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Conserved domains on  [gi|298493216|ref|NP_001177275|]
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carboxylesterase 2 isoform 2 precursor [Rattus norvegicus]

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

CATH:  3.40.50.1820
EC:  3.1.1.-
Gene Ontology:  GO:0052689
PubMed:  8453375|3163407|8280778|9704093|11099800|37582413|31545554
SCOP:  3000102|4000699

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
30-446 0e+00

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 544.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216   30 SPIRTTHTGQILGSLIHMKGLDvGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMqafkll 109
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSP------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  110 klTLPLIPMSEDCLYLNIYTPNHAHEGSN-LPVMVWIHGGALVIGMASLYDGSMLAAMENVVVVTIQYRLGVLGFFSTGD 188
Cdd:pfam00135  75 --GSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  189 QHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDV 268
Cdd:pfam00135 153 DEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  269 VYRTVANLSGCEQVDSKALVNCLRGKSEEEIMSINKAFRIISG--------IVDGIFLPRHPKELLASADFHPIPSIIGV 340
Cdd:pfam00135 233 RAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYGSvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  341 NNDEYGWIIPSSMTTTDSKKKMDRQMVQAILQKRVAQMM--WPPEFSDLLLEEYM--GDSEDPQFLQVQFKEMMEDFTFV 416
Cdd:pfam00135 313 TKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDDPETSRRALVELLTDYLFN 392

                         410       420       430
                  ....*....|....*....|....*....|.
gi 298493216  417 IPALQVAHFQRS-NAPVYFYEFQLCTTGESQ 446
Cdd:pfam00135 393 CPVIRFADLHASrGTPVYMYSFDYRGSSLRY 423
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
30-446 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 544.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216   30 SPIRTTHTGQILGSLIHMKGLDvGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMqafkll 109
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSP------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  110 klTLPLIPMSEDCLYLNIYTPNHAHEGSN-LPVMVWIHGGALVIGMASLYDGSMLAAMENVVVVTIQYRLGVLGFFSTGD 188
Cdd:pfam00135  75 --GSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  189 QHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDV 268
Cdd:pfam00135 153 DEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  269 VYRTVANLSGCEQVDSKALVNCLRGKSEEEIMSINKAFRIISG--------IVDGIFLPRHPKELLASADFHPIPSIIGV 340
Cdd:pfam00135 233 RAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYGSvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  341 NNDEYGWIIPSSMTTTDSKKKMDRQMVQAILQKRVAQMM--WPPEFSDLLLEEYM--GDSEDPQFLQVQFKEMMEDFTFV 416
Cdd:pfam00135 313 TKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDDPETSRRALVELLTDYLFN 392

                         410       420       430
                  ....*....|....*....|....*....|.
gi 298493216  417 IPALQVAHFQRS-NAPVYFYEFQLCTTGESQ 446
Cdd:pfam00135 393 CPVIRFADLHASrGTPVYMYSFDYRGSSLRY 423
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 48-438 1.12e-149

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: 434.84  E-value: 1.12e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  48 KGLDVG-VHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDitamNMQAFKLLKLTLPlipMSEDCLYLN 126
Cdd:cd00312   10 RGVDEGgVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQW----DQLGGGLWNAKLP---GSEDCLYLN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 127 IYTPNHAHEGSNLPVMVWIHGGALVIGMASLYDG-SMLAAMENVVVVTIQYRLGVLGFFSTGDQHARGNWGYLDQVAALH 205
Cdd:cd00312   83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 206 WVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDVVYRTVANLSGCEQVDSK 285
Cdd:cd00312  163 WVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCNDTSSA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 286 ALVNCLRGKSEEEIMSINK--------AFRIISGIVDGIFLPRHPKELLASADFHPIPSIIGVNNDEYGWIIPSSMTTTD 357
Cdd:cd00312  243 ELLDCLRSKSAEELLDATRklllfsysPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 358 SKKKMDRQ----MVQAILQKRvaqmmwPPEFSDLLLEEYMGDSEDPqflQVQFK---EMMEDFTFVIPA-LQVAHFQRSN 429
Cdd:cd00312  323 KLIIETNDrwleLLPYLLFYA------DDALADKVLEKYPGDVDDS---VESRKnlsDMLTDLLFKCPArYFLAQHRKAG 393

