0e+00

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 576.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081   1 MCLQDLTaveseflsQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSN-LPVMVWIHGGALVFGMASLYDGSMLAALENVVV 79
Cdd:pfam00135  64 RCPQNGD--------LTSPGSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  80 VIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIM 159
Cdd:pfam00135 136 VTINYRLGPLGFLSTGDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAIL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 160 ESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKP---------FKMIPgVVDGVFLPRHP 230
Cdd:pfam00135 216 MSGSALSPWAIQSNARQRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKllvygsvpfVPFGP-VVDGDFLPEHP 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 231 QELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLM--LPPTFGDLLREEYI--GDNGD 306
Cdd:pfam00135 295 EELLKSGNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDD 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 307 PQTLQAQFQEMMADSMFVIPALQVAHFQCSR-APVYFYEFQHQPSWLKniRPPHMKADHGDELPFVFRSFFGGNYIkFTE 385
Cdd:pfam00135 375 PETSRRALVELLTDYLFNCPVIRFADLHASRgTPVYMYSFDYRGSSLR--YPKWVGVDHGDELPYVFGTPFVGALL-FTE 451

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1463570081 386 EEEQLSRKMMKYWANFARNGNPNG-EGLPHWPLF-DQEEQYLQLNLQPAVGRALKAHRLQFW 445
Cdd:pfam00135 452 EDEKLSRKMMTYWTNFAKTGNPNGpEGLPKWPPYtDENGQYLSIDLEPRVKQGLKAERCAFW 513
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
1-445 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 576.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081   1 MCLQDLTaveseflsQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSN-LPVMVWIHGGALVFGMASLYDGSMLAALENVVV 79
Cdd:pfam00135  64 RCPQNGD--------LTSPGSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  80 VIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIM 159
Cdd:pfam00135 136 VTINYRLGPLGFLSTGDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAIL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 160 ESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKP---------FKMIPgVVDGVFLPRHP 230
Cdd:pfam00135 216 MSGSALSPWAIQSNARQRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKllvygsvpfVPFGP-VVDGDFLPEHP 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 231 QELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLM--LPPTFGDLLREEYI--GDNGD 306
Cdd:pfam00135 295 EELLKSGNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDD 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 307 PQTLQAQFQEMMADSMFVIPALQVAHFQCSR-APVYFYEFQHQPSWLKniRPPHMKADHGDELPFVFRSFFGGNYIkFTE 385
Cdd:pfam00135 375 PETSRRALVELLTDYLFNCPVIRFADLHASRgTPVYMYSFDYRGSSLR--YPKWVGVDHGDELPYVFGTPFVGALL-FTE 451

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1463570081 386 EEEQLSRKMMKYWANFARNGNPNG-EGLPHWPLF-DQEEQYLQLNLQPAVGRALKAHRLQFW 445
Cdd:pfam00135 452 EDEKLSRKMMTYWTNFAKTGNPNGpEGLPKWPPYtDENGQYLSIDLEPRVKQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-431 5.56e-155

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: 449.09  E-value: 5.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081   1 MCLQDltavesEFLSQFNMTFPSDsMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDG-SMLAALENVVV 79
Cdd:cd00312    56 SCMQW------DQLGGGLWNAKLP-GSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGdGLAREGDNVIV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  80 VIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIM 159
Cdd:cd00312   129 VSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAIS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 160 ESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPG--------VVDGVFLPRHPQ 231
Cdd:cd00312   209 QSGSALSPWAIQENARGRAKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFSYspflpfgpVVDGDFIPDDPE 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 232 ELLASADFQPVPSIVGVNNNEFGWLIPkvmRIYDTQKEMDREASQAALQKMLTLLMLPPT-FGDLLREEYIGDNGDPQTL 310
Cdd:cd00312   289 ELIKEGKFAKVPLIIGVTKDEGGYFAA---MLLNFDAKLIIETNDRWLELLPYLLFYADDaLADKVLEKYPGDVDDSVES 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 311 QAQFQEMMADSMFVIPA-LQVAHF-QCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGgnYIKFTEEEE 388
Cdd:cd00312   366 RKNLSDMLTDLLFKCPArYFLAQHrKAGGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLL--KEGLREEEE 443

