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Conserved domains on  [gi|114793724|pdb|2DR0|B]
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Chain B, Liver carboxylesterase 1

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

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
4-528 0e+00

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 634.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B          4 SPPVVDTVHGKVLGKFVSLEGFaQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQllself 83
Cdd:pfam00135   1 DSPVVTTSLGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTS------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B         84 tnrKENIPLKLSEDCLYLNIYTPADLTK-KNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST 162
Cdd:pfam00135  74 ---PGSSGLEGSEDCLYLNVYTPKELKEnKNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLST 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        163 GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD 242
Cdd:pfam00135 151 GDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        243 VKpLAEQIAITAGCKTTTSAVMVHCLRQKTEeellettlkMKFLSLDLQGDPRESQPLL--GTVIDGMLLLKTPEELQAE 320
Cdd:pfam00135 231 RQ-RAKELAKLVGCPTSDSAELVECLRSKPA---------EELLDAQLKLLVYGSVPFVpfGPVVDGDFLPEHPEELLKS 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        321 RNFHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAK--ELIPEATEKYL--GGTDDTVKKKD 396
Cdd:pfam00135 301 GNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLVDLpeEISAALREEYLdwGDRDDPETSRR 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        397 LFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSsdMKPKTVIGDHGDELFSVFGAPFL-KEGASEEEIRLSK 475
Cdd:pfam00135 381 ALVELLTDYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSL--RYPKWVGVDHGDELPYVFGTPFVgALLFTEEDEKLSR 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
2DR0_B        476 MVMKFWANFARNGNPNG-EGLPHWPEYNQKEG-YLQIGANTQAAQKLKDKEVAFW 528
Cdd:pfam00135 459 KMMTYWTNFAKTGNPNGpEGLPKWPPYTDENGqYLSIDLEPRVKQGLKAERCAFW 513
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
4-528 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 634.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B          4 SPPVVDTVHGKVLGKFVSLEGFaQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQllself 83
Cdd:pfam00135   1 DSPVVTTSLGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTS------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B         84 tnrKENIPLKLSEDCLYLNIYTPADLTK-KNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST 162
Cdd:pfam00135  74 ---PGSSGLEGSEDCLYLNVYTPKELKEnKNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLST 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        163 GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD 242
Cdd:pfam00135 151 GDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        243 VKpLAEQIAITAGCKTTTSAVMVHCLRQKTEeellettlkMKFLSLDLQGDPRESQPLL--GTVIDGMLLLKTPEELQAE 320
Cdd:pfam00135 231 RQ-RAKELAKLVGCPTSDSAELVECLRSKPA---------EELLDAQLKLLVYGSVPFVpfGPVVDGDFLPEHPEELLKS 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        321 RNFHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAK--ELIPEATEKYL--GGTDDTVKKKD 396
Cdd:pfam00135 301 GNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLVDLpeEISAALREEYLdwGDRDDPETSRR 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        397 LFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSsdMKPKTVIGDHGDELFSVFGAPFL-KEGASEEEIRLSK 475
Cdd:pfam00135 381 ALVELLTDYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSL--RYPKWVGVDHGDELPYVFGTPFVgALLFTEEDEKLSR 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
2DR0_B        476 MVMKFWANFARNGNPNG-EGLPHWPEYNQKEG-YLQIGANTQAAQKLKDKEVAFW 528
Cdd:pfam00135 459 KMMTYWTNFAKTGNPNGpEGLPKWPPYTDENGqYLSIDLEPRVKQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
7-519 0e+00

