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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Amos Bairoch

ProRule PRU00240


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00240
General rule information [?]

Accession PRU00240
Dates 12-DEC-2003 (Created)
19-NOV-2022 (Last updated, Version 14)
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;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1> and <Feature:PS50141:27=E>
Protein name + RecName: EC=3.5.4.-;
end case

Keywords [?]

Hydrolase
end case
case <FTGroup:1>
Metal-binding
Zinc
end case

Gene Ontology [?]

case <FTGroup:1> and <Feature:PS50141:27=E>
GO:0016787; Molecular function:hydrolase activity

Features [?]

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 [?]

Size range 325-367 amino acids
Related rules None
Fusion None
Repeats 1
Topology Not cytoplasmic

Copyright

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 [?]