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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 PRU01025


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01025
General rule information [?]

Accession PRU01025
Dates 26-AUG-2014 (Created)
22-NOV-2019 (Last updated, Version 9)
Data class Domain;
Predictors PROSITE; PS51688; ICA
Name Intramolecular chaperone auto-processing (ICA) domain
Function The Intramolecular Chaperone Auto-processing (ICA)] domain, also called Intramolecuar Chaperone Domain (ICD) or C-terminal Intramolecular Chaperone Domain (CIMCD), is capable of catalyzing trimerization-dependent auto-proteolysis. The ICA domain contains two absolutely conserved serine and lysine residues. They form a catalytic dyad that mediates cleavage at the serine residue. The ICA domain belongs to peptidase family S74.
Scope(s) Eukaryota
Viruses
Example(s) Q9Y2G1;

Propagated annotation [?]

Keywords [?]

case <FTGroup:1>
Autocatalytic cleavage
end case

Features [?]

From: PS51688
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase S74 #"
SITE 1-1 1 /note="Cleavage; by autolysis" P-S 1

Additional information [?]

Size range 88-238 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 [?]