                        410
                 ....*....|
gi 298493216 430 -APVYFYEFQ 438
Cdd:cd00312  394 gSPVYAYVFD 403
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
30-437 2.44e-137

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 403.50  E-value: 2.44e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  30 SPIRTTHTGQILGSLIHmkgldvGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMQafkll 109
Cdd:COG2272   12 APVVRTEAGRVRGVVEG------GVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPG----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 110 kltlPLIPMSEDCLYLNIYTPNHAhEGSNLPVMVWIHGGALVIGMAS--LYDGSMLAAmENVVVVTIQYRLGVLGFF--- 184
Cdd:COG2272   81 ----GPAPGSEDCLYLNVWTPALA-AGAKLPVMVWIHGGGFVSGSGSepLYDGAALAR-RGVVVVTINYRLGALGFLalp 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 185 --STGDQHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLI 262
Cdd:COG2272  155 alSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 263 SVSSDVVyRTVANLSGCEQVDskalVNCLRGKSEEEIMSI-NKAFRIISG------IVDGIFLPRHPKELLASADFHPIP 335
Cdd:COG2272  235 AEAEAVG-AAFAAALGVAPAT----LAALRALPAEELLAAqAALAAEGPGglpfgpVVDGDVLPEDPLEAFAAGRAADVP 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 336 SIIGVNNDEYGWIipssMTTTDSKKKMDRQMVQAILQKRVaqmmwpPEFSDLLLEEYMGDSedpqfLQVQFKEMMEDFTF 415
Cdd:COG2272  310 LLIGTNRDEGRLF----AALLGDLGPLTAADYRAALRRRF------GDDADEVLAAYPAAS-----PAEALAALATDRVF 374

                        410       420
                 ....*....|....*....|...
gi 298493216 416 VIPALQVAH-FQRSNAPVYFYEF 437
Cdd:COG2272  375 RCPARRLAEaHAAAGAPVYLYRF 397
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
30-446 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 544.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216   30 SPIRTTHTGQILGSLIHMKGLDvGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMqafkll 109
Cdd:pfam00135   2 SPVVTTSLGRVRGKRLKVDGGK-PVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTSP------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  110 klTLPLIPMSEDCLYLNIYTPNHAHEGSN-LPVMVWIHGGALVIGMASLYDGSMLAAMENVVVVTIQYRLGVLGFFSTGD 188
Cdd:pfam00135  75 --GSSGLEGSEDCLYLNVYTPKELKENKNkLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  189 QHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDV 268
Cdd:pfam00135 153 DEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  269 VYRTVANLSGCEQVDSKALVNCLRGKSEEEIMSINKAFRIISG--------IVDGIFLPRHPKELLASADFHPIPSIIGV 340
Cdd:pfam00135 233 RAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLVYGSvpfvpfgpVVDGDFLPEHPEELLKSGNFPKVPLLIGV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  341 NNDEYGWIIPSSMTTTDSKKKMDRQMVQAILQKRVAQMM--WPPEFSDLLLEEYM--GDSEDPQFLQVQFKEMMEDFTFV 416
Cdd:pfam00135 313 TKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLvdLPEEISAALREEYLdwGDRDDPETSRRALVELLTDYLFN 392

                         410       420       430
                  ....*....|....*....|....*....|.
gi 298493216  417 IPALQVAHFQRS-NAPVYFYEFQLCTTGESQ 446
Cdd:pfam00135 393 CPVIRFADLHASrGTPVYMYSFDYRGSSLRY 423
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 48-438 1.12e-149

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: 434.84  E-value: 1.12e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  48 KGLDVG-VHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDitamNMQAFKLLKLTLPlipMSEDCLYLN 126
Cdd:cd00312   10 RGVDEGgVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQW----DQLGGGLWNAKLP---GSEDCLYLN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 127 IYTPNHAHEGSNLPVMVWIHGGALVIGMASLYDG-SMLAAMENVVVVTIQYRLGVLGFFSTGDQHARGNWGYLDQVAALH 205
Cdd:cd00312   83 VYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 206 WVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLISVSSDVVYRTVANLSGCEQVDSK 285
Cdd:cd00312  163 WVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAKRLARLLGCNDTSSA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 286 ALVNCLRGKSEEEIMSINK--------AFRIISGIVDGIFLPRHPKELLASADFHPIPSIIGVNNDEYGWIIPSSMTTTD 357
Cdd:cd00312  243 ELLDCLRSKSAEELLDATRklllfsysPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 358 SKKKMDRQ----MVQAILQKRvaqmmwPPEFSDLLLEEYMGDSEDPqflQVQFK---EMMEDFTFVIPA-LQVAHFQRSN 429
Cdd:cd00312  323 KLIIETNDrwleLLPYLLFYA------DDALADKVLEKYPGDVDDS---VESRKnlsDMLTDLLFKCPArYFLAQHRKAG 393

