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Conserved domains on  [gi|1808670914|ref|NP_001365360|]
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epoxide hydrolase 1 isoform d [Homo sapiens]

Protein Classification

epoxide hydrolase( domain architecture ID 10534184)

epoxide hydrolase catalyzes the conversion of epoxides to trans-dihydrodiols, thus preventing or reducing their reaction with cellular macromolecules such as protein or DNA; epoxide hydrolase such as juvenile hormone epoxide hydrolase, which catalyzes juvenile hormone hydrolysis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
48-124 2.66e-32

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


:

Pssm-ID: 461913  Cd Length: 106  Bit Score: 117.18  E-value: 2.66e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1808670914  48 IRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGFN 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWYGVPLDYLRELVDYWRDGYDWRAQEARLNSFPQFTTEIDGLD 77
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
121-328 9.47e-18

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam00561:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 245  Bit Score: 81.78  E-value: 9.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 121 EGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMAlvLSNFSTLTLLLGQRFGRFLGLTE 200
Cdd:pfam00561  48 DDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 201 RDVELLYPVKEKVFYSLMRESGYMHIQCTK--PDTVGSALNDS---PVGLAAYILEKFSTWTNTEFRYLedgglerkfsL 275
Cdd:pfam00561 126 GFVADFAPNPLGRLVAKLLALLLLRLRLLKalPLLNKRFPSGDyalAKSLVTGALLFIETWSTELRAKF----------L 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1808670914 276 DDLLTNVMLYWTTGTIISSQRfYKENLGQGWmtqKHERMKVYVPTGFSAFPFE 328
Cdd:pfam00561 196 GRLDEPTLIIWGDQDPLVPPQ-ALEKLAQLF---PNARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
48-124 2.66e-32

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


Pssm-ID: 461913  Cd Length: 106  Bit Score: 117.18  E-value: 2.66e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1808670914  48 IRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGFN 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWYGVPLDYLRELVDYWRDGYDWRAQEARLNSFPQFTTEIDGLD 77
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
121-328 9.47e-18

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 81.78  E-value: 9.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 121 EGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMAlvLSNFSTLTLLLGQRFGRFLGLTE 200
Cdd:pfam00561  48 DDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 201 RDVELLYPVKEKVFYSLMRESGYMHIQCTK--PDTVGSALNDS---PVGLAAYILEKFSTWTNTEFRYLedgglerkfsL 275
Cdd:pfam00561 126 GFVADFAPNPLGRLVAKLLALLLLRLRLLKalPLLNKRFPSGDyalAKSLVTGALLFIETWSTELRAKF----------L 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1808670914 276 DDLLTNVMLYWTTGTIISSQRfYKENLGQGWmtqKHERMKVYVPTGFSAFPFE 328
Cdd:pfam00561 196 GRLDEPTLIIWGDQDPLVPPQ-ALEKLAQLF---PNARLVVIPDAGHFAFLEG 244
 
Name Accession Description Interval E-value
EHN pfam06441
Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic ...
48-124 2.66e-32

Epoxide hydrolase N terminus; This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organizms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.


Pssm-ID: 461913  Cd Length: 106  Bit Score: 117.18  E-value: 2.66e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1808670914  48 IRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGFN 124
Cdd:pfam06441   1 IRPFTIHVPDEELDDLRQRLALTRWPDELEGDDWWYGVPLDYLRELVDYWRDGYDWRAQEARLNSFPQFTTEIDGLD 77
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
121-328 9.47e-18

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


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 81.78  E-value: 9.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 121 EGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMAlvLSNFSTLTLLLGQRFGRFLGLTE 200
Cdd:pfam00561  48 DDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGA--LDPPHELDEADRFILALFPGFFD 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1808670914 201 RDVELLYPVKEKVFYSLMRESGYMHIQCTK--PDTVGSALNDS---PVGLAAYILEKFSTWTNTEFRYLedgglerkfsL 275
Cdd:pfam00561 126 GFVADFAPNPLGRLVAKLLALLLLRLRLLKalPLLNKRFPSGDyalAKSLVTGALLFIETWSTELRAKF----------L 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1808670914 276 DDLLTNVMLYWTTGTIISSQRfYKENLGQGWmtqKHERMKVYVPTGFSAFPFE 328
Cdd:pfam00561 196 GRLDEPTLIIWGDQDPLVPPQ-ALEKLAQLF---PNARLVVIPDAGHFAFLEG 244
 
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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