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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 PRU01222


View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01222
General rule information [?]

Accession PRU01222
Dates 18-JAN-2019 (Created)
22-NOV-2019 (Last updated, Version 4)
Data class Domain;
Predictors PROSITE; PS51874; PCV_3C_PRO
Name Picornavirales 3C/3C-like protease domain
Function The 3C (for the family Picornaviridae) or 3C-like (3CL) protease (for other families) plays a central role in the cleavage of the viral precursor polyprotein. In addition to its key role in processing the polyprotein, 3C/3C-like protease is able to cleave a number of host proteins to remodel the cellular environment for virus reproduction.
Scope(s) Viruses
Riboviria
Example(s) P06209;

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTGroup:1> or <FTGroup:2>
Protein name Contains:
RecName: Full=Protease 3C;
                 EC=3.4.22.28;
AltName: Full=Picornain 3C;
                 Short=P3C;
else case <FTGroup:3>
Protein name Contains:
RecName: Full=Picornain 3C-like protease;
                 EC=3.4.22.-;
                 Short=3C-like protease;
else case <FTGroup:4>
Protein name Contains:
RecName: Full=3C-like protease;
                 EC=3.4.22.-;
                 Short=3CL-PRO;
end case

Comments [?]

case <FTGroup:1> or <FTGroup:2>
CATALYTIC ACTIVITY Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
end case

Keywords [?]

Hydrolase
Protease
Thiol protease
end case

Gene Ontology [?]

case <FTGroup:1> or <FTGroup:2> or <FTGroup:3> or <FTGroup:4>
GO:0004197; Molecular function:cysteine-type endopeptidase activity

Features [?]

From: PS51874
Key From To Description Tag Condition FTGroup
DOMAIN from to /note="Peptidase C3 #"
case <OS:Foot-and-mouth disease virus>
ACT_SITE 41 41 /note="For protease 3C activity; Proton donor/acceptor" H 1
ACT_SITE 78 78 /note="For protease 3C activity" [ED] 1
ACT_SITE 164 164 /note="For protease 3C activity" C 1
else case <OC:Picornaviridae>
ACT_SITE 41 41 /note="For protease 3C activity" H 2
ACT_SITE 78 78 /note="For protease 3C activity" [ED] 2
ACT_SITE 164 164 /note="For protease 3C activity" C 2
else case <OC:Picornavirales>
ACT_SITE 41 41 /note="For picornain 3C-like protease activity" H 3
ACT_SITE 78 78 /note="For picornain 3C-like protease activity" [ED] 3
ACT_SITE 164 164 /note="For picornain 3C-like protease activity" C 3
else
ACT_SITE 41 41 /note="For 3C-like protease activity" H 4
ACT_SITE 78 78 /note="For 3C-like protease activity" [ED] 4
ACT_SITE 164 164 /note="For 3C-like protease activity" C 4
end case

Additional information [?]

Size range 170-250 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 [?]