                        410
                 ....*....|
gi 298493216 430 -APVYFYEFQ 438
Cdd:cd00312  394 gSPVYAYVFD 403
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
30-437 2.44e-137

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 403.50  E-value: 2.44e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  30 SPIRTTHTGQILGSLIHmkgldvGVHSFLGIPFAKPPIGPLRFAPPEAPEPWSGVRDGTSHPAMCLQDITAMNMQafkll 109
Cdd:COG2272   12 APVVRTEAGRVRGVVEG------GVRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPG----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 110 kltlPLIPMSEDCLYLNIYTPNHAhEGSNLPVMVWIHGGALVIGMAS--LYDGSMLAAmENVVVVTIQYRLGVLGFF--- 184
Cdd:COG2272   81 ----GPAPGSEDCLYLNVWTPALA-AGAKLPVMVWIHGGGFVSGSGSepLYDGAALAR-RGVVVVTINYRLGALGFLalp 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 185 --STGDQHARGNWGYLDQVAALHWVQQNIAHFGGNPDRVTIFGESAGGTSVSSHVVSPMSRGLFHGAIMESGVALMSSLI 262
Cdd:COG2272  155 alSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLSVLTL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 263 SVSSDVVyRTVANLSGCEQVDskalVNCLRGKSEEEIMSI-NKAFRIISG------IVDGIFLPRHPKELLASADFHPIP 335
Cdd:COG2272  235 AEAEAVG-AAFAAALGVAPAT----LAALRALPAEELLAAqAALAAEGPGglpfgpVVDGDVLPEDPLEAFAAGRAADVP 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 336 SIIGVNNDEYGWIipssMTTTDSKKKMDRQMVQAILQKRVaqmmwpPEFSDLLLEEYMGDSedpqfLQVQFKEMMEDFTF 415
Cdd:COG2272  310 LLIGTNRDEGRLF----AALLGDLGPLTAADYRAALRRRF------GDDADEVLAAYPAAS-----PAEALAALATDRVF 374

                        410       420
                 ....*....|....*....|...
gi 298493216 416 VIPALQVAH-FQRSNAPVYFYEF 437
Cdd:COG2272  375 RCPARRLAEaHAAAGAPVYLYRF 397
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
127-230 1.01e-17

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 81.46  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 127 IYTPnhAHEGSNLPVMVWIHGGALVIGMASLYDG--SMLAAMENVVVVTIQYRLGVLGFFSTGdqhargnwgyLDQV-AA 203
Cdd:COG0657    3 VYRP--AGAKGPLPVVVYFHGGGWVSGSKDTHDPlaRRLAARAGAAVVSVDYRLAPEHPFPAA----------LEDAyAA 70

                         90       100
                 ....*....|....*....|....*..
gi 298493216 204 LHWVQQNIAHFGGNPDRVTIFGESAGG 230
Cdd:COG0657   71 LRWLRANAAELGIDPDRIAVAGDSAGG 97
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 142-230 4.40e-13

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: 68.01  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  142 MVWIHGGALVIGMASLYDGSM--LAAMENVVVVTIQYRLGvlgffstgDQH---ArgnwGYLDQVAALHWVQQNIAHFGG 216
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCrrLAAEAGAVVVSVDYRLA--------PEHpfpA----AYDDAYAALRWLAEQAAELGA 68

                          90
                  ....*....|....
gi 298493216  217 NPDRVTIFGESAGG 230
Cdd:pfam07859  69 DPSRIAVAGDSAGG 82
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 125-230 1.19e-10