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: 595.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        7 VVDTVHGKVLGKFVSlegfaqPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLselftnr 86
Cdd:cd00312   1 LVVTPNGKVRGVDEG------GVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQLGGGL------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       87 kENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAA-HENVVVVTIQYRLGIWGFFSTGDE 165
Cdd:cd00312  68 -WNAKLPGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAReGDNVIVVSINYRLGVLGFLSTGDI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      166 HSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGdVKP 245
Cdd:cd00312 147 ELPGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQEN-ARG 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      246 LAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGdpresqpLLGTVIDGMLLLKTPEELQAERNFHT 325
Cdd:cd00312 226 RAKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFSYSPFL-------PFGPVVDGDFIPDDPEELIKEGKFAK 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      326 VPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSLLwkSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADV 405
Cdd:cd00312 299 VPLIIGVTKDEGGYFAAMLLNFDAKLIIETNDRWLELL--PYLLFYADDALADKVLEKYPGDVDDSVESRKNLSDMLTDL 376
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      406 MFGVPSVIVARNHRDA-GAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANF 484
Cdd:cd00312 377 LFKCPARYFLAQHRKAgGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLKEGLREEEEKLSRTMMKYWANF 456
                       490       500       510
                ....*....|....*....|....*....|....*..
2DR0_B      485 ARNGNPNGEG-LPHWPEYN-QKEGYLQIGANTQAAQK 519
Cdd:cd00312 457 AKTGNPNTEGnLVVWPAYTsESEKYLDINIEGTEIKQ 493
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-532 1.39e-155

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 453.58  E-value: 1.39e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        1 HPSSPPVVDTVHGKVLGkfVSLEGfaqpVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLS 80
Cdd:COG2272   8 AAAAAPVVRTEAGRVRG--VVEGG----VRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       81 elftnrkeniPLKLSEDCLYLNIYTPADLTKKnRLPVMVWIHGGGLMVGAAST--YDGLALAAhENVVVVTIQYRLGIWG 158
Cdd:COG2272  82 ----------PAPGSEDCLYLNVWTPALAAGA-KLPVMVWIHGGGFVSGSGSEplYDGAALAR-RGVVVVTINYRLGALG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      159 FF-----STGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVAL 233
Cdd:COG2272 150 FLalpalSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      234 TsvLVKKGDVKPLAEQIAITAGCKTTTSAvmvhCLRQKTEEellettlkmKFLSLDLQGDPRESQPL-LGTVIDGMLLLK 312
Cdd:COG2272 230 S--VLTLAEAEAVGAAFAAALGVAPATLA----ALRALPAE---------ELLAAQAALAAEGPGGLpFGPVVDGDVLPE 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      313 TPEELQAERNFHTVPYMVGINKQEFGWLIPML-MSYPLSEGQLDQktamsLLWKSYPlvciakELIPEATEKYLGGTDdt 391
Cdd:COG2272 295 DPLEAFAAGRAADVPLLIGTNRDEGRLFAALLgDLGPLTAADYRA-----ALRRRFG------DDADEVLAAYPAASP-- 361
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      392 vkkKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVigdHGDELFSVFG--APFLKEGASEE 469
Cdd:COG2272 362 ---AEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGLGAF---HGAELPFVFGnlDAPALTGLTPA 435
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2DR0_B      470 EIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEG-YLQIGANTQAAQKLKDKE-VAFWTNLF 532
Cdd:COG2272 436 DRALSDQMQAYWVNFARTGDPNGPGLPEWPAYDPEDRaVMVFDAEPRVVNDPDAEErLDLWDGVV 500
PRK10162 PRK10162
acetyl esterase;
117-205 1.10e-04

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 44.32  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       117 VMVWIHGGGLMVGAASTYDGLA--LAAHENVVVVTIQYRLGIWGFFSTGDEHSrgnwghldqVAALRWVQDNIASFGGNP 194
Cdd:PRK10162  83 TLFYLHGGGFILGNLDTHDRIMrlLASYSGCTVIGIDYTLSPEARFPQAIEEI---------VAVCCYFHQHAEDYGINM 153
                         90
                 ....*....|.
2DR0_B       195 GSVTIFGESAG 205
Cdd:PRK10162 154 SRIGFAGDSAG 164
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
4-528 0e+00

