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.
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.
ProRule PRU00870
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU00870
General rule information
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| Accession | PRU00870 |
| Dates | 09-AUG-2011 (Created)
21-NOV-2019 (Last updated, Version 7) |
| Data class | Domain; |
| 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. |
| Scope(s) |
Viruses Norovirus |
| Example(s) | P54634; |
Propagated annotation
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Identifier, protein and gene names
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| case <FTGroup:1> | |
| Protein name | + Contains: RecName: Full=3C-like protease; Short=3CLpro; EC=3.4.22.66; |
Comments
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| 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 | |
Keywords
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| Hydrolase | |
| Protease | |
| Thiol protease | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0008234; Molecular function:cysteine-type peptidase activity | |
| GO:0016787; Molecular function:hydrolase activity | |
| GO:0008233; Molecular function:peptidase activity | |
Features
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| From: PS51537 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Peptidase C37 #" | |||||||||
| ACT_SITE | 30 | 30 | /note="For 3CLpro activity" | H | 1 | |||||||
| ACT_SITE | 54 | 54 | /note="For 3CLpro activity" | E | 1 | |||||||
| ACT_SITE | 139 | 139 | /note="For 3CLpro activity" | C | 1 | |||||||
Additional information
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| Size range | 171-191 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
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
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- UniProtKB/Swiss-Prot sets
Viruses [4] All [ 4 ]
- Retrieve set of proteins with 3D structure for this domain