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1463570081 389 QLSRKMMKYWANFARNGNPNGEG-LPHWPLFD-QEEQYLQLNLQP 431
Cdd:cd00312   444 KLSRTMMKYWANFAKTGNPNTEGnLVVWPAYTsESEKYLDINIEG 488
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
17-447 2.43e-142

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 416.98  E-value: 2.43e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  17 FNMTFPSDSMSEDCLYLSIYTPAHShEGSNLPVMVWIHGGALVFGMAS--LYDGSMLAAlENVVVVIIQYRLGVLGFF-- 92
Cdd:COG2272    76 PGDPGGPAPGSEDCLYLNVWTPALA-AGAKLPVMVWIHGGGFVSGSGSepLYDGAALAR-RGVVVVTINYRLGALGFLal 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  93 ---STGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGL 169
Cdd:COG2272   154 palSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLT 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 170 IASSADVISTVVANLSAcdqvdSEALVGCLRGKSKEEILAI-NKPFKMIPG------VVDGVFLPRHPQELLASADFQPV 242
Cdd:COG2272   234 LAEAEAVGAAFAAALGV-----APATLAALRALPAEELLAAqAALAAEGPGglpfgpVVDGDVLPEDPLEAFAAGRAADV 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 243 PSIVGVNNNEFGWLipkvMRIYDTQKEMDREASQAALQKMLtllmlpPTFGDLLREEYigDNGDPQTLQAQfqeMMADSM 322
Cdd:COG2272   309 PLLIGTNRDEGRLF----AALLGDLGPLTAADYRAALRRRF------GDDADEVLAAY--PAASPAEALAA---LATDRV 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 323 FVIPALQVAHFQCSR-APVYFYEFQHQPSWLkniRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANF 401
Cdd:COG2272   374 FRCPARRLAEAHAAAgAPVYLYRFDWRSPPL---RGFGLGAFHGAELPFVFGNLDAPALTGLTPADRALSDQMQAYWVNF 450

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1463570081 402 ARNGNPNGEGLPHWPLFDQEE-QYLQLNLQPAVGRAL-KAHRLQFWKK 447
Cdd:COG2272   451 ARTGDPNGPGLPEWPAYDPEDrAVMVFDAEPRVVNDPdAEERLDLWDG 498
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
1-445 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 576.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081   1 MCLQDLTaveseflsQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSN-LPVMVWIHGGALVFGMASLYDGSMLAALENVVV 79
Cdd:pfam00135  64 RCPQNGD--------LTSPGSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIV 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  80 VIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIM 159
Cdd:pfam00135 136 VTINYRLGPLGFLSTGDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAIL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 160 ESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKP---------FKMIPgVVDGVFLPRHP 230
Cdd:pfam00135 216 MSGSALSPWAIQSNARQRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKllvygsvpfVPFGP-VVDGDFLPEHP 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 231 QELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLM--LPPTFGDLLREEYI--GDNGD 306
Cdd:pfam00135 295 EELLKSGNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDD 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 307 PQTLQAQFQEMMADSMFVIPALQVAHFQCSR-APVYFYEFQHQPSWLKniRPPHMKADHGDELPFVFRSFFGGNYIkFTE 385
Cdd:pfam00135 375 PETSRRALVELLTDYLFNCPVIRFADLHASRgTPVYMYSFDYRGSSLR--YPKWVGVDHGDELPYVFGTPFVGALL-FTE 451

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1463570081 386 EEEQLSRKMMKYWANFARNGNPNG-EGLPHWPLF-DQEEQYLQLNLQPAVGRALKAHRLQFW 445
Cdd:pfam00135 452 EDEKLSRKMMTYWTNFAKTGNPNGpEGLPKWPPYtDENGQYLSIDLEPRVKQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 1-431 5.56e-155

