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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 PRU00167


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00167
General rule information [?]

Accession PRU00167
Dates 12-DEC-2003 (Created)
20-MAR-2025 (Last updated, Version 8)
Data class Domain;
Predictors PROSITE; PS50018; RAS_GTPASE_ACTIV_2
Name Ras-GAP domain
Function Ras proteins are membrane-associated molecular switches that bind GTP and GDP and slowly hydrolyze GTP to GDP. This intrinsic GTPase activity of ras is stimulated by a family of proteins collectively known as 'GAP' or GTPase-activating proteins. The key residue for GAP-mediated catalysis is the so-called "arginine finger".
Scope(s) Eukaryota
Example(s) P21359;

Propagated annotation [?]

Keywords [?]

GTPase activation
end case

Gene Ontology [?]

case <Feature:PS50018:26=R>
GO:0005096; Molecular function:GTPase activator activity

Cross-references [?]

PROSITE PS00509; RAS_GTPASE_ACTIV_1; 1;

Features [?]

From: PS50018
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Ras-GAP #"
SITE 26 26 /note="Arginine finger; crucial for GTP hydrolysis by stabilizing the transition state" R

Additional information [?]

Size range 190-234 amino acids
Related rules None
Fusion None
Repeats 1
Topology Undefined

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 [?]