General rule information
[?]
Accession |
PRU00870 |
Dates |
9-AUG-2011 (Created) 21-NOV-2019 (Last updated, Version 6) |
Predictors |
PROSITE; PS51537; NV_3CL_PRO
|
Name |
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. |
Propagated annotation
[?]
case <FTGroup:1>
+ Contains:
RecName: Full=3C-like protease;
Short=3CLpro;
EC 3.4.22.66; |
Function |
3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave polyadenylate-binding protein thereby inhibiting cellular translation. |
Catalytic activity |
Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-|-Xaa and the P1' position is occupied by Gly-|-Yaa.; EC=3.4.22.66; |
Ptm |
Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro is first autocatalytically cleaved, then processes the whole polyprotein. |
end case
case <FTGroup:1>
GO:0008234; Molecular function: cysteine-type peptidase activity.
GO:0016787; Molecular function: hydrolase activity.
GO:0008233; Molecular function: peptidase activity.
end case
From: PS51537 |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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DOMAIN
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from
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to
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Peptidase C37 #
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ACT_SITE
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30
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30
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For 3CLpro activity
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H
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1
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ACT_SITE
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54
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54
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For 3CLpro activity
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E
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1
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ACT_SITE
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139
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139
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For 3CLpro activity
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C
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1
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Additional information
[?]
Size range |
171-191 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
P54634 (POLG_LORDV) |
Scope |
Viruses; Norovirus |
Comments |
None |
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
[?]