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: 449.09  E-value: 5.56e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081   1 MCLQDltavesEFLSQFNMTFPSDsMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDG-SMLAALENVVV 79
Cdd:cd00312    56 SCMQW------DQLGGGLWNAKLP-GSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGdGLAREGDNVIV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  80 VIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIM 159
Cdd:cd00312   129 VSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAIS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 160 ESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPG--------VVDGVFLPRHPQ 231
Cdd:cd00312   209 QSGSALSPWAIQENARGRAKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFSYspflpfgpVVDGDFIPDDPE 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 232 ELLASADFQPVPSIVGVNNNEFGWLIPkvmRIYDTQKEMDREASQAALQKMLTLLMLPPT-FGDLLREEYIGDNGDPQTL 310
Cdd:cd00312   289 ELIKEGKFAKVPLIIGVTKDEGGYFAA---MLLNFDAKLIIETNDRWLELLPYLLFYADDaLADKVLEKYPGDVDDSVES 365

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 311 QAQFQEMMADSMFVIPA-LQVAHF-QCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGgnYIKFTEEEE 388
Cdd:cd00312   366 RKNLSDMLTDLLFKCPArYFLAQHrKAGGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLL--KEGLREEEE 443

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1463570081 389 QLSRKMMKYWANFARNGNPNGEG-LPHWPLFD-QEEQYLQLNLQP 431
Cdd:cd00312   444 KLSRTMMKYWANFAKTGNPNTEGnLVVWPAYTsESEKYLDINIEG 488
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
17-447 2.43e-142

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 416.98  E-value: 2.43e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  17 FNMTFPSDSMSEDCLYLSIYTPAHShEGSNLPVMVWIHGGALVFGMAS--LYDGSMLAAlENVVVVIIQYRLGVLGFF-- 92
Cdd:COG2272    76 PGDPGGPAPGSEDCLYLNVWTPALA-AGAKLPVMVWIHGGGFVSGSGSepLYDGAALAR-RGVVVVTINYRLGALGFLal 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  93 ---STGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGL 169
Cdd:COG2272   154 palSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLT 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 170 IASSADVISTVVANLSAcdqvdSEALVGCLRGKSKEEILAI-NKPFKMIPG------VVDGVFLPRHPQELLASADFQPV 242
Cdd:COG2272   234 LAEAEAVGAAFAAALGV-----APATLAALRALPAEELLAAqAALAAEGPGglpfgpVVDGDVLPEDPLEAFAAGRAADV 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 243 PSIVGVNNNEFGWLipkvMRIYDTQKEMDREASQAALQKMLtllmlpPTFGDLLREEYigDNGDPQTLQAQfqeMMADSM 322
Cdd:COG2272   309 PLLIGTNRDEGRLF----AALLGDLGPLTAADYRAALRRRF------GDDADEVLAAY--PAASPAEALAA---LATDRV 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081 323 FVIPALQVAHFQCSR-APVYFYEFQHQPSWLkniRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANF 401
Cdd:COG2272   374 FRCPARRLAEAHAAAgAPVYLYRFDWRSPPL---RGFGLGAFHGAELPFVFGNLDAPALTGLTPADRALSDQMQAYWVNF 450

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1463570081 402 ARNGNPNGEGLPHWPLFDQEE-QYLQLNLQPAVGRAL-KAHRLQFWKK 447
Cdd:COG2272   451 ARTGDPNGPGLPEWPAYDPEDrAVMVFDAEPRVVNDPdAEERLDLWDG 498
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
35-138 1.87e-19

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 86.47  E-value: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  35 IYTPAHSHEgsNLPVMVWIHGGALVFGMASLYDG--SMLAALENVVVVIIQYRLgvlgffSTGDKHATGnwgyLDQV-AA 111
Cdd:COG0657     3 VYRPAGAKG--PLPVVVYFHGGGWVSGSKDTHDPlaRRLAARAGAAVVSVDYRL------APEHPFPAA----LEDAyAA 70

                          90       100
                  ....*....|....*....|....*..
gi 1463570081 112 LRWVQQNIAHFGGNPDRVTIFGESAGG 138
Cdd:COG0657    71 LRWLRANAAELGIDPDRIAVAGDSAGG 97
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 33-138 2.36e-13

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: 69.13  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  33 LSIYTPAHshEGSNLPVMVWIHGGALVFG----MASLYDGSMLAALEN-VVVVIIQYRLgvlgffsTGDKHATgnwgylD 107
Cdd:pfam20434   1 LDIYLPKN--AKGPYPVVIWIHGGGWNSGdkeaDMGFMTNTVKALLKAgYAVASINYRL-------STDAKFP------A 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1463570081 108 QV----AALRWVQQNIAHFGGNPDRVTIFGESAGG 138
Cdd:pfam20434  66 QIqdvkAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 50-138 2.36e-12