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 634.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B          4 SPPVVDTVHGKVLGKFVSLEGFaQPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQllself 83
Cdd:pfam00135   1 DSPVVTTSLGRVRGKRLKVDGG-KPVYAFLGIPYAEPPVGELRFQPPEPPEPWTGVRDATKFGPRCPQNGDLTS------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B         84 tnrKENIPLKLSEDCLYLNIYTPADLTK-KNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST 162
Cdd:pfam00135  74 ---PGSSGLEGSEDCLYLNVYTPKELKEnKNKLPVMVWIHGGGFMFGSGSLYDGSYLAAEGDVIVVTINYRLGPLGFLST 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        163 GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGD 242
Cdd:pfam00135 151 GDDEAPGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        243 VKpLAEQIAITAGCKTTTSAVMVHCLRQKTEeellettlkMKFLSLDLQGDPRESQPLL--GTVIDGMLLLKTPEELQAE 320
Cdd:pfam00135 231 RQ-RAKELAKLVGCPTSDSAELVECLRSKPA---------EELLDAQLKLLVYGSVPFVpfGPVVDGDFLPEHPEELLKS 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        321 RNFHTVPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAK--ELIPEATEKYL--GGTDDTVKKKD 396
Cdd:pfam00135 301 GNFPKVPLLIGVTKDEGLLFAAYILDNVDILKALEEKLLRSLLIDLLYLLLVDLpeEISAALREEYLdwGDRDDPETSRR 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        397 LFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSsdMKPKTVIGDHGDELFSVFGAPFL-KEGASEEEIRLSK 475
Cdd:pfam00135 381 ALVELLTDYLFNCPVIRFADLHASRGTPVYMYSFDYRGSSL--RYPKWVGVDHGDELPYVFGTPFVgALLFTEEDEKLSR 458
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
2DR0_B        476 MVMKFWANFARNGNPNG-EGLPHWPEYNQKEG-YLQIGANTQAAQKLKDKEVAFW 528
Cdd:pfam00135 459 KMMTYWTNFAKTGNPNGpEGLPKWPPYTDENGqYLSIDLEPRVKQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
7-519 0e+00

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: 595.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        7 VVDTVHGKVLGKFVSlegfaqPVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLselftnr 86
Cdd:cd00312   1 LVVTPNGKVRGVDEG------GVYSFLGIPYAEPPVGDLRFKEPQPYEPWSDVLDATSYPPSCMQWDQLGGGL------- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       87 kENIPLKLSEDCLYLNIYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAA-HENVVVVTIQYRLGIWGFFSTGDE 165
Cdd:cd00312  68 -WNAKLPGSEDCLYLNVYTPKNTKPGNSLPVMVWIHGGGFMFGSGSLYPGDGLAReGDNVIVVSINYRLGVLGFLSTGDI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      166 HSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVALTSVLVKKGdVKP 245
Cdd:cd00312 147 ELPGNYGLKDQRLALKWVQDNIAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQEN-ARG 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      246 LAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLKMKFLSLDLQGdpresqpLLGTVIDGMLLLKTPEELQAERNFHT 325
Cdd:cd00312 226 RAKRLARLLGCNDTSSAELLDCLRSKSAEELLDATRKLLLFSYSPFL-------PFGPVVDGDFIPDDPEELIKEGKFAK 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      326 VPYMVGINKQEFGWLIPMLMSYPLSEGQLDQKTAMSLLwkSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDLIADV 405
Cdd:cd00312 299 VPLIIGVTKDEGGYFAAMLLNFDAKLIIETNDRWLELL--PYLLFYADDALADKVLEKYPGDVDDSVESRKNLSDMLTDL 376
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      406 MFGVPSVIVARNHRDA-GAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPFLKEGASEEEIRLSKMVMKFWANF 484
Cdd:cd00312 377 LFKCPARYFLAQHRKAgGSPVYAYVFDHRSSLSVGRWPPWLGTVHGDEIFFVFGNPLLKEGLREEEEKLSRTMMKYWANF 456
                       490       500       510
                ....*....|....*....|....*....|....*..
2DR0_B      485 ARNGNPNGEG-LPHWPEYN-QKEGYLQIGANTQAAQK 519
Cdd:cd00312 457 AKTGNPNTEGnLVVWPAYTsESEKYLDINIEGTEIKQ 493
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
1-532 1.39e-155

