ProRule PRU01166
General rule information
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Accession | PRU01166 |
Dates | 28-NOV-2016 (Created)
1-MAR-2024 (Last updated, Version 10) |
Data class | Domain; |
Predictors |
PROSITE; PS51822; HV_PV_NS3_PRO |
Name | Hepacivirus/Pegivirus NS3 protease domain |
Function | The NS3/A4 protease is not only essential for generating mature viral proteins required for viral replication, but also hydrolyzes proteins, which are part of the innate immune system, thereby confounding the innate immune response to viral infection. |
Scope(s) |
Viruses Hepacivirus |
Example(s) | Q9WMX2 (POLG_HCVCO); |
Propagated annotation
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Identifier, protein and gene names
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case <FTGroup:1> | |
Protein name | Contains: RecName: Full=Serine protease NS3; EC=3.4.21.98; AltName: Full=Hepacivirin; AltName: Full=NS3P; AltName: Full=p70; |
end case | |
case <FTGroup:1> and <AnyFeature:PS51192> and <AnyFeature:PS51194> |
Comments
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FUNCTION | NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS. |
end case | |
case <FTGroup:1> | |
CATALYTIC ACTIVITY | Reaction=Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.; EC=3.4.21.98; |
end case | |
case <FTGroup:2> | |
COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per NS3 protease domain; |
end case | |
case <FTGroup:1> and <AnyFeature:PS51693> | |
ACTIVITY REGULATION | Activity of auto-protease NS2-3 is dependent on zinc ions and completely inhibited by EDTA. Serine protease NS3 is also activated by zinc ions. |
end case | |
case <FTGroup:1> and <AnyFeature:PS51192> and <AnyFeature:PS51194> | |
DOMAIN | The N-terminal one-third of serine protease NS3 contains the protease activity. This region contains a zinc atom that does not belong to the active site, but may play a structural rather than a catalytic role. This region is essential for the activity of protease NS2-3, maybe by contributing to the folding of the latter. The helicase activity is located in the C-terminus of NS3. |
end case |
Keywords
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Gene Ontology
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case <FTGroup:2> | |
GO:0008270; Molecular function:zinc ion binding | |
end case | |
case <FTGroup:1> | |
GO:0004252; Molecular function:serine-type endopeptidase activity | |
GO:0039502; Biological process:symbiont-mediated suppression of host type I interferon-mediated signaling pathway | |
GO:0039545; Biological process:symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity | |
end case |
Features
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From: PS51822 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | /note="Peptidase S29 #" | |||||||||
ACT_SITE | 57 | 57 | /note="Charge relay system; for serine protease NS3 activity" | H | 1 | |||||||
ACT_SITE | 81 | 81 | /note="Charge relay system; for serine protease NS3 activity" | D | 1 | |||||||
ACT_SITE | 139 | 139 | /note="Charge relay system; for serine protease NS3 activity" | S | 1 | |||||||
BINDING | 97 | 97 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 2 | |||||||
BINDING | 99 | 99 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 2 | |||||||
BINDING | 145 | 145 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 2 | |||||||
BINDING | 149 | 149 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 2 |
Additional information
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Size range | 172-192 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 [33] All [ 33 ]
- Retrieve set of proteins with 3D structure for this domain