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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 PRU00881


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00881
General rule information [?]

Accession PRU00881
Dates 23-MAR-2012 (Created)
21-NOV-2019 (Last updated, Version 5)
Data class Domain;
Predictors PROSITE; PS51548; BIRNAVIRUS_VP4_PRO
Name Birnavirus VP4 protease domain
Function The birnavirus VP4 protease domain displays a catalytic serine/ lysine dyad in its active site.
Scope(s) Viruses
Birnaviridae
Example(s) P22351;

Propagated annotation [?]

Comments [?]

case <FTGroup:1>
FUNCTIONProtease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation.
end case

Keywords [?]

Hydrolase
Protease
Serine protease
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0016787; Molecular function:hydrolase activity
GO:0008233; Molecular function:peptidase activity
GO:0008236; Molecular function:serine-type peptidase activity

Features [?]

From: PS51548
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase S50 #"
ACT_SITE 125 125 /note="Nucleophile" S 1
ACT_SITE 163 163 K 1

Additional information [?]

Size range 972-1069 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 [?]