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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 PRU00863


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00863
General rule information [?]

Accession PRU00863
Dates 10-AUG-2011 (Created)
21-NOV-2019 (Last updated, Version 8)
Data class Domain;
Predictors PROSITE; PS51531; FV_PR
Name Foamy virus protease (FV PR) domain
Function The FV PR domain forms peptidase family A9 (spumapepsin family). Retrovriral PRs belong to the family of aspartic proteases and are active as homodimers, with the active site triplets (Asp-Thr/Ser-Gly; D-T/S-G) from both chain contributing to the symetric active site of the enzyme.
Scope(s) Viruses
Spumavirus
Example(s) P14350;

Propagated annotation [?]

Comments [?]

case <FT:2>
SUBUNITThe protease is a homodimer, whose active site consists of two apposed aspartic acid residues.

Keywords [?]

Aspartyl protease
Hydrolase
Protease
end case

Gene Ontology [?]

GO:0004190; Molecular function:aspartic-type endopeptidase activity
GO:0016787; Molecular function:hydrolase activity
GO:0008233; Molecular function:peptidase activity

Features [?]

From: PS51531
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase A9 #"
ACT_SITE 21 21 /note="For protease activity" D

Additional information [?]

Size range 130-153 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 [?]