Function for haloacid dehalogenase-like hydrolase domain containing 2: Difference between revisions
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GO Annotations in Tabular Form | |||
{| border="1" cellspacing="0" cellpadding="5" | {| border="1" cellspacing="0" cellpadding="5" | ||
! Category | ! Category | ||
! Classification | ! Classification | ||
! Term Evidence | ! Term Evidence | ||
! Inferred From | |||
! Ref(s) | |||
|- | |- | ||
| | | Molecular | ||
| | | Function catalytic | ||
| | | activity | ||
| | | IEA | ||
| | | InterPro:IPR005834 | ||
| J:72247 | |||
|- | |- | ||
| | | Molecular Function | ||
| | | hydrolase activity | ||
| | | IEA | ||
| | | InterPro:IPR006357 | ||
| | | J:72247 | ||
|- | |||
| Molecular Function | |||
| hydrolase activity | |||
| IEA | |||
| SP_KW:KW-0378 | |||
| J:60000 | |||
|- | |||
| Molecular Function | |||
| magnesium ion binding | |||
| IEA | |||
| SP_KW:KW-0460 | |||
| J:60000 | |||
|- | |||
| Biological Process | |||
| metabolic process | |||
| IEA | |||
| InterPro:IPR005834,InterPro:IPR006357 | |||
| J:72247 | |||
|- | |- | ||
|} | |} | ||
(pre) | |||
Gene Ontology Evidence Code Abbreviations: | Gene Ontology Evidence Code Abbreviations: | ||
IEA | |||
IC Inferred by curator | |||
IDA Inferred from direct assay | |||
IEA Inferred from electronic annotation | |||
IGI Inferred from genetic interaction | |||
IMP Inferred from mutant phenotype | |||
IPI Inferred from physical interaction | |||
ISS Inferred from sequence or structural similarity | |||
NAS Non-traceable author statement | |||
ND No biological data available | |||
RCA Reviewed computational analysis | |||
TAS Traceable author statement | |||
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Revision as of 05:47, 5 June 2007
Haloacid dehalogenase-like hydrolase domain containing 2 (2HO4:A,B)
Where's does this name come from?
Hydolase indicates it's main molecular function, hydrolase activity. /Link
Definition of hydrolase activity:
Catalysis of the hydrolysis of various bonds
e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
Hydrolase is the systematic name for any enzyme of EC class 3.
The name Domain containing 2 illustrate it has 2 domains
Sequence and Secondary Structure /Link
From the above diagram, we see 2 domains color in blue and purple showed separately.
Type: polypeptide(L)
Length: 259 residues
Secondary Structure: 44% helical (14 helices; 123 residues) 17% beta sheet (12 strands; 48 residues)
2HO4Aa: pdp domain 2HO4Aa (in purple)
2HO4Ab: pdp domain 2HO4Ab (in blue)
But this does not conclude all it's function
Protein Data Bank (PDB)
Ligands and Prosthetic Groups
ID | Name Chemical | Formula | Weight Ligand | Link |
---|---|---|---|---|
PO4 | Phosphate Ion | O4 P 3- | 94.971 | /View |
MG | Magnesium Ion | Mg 2+ | 24.305 | /View |
MSE | Selenomethionine | C5 H11 N O2 Se | 196.107 | /View |
/PBD Biology and Chemistry Report
Mouse Genome Informatics(MGI)
/Gene Ontology Classifications
We found 5 Category of Function or Process with evidence.
GO Annotations in Tabular Form
Category | Classification | Term Evidence | Inferred From | Ref(s) | |
---|---|---|---|---|---|
Molecular | Function catalytic | activity | IEA | InterPro:IPR005834 | J:72247 |
Molecular Function | hydrolase activity | IEA | InterPro:IPR006357 | J:72247 | |
Molecular Function | hydrolase activity | IEA | SP_KW:KW-0378 | J:60000 | |
Molecular Function | magnesium ion binding | IEA | SP_KW:KW-0460 | J:60000 | |
Biological Process | metabolic process | IEA | InterPro:IPR005834,InterPro:IPR006357 | J:72247 |