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: 66.08  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  50 MVWIHGGALVFGMASLYDGSM--LAALENVVVVIIQYRLGvlgffstgDKH---AtgnwGYLDQVAALRWVQQNIAHFGG 124
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCrrLAAEAGAVVVSVDYRLA--------PEHpfpA----AYDDAYAALRWLAEQAAELGA 68

                          90
                  ....*....|....
gi 1463570081 125 NPDRVTIFGESAGG 138
Cdd:pfam07859  69 DPSRIAVAGDSAGG 82
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
35-164 1.66e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.10  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  35 IYTPAhshEGSNLPVMVWIHGGALVFGMASLYDGSMLAALeNVVVVIIQYRlgvlgffstGDKHATGNWG---YLDQVAA 111
Cdd:COG1506    14 LYLPA---DGKKYPVVVYVHGGPGSRDDSFLPLAQALASR-GYAVLAPDYR---------GYGESAGDWGgdeVDDVLAA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1463570081 112 LRWVqqnIAHFGGNPDRVTIFGESAGGTSVSSLVVspISQGLFHGAIMESGVA 164
Cdd:COG1506    81 IDYL---AARPYVDPDRIGIYGHSYGGYMALLAAA--RHPDRFKAAVALAGVS 128
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 35-138 3.78e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 45.29  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  35 IYTPAHSHEGsnLPVMVWIHGGALVFGMASLYdGSMLAALeNVVVVIIQYRlgvlgFF--STGDKHATGNWGYLDQVAAL 112
Cdd:COG1073    27 LYLPAGASKK--YPAVVVAHGNGGVKEQRALY-AQRLAEL-GFNVLAFDYR-----GYgeSEGEPREEGSPERRDARAAV 97

                          90       100
                  ....*....|....*....|....*.
gi 1463570081 113 RWVQQniaHFGGNPDRVTIFGESAGG 138
Cdd:COG1073    98 DYLRT---LPGVDPERIGLLGISLGG 120
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
71-164 3.89e-04

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 41.83  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  71 LAALENVVVVIIQYR-LGVLG--FFSTGDKHaTGNWGYLDQVAALRWVqqnIAHFGGNPDRVTIFGESAGGTSVSSLVVs 147
Cdd:pfam00326   9 LLADRGYVVAIANGRgSGGYGeaFHDAGKGD-LGQNEFDDFIAAAEYL---IEQGYTDPDRLAIWGGSYGGYLTGAALN- 83

                          90
                  ....*....|....*...
gi 1463570081 148 piSQG-LFHGAIMESGVA 164
Cdd:pfam00326  84 --QRPdLFKAAVAHVPVV 99
COG4099 COG4099
Predicted peptidase [General function prediction only];
34-138 6.61e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 41.11  E-value: 6.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  34 SIYTPAHSHEGSNLPVMVWIHGG---------ALVFGmASLYDGSMLAALENVVVVIIQYRLGvlgffstgdkhatGNWG 104
Cdd:COG4099    36 RLYLPKGYDPGKKYPLVLFLHGAgergtdnekQLTHG-APKFINPENQAKFPAIVLAPQCPED-------------DYWS 101

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1463570081 105 YLDQVAAL-RWVQQNIAHFGGNPDRVTIFGESAGG 138
Cdd:COG4099   102 DTKALDAVlALLDDLIAEYRIDPDRIYLTGLSMGG 136
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 33-141 2.16e-03

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 39.75  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1463570081  33 LSIYTPAHSHEGSNLPVMVWIHGGALV--FGMASLYDGSMLAALENVVVVIIQYRLGVLGFFST---GDKHATGNWG--Y 105
Cdd:pfam00756  10 VQVYLPEDYPPGRKYPVLYLLDGTGWFqnGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDwdrGLNATEGPGAyaY 89

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1463570081 106 LDQVAA--LRWVQqniAHFGGNPDRVTIFGESAGGTSV 141
Cdd:pfam00756  90 ETFLTQelPPLLD---ANFPTAPDGRALAGQSMGGLGA 124
 
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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