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: 61.04  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  125 LNIYTPnhAHEGSNLPVMVWIHGGALVIG----MASLYDGSMLAAMEN-VVVVTIQYRLgvlgffsTGDQHARgnwgylD 199
Cdd:pfam20434   1 LDIYLP--KNAKGPYPVVIWIHGGGWNSGdkeaDMGFMTNTVKALLKAgYAVASINYRL-------STDAKFP------A 65

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 298493216  200 QV----AALHWVQQNIAHFGGNPDRVTIFGESAGG 230
Cdd:pfam20434  66 QIqdvkAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
127-267 1.90e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 57.72  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 127 IYTPnhaHEGSNLPVMVWIHGGALVIGMASLYDGSMLAAMeNVVVVTIQYRlgvlgffstGDQHARGNWG---YLDQVAA 203
Cdd:COG1506   14 LYLP---ADGKKYPVVVYVHGGPGSRDDSFLPLAQALASR-GYAVLAPDYR---------GYGESAGDWGgdeVDDVLAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298493216 204 LHWVqqnIAHFGGNPDRVTIFGESAGGTSVSSHVVspMSRGLFHGAIMESGVALMSSLISVSSD 267
Cdd:COG1506   81 IDYL---AARPYVDPDRIGIYGHSYGGYMALLAAA--RHPDRFKAAVALAGVSDLRSYYGTTRE 139
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 126-230 4.55e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.91  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 126 NIYTPnhAHEGSNLPVMVWIHGGALVIGMASLYdGSMLAAMeNVVVVTIQYRlgvlgFF--STGDQHargNWGYLDQVAA 203
Cdd:COG1073   26 DLYLP--AGASKKYPAVVVAHGNGGVKEQRALY-AQRLAEL-GFNVLAFDYR-----GYgeSEGEPR---EEGSPERRDA 93

                         90       100
                 ....*....|....*....|....*..
gi 298493216 204 LHWVQQNIAHFGGNPDRVTIFGESAGG 230
Cdd:COG1073   94 RAAVDYLRTLPGVDPERIGLLGISLGG 120
COG4099 COG4099
Predicted peptidase [General function prediction only];
126-230 1.41e-03

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.95  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216 126 NIYTPNHAHEGSNLPVMVWIHGG---------ALVIGmASLYDGSMLAAMENVVVVTIQYRLGvlGFFSTGDQHArgnwg 196
Cdd:COG4099   36 RLYLPKGYDPGKKYPLVLFLHGAgergtdnekQLTHG-APKFINPENQAKFPAIVLAPQCPED--DYWSDTKALD----- 107

                         90       100       110
                 ....*....|....*....|....*....|....
gi 298493216 197 yldqvAALHWVQQNIAHFGGNPDRVTIFGESAGG 230
Cdd:COG4099  108 -----AVLALLDDLIAEYRIDPDRIYLTGLSMGG 136
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 125-233 3.97e-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: 38.98  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  125 LNIYTPNHAHEGSNLPVMVWIHGGALVIGMA--SLYDGSML-AAMENVVVVTIQYRlGVLGFFSTGDQ---HARGNWG-- 196
Cdd:pfam00756  10 VQVYLPEDYPPGRKYPVLYLLDGTGWFQNGPakEGLDRLAAsGEIPPVIIVGSPRG-GEVSFYSDWDRglnATEGPGAya 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 298493216  197 YLDQVAA--LHWVQqniAHFGGNPDRVTIFGESAGGTSV 233
Cdd:pfam00756  89 YETFLTQelPPLLD---ANFPTAPDGRALAGQSMGGLGA 124
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
161-258 5.35e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.98  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298493216  161 SMLAAMeNVVVVTIQYRLGvlGFFSTGDQHA-RGNWG---YLDQVAAL-HWVQQNIAhfggNPDRVTIFGESAGGTSVSS 235
Cdd:pfam00326   8 QLLADR-GYVVAIANGRGS--GGYGEAFHDAgKGDLGqneFDDFIAAAeYLIEQGYT----DPDRLAIWGGSYGGYLTGA 80

                          90       100
                  ....*....|....*....|...
gi 298493216  236 hVVSPMSRgLFHGAIMESGVALM 258
Cdd:pfam00326  81 -ALNQRPD-LFKAAVAHVPVVDW 101
 
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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