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 453.58  E-value: 1.39e-155
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        1 HPSSPPVVDTVHGKVLGkfVSLEGfaqpVAIFLGIPFAKPPLGPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLS 80
Cdd:COG2272   8 AAAAAPVVRTEAGRVRG--VVEGG----VRVFLGIPYAAPPVGELRWRAPQPVEPWTGVRDATEFGPACPQPPRPGDPGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       81 elftnrkeniPLKLSEDCLYLNIYTPADLTKKnRLPVMVWIHGGGLMVGAAST--YDGLALAAhENVVVVTIQYRLGIWG 158
Cdd:COG2272  82 ----------PAPGSEDCLYLNVWTPALAAGA-KLPVMVWIHGGGFVSGSGSEplYDGAALAR-RGVVVVTINYRLGALG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      159 FF-----STGDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLFHRAISESGVAL 233
Cdd:COG2272 150 FLalpalSGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      234 TsvLVKKGDVKPLAEQIAITAGCKTTTSAvmvhCLRQKTEEellettlkmKFLSLDLQGDPRESQPL-LGTVIDGMLLLK 312
Cdd:COG2272 230 S--VLTLAEAEAVGAAFAAALGVAPATLA----ALRALPAE---------ELLAAQAALAAEGPGGLpFGPVVDGDVLPE 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      313 TPEELQAERNFHTVPYMVGINKQEFGWLIPML-MSYPLSEGQLDQktamsLLWKSYPlvciakELIPEATEKYLGGTDdt 391
Cdd:COG2272 295 DPLEAFAAGRAADVPLLIGTNRDEGRLFAALLgDLGPLTAADYRA-----ALRRRFG------DDADEVLAAYPAASP-- 361
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      392 vkkKDLFLDLIADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVigdHGDELFSVFG--APFLKEGASEE 469
Cdd:COG2272 362 ---AEALAALATDRVFRCPARRLAEAHAAAGAPVYLYRFDWRSPPLRGFGLGAF---HGAELPFVFGnlDAPALTGLTPA 435
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2DR0_B      470 EIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEG-YLQIGANTQAAQKLKDKE-VAFWTNLF 532
Cdd:COG2272 436 DRALSDQMQAYWVNFARTGDPNGPGLPEWPAYDPEDRaVMVFDAEPRVVNDPDAEErLDLWDGVV 500
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
103-206 1.13e-20

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 90.32  E-value: 1.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      103 IYTPADLTKKnrLPVMVWIHGGGLMVGAASTYDGLA--LAAHENVVVVTIQYRLGiwgffstgDEHSrgnW-GHLDQV-A 178
Cdd:COG0657   3 VYRPAGAKGP--LPVVVYFHGGGWVSGSKDTHDPLArrLAARAGAAVVSVDYRLA--------PEHP---FpAALEDAyA 69
                        90       100
                ....*....|....*....|....*...
2DR0_B      179 ALRWVQDNIASFGGNPGSVTIFGESAGG 206
Cdd:COG0657  70 ALRWLRANAAELGIDPDRIAVAGDSAGG 97
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
118-206 1.50e-14

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: 72.63  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        118 MVWIHGGGLMVGAASTYDGLA--LAAHENVVVVTIQYRLgiwgffstGDEHSrgnW--GHLDQVAALRWVQDNIASFGGN 193
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCrrLAAEAGAVVVSVDYRL--------APEHP---FpaAYDDAYAALRWLAEQAAELGAD 69
                          90
                  ....*....|...
2DR0_B        194 PGSVTIFGESAGG 206
Cdd:pfam07859  70 PSRIAVAGDSAGG 82
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
103-232 2.34e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.80  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      103 IYTPADltkKNRLPVMVWIHGGGlmVGAASTYDGLALAAHEN-VVVVTIQYRlgiwgffstGDEHSRGNWGHL---DQVA 178
Cdd:COG1506  14 LYLPAD---GKKYPVVVYVHGGP--GSRDDSFLPLAQALASRgYAVLAPDYR---------GYGESAGDWGGDevdDVLA 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
2DR0_B      179 ALRWVqdnIASFGGNPGSVTIFGESAGGesVSVLVLSPLAKNLFHRAISESGVA 232
Cdd:COG1506  80 AIDYL---AARPYVDPDRIGIYGHSYGG--YMALLAAARHPDRFKAAVALAGVS 128
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
101-206 5.33e-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: 56.42  E-value: 5.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        101 LNIYTPAdlTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENV-----VVVTIQYRLgiwgffsTGDEHSRgnwghlD 175
Cdd:pfam20434   1 LDIYLPK--NAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALlkagyAVASINYRL-------STDAKFP------A 65
                          90       100       110
                  ....*....|....*....|....*....|....*
2DR0_B        176 QV----AALRWVQDNIASFGGNPGSVTIFGESAGG 206
Cdd:pfam20434  66 QIqdvkAAIRFLRANAAKYGIDTNKIALMGFSAGG 100
PRK10162 PRK10162
acetyl esterase;
117-205 1.10e-04

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 44.32  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       117 VMVWIHGGGLMVGAASTYDGLA--LAAHENVVVVTIQYRLGIWGFFSTGDEHSrgnwghldqVAALRWVQDNIASFGGNP 194
Cdd:PRK10162  83 TLFYLHGGGFILGNLDTHDRIMrlLASYSGCTVIGIDYTLSPEARFPQAIEEI---------VAVCCYFHQHAEDYGINM 153
                         90
                 ....*....|.
2DR0_B       195 GSVTIFGESAG 205
Cdd:PRK10162 154 SRIGFAGDSAG 164
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
103-206 3.42e-04

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 42.68  E-value: 3.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      103 IYTPADLTKKNRLPVMVWIHGGGlmvGAASTYD---GL-ALAAHENVVVV----TIQYRLGIWGFFSTGDEHSRGnwGHL 174
Cdd:COG3509  41 LYVPAGYDGGAPLPLVVALHGCG---GSAADFAagtGLnALADREGFIVVypegTGRAPGRCWNWFDGRDQRRGR--DDV 115
                        90       100       110
                ....*....|....*....|....*....|..
2DR0_B      175 DQVAALrwVQDNIASFGGNPGSVTIFGESAGG 206
Cdd:COG3509 116 AFIAAL--VDDLAARYGIDPKRVYVTGLSAGG 145
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
101-235 5.68e-04

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: 41.68  E-value: 5.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B        101 LNIYTPADLTKKNRLPVMVWIHGGGL--MVGAASTYDGLALAAH-ENVVVVTIQY-----RLGIWGFfstGDEHSRGNWG 172
Cdd:pfam00756  10 VQVYLPEDYPPGRKYPVLYLLDGTGWfqNGPAKEGLDRLAASGEiPPVIIVGSPRggevsFYSDWDR---GLNATEGPGA 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2DR0_B        173 H--LDQVAA--LRWVQDNiasFGGNPGSVTIFGESAGGesVSVLVLSPLAKNLFHRAISESGVALTS 235
Cdd:pfam00756  87 YayETFLTQelPPLLDAN---FPTAPDGRALAGQSMGG--LGALYLALKYPDLFGSVSSFSPILNPS 148
COG4099 COG4099
Predicted peptidase [General function prediction only];
75-206 8.29e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 41.11  E-value: 8.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B       75 AGQLLSELFTNRKENIPLKlsedclYlNIYTPADLTKKNRLPVMVWIHGGG---------LMVGAAStYDGLALAAHENV 145
Cdd:COG4099  16 QDGFEARTFTDPSDGDTLP------Y-RLYLPKGYDPGKKYPLVLFLHGAGergtdnekqLTHGAPK-FINPENQAKFPA 87
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2DR0_B      146 VVVTIQYRLGIWgffstgdehsrgnWGHLDQVAAL-RWVQDNIASFGGNPGSVTIFGESAGG 206
Cdd:COG4099  88 IVLAPQCPEDDY-------------WSDTKALDAVlALLDDLIAEYRIDPDRIYLTGLSMGG 136
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
101-230 1.37e-03

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 40.99  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DR0_B      101 LNIYTPADLTKKN-RLPVMVWIHGGGL-------MVGAASTYDGLAlAAHE--NVVVVTIQYRLGiwgffSTGDEHSRGN 170
Cdd:COG2382  97 VWVYLPPGYDNPGkKYPVLYLLDGGGGdeqdwfdQGRLPTILDNLI-AAGKipPMIVVMPDGGDG-----GDRGTEGPGN 170
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2DR0_B      171 WGHLDQVAA--LRWVQDNiASFGGNPGSVTIFGESAGG-ESVSVLVLSPlakNLFHRAISESG 230
Cdd:COG2382 171 DAFERFLAEelIPFVEKN-YRVSADPEHRAIAGLSMGGlAALYAALRHP---DLFGYVGSFSG 229
 
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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