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ProRule PRU00275
General rule information
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Accession | PRU00275 |
Dates | 12-DEC-2003 (Created)
21-NOV-2019 (Last updated, Version 20) |
Data class | Domain; |
Predictors |
PROSITE; PS50175; ASP_PROT_RETROV |
Name | Eukaryotic and viral aspartyl proteases |
Function | Belongs to peptidase family A2 |
Scope(s) |
Eukaryota Viruses |
Example(s) | P51518 (PRO_SRV2); |
Propagated annotation
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Identifier, protein and gene names
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case <OS:Human immunodeficiency virus 1> and <FTTag:act_site> | |
Protein name | + RecName: EC=3.4.23.16; |
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site> | |
Protein name | + RecName: EC=3.4.23.47; |
else case <FTTag:act_site> | |
Protein name | + RecName: EC=3.4.23.-; |
end case |
Comments
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case <OS:Human immunodeficiency virus 1> | |
FUNCTION | The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles. |
else case <OC:Retroviridae> | |
FUNCTION | The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. |
end case | |
case <OS:Human immunodeficiency virus 1> and <FTTag:act_site> | |
CATALYTIC ACTIVITY | Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; |
else case <OS:Human immunodeficiency virus 2> and <FTTag:act_site> | |
CATALYTIC ACTIVITY | Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; |
end case |
Keywords
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Aspartyl protease | |
Hydrolase | |
Protease | |
end case |
Gene Ontology
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case <FTTag:act_site> | |
GO:0004190; Molecular function:aspartic-type endopeptidase activity | |
GO:0016787; Molecular function:hydrolase activity | |
GO:0008233; Molecular function:peptidase activity |
Cross-references
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PROSITE | PS00141; ASP_PROTEASE; 1; |
Features
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From: PS50175 | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
