AC   PRU00870;
DC   Domain;
TR   PROSITE; PS51537; NV_3CL_PRO; 1; level=0
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Names: Norovirus 3C-like protease (NV 3CLpro) domain
Function: NV 3CLpros belong to the chymotrypsin-like protease family, in that
 they appear to have chymotrypsin-like folds. Whether the 3CLpro domain has a
 catalytic dyad of composed of histidine and cysteine or tryad of histidine,
 glutamate and cysteine remains controversial.
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case <FTGroup:1>
DE   + Contains:
DE       RecName: Full=3C-like protease;
DE                Short=3CLpro;
DE                EC=3.4.22.66;
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CC   -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp is
CC       first released by autocleavage, then all other proteins are cleaved.
CC       May cleave polyadenylate-binding protein thereby inhibiting cellular
CC       translation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase with a preference for cleavage when the P1
CC         position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC         Gly-|-Yaa.; EC=3.4.22.66;
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro
CC       is first autocatalytically cleaved, then processes the whole
CC       polyprotein.
end case
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case <FTGroup:1>
GO   GO:0008234; F:cysteine-type peptidase activity
GO   GO:0016787; F:hydrolase activity
GO   GO:0008233; F:peptidase activity
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KW   Hydrolase
KW   Protease
KW   Thiol protease
end case
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FT   From: PS51537
FT   DOMAIN          from..to
FT                   /note="Peptidase C37 #"
FT   ACT_SITE        30
FT                   /note="For 3CLpro activity"
FT   Group: 1; Condition: H
FT   ACT_SITE        54
FT                   /note="For 3CLpro activity"
FT   Group: 1; Condition: E
FT   ACT_SITE        139
FT                   /note="For 3CLpro activity"
FT   Group: 1; Condition: C
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Chop: Nter=0; Cter=0;
Size: 171-191;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: P54634;
Scope:
 Viruses; Norovirus
Comments: None;
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# Revision 1.6 2019/11/21
//