ProRule PRU00240
General rule information
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Accession | PRU00240 |
Dates | 12-DEC-2003 (Created)
19-NOV-2022 (Last updated, Version 13) |
Data class | Domain; |
Predictors |
PROSITE; PS50141; A_DEAMIN_EDITASE |
Name | Adenosine to inosine editase domain |
Function | Enzymes that catalyze the site-selective deamination of adenosine residue into inosine within double stranded regions of mRNA. |
Scope(s) |
Eukaryota |
Example(s) | Q99MU3 (DSRAD_MOUSE); |
Propagated annotation
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Identifier, protein and gene names
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case <FTGroup:1> and <Feature:PS50141:27=E> | |
Protein name | + RecName: EC=3.5.4.-; |
end case |
Keywords
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Hydrolase | |
end case | |
case <FTGroup:1> | |
Metal-binding | |
Zinc | |
end case |
Gene Ontology
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case <FTGroup:1> and <Feature:PS50141:27=E> | |
GO:0016787; Molecular function:hydrolase activity |
Features
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From: PS50141 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | /note="A to I editase #" | |||||||||
BINDING | 25 | 25 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
ACT_SITE | 27 | 27 | /note="Proton donor" | E | ||||||||
BINDING | 81 | 81 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 149 | 149 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 |
Additional information
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Size range | 325-367 amino acids |
Related rules |
None |
Fusion | None |
Repeats | 1 |
Topology | Not cytoplasmic |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [29] All [ 29 ]
- Retrieve set of proteins with 3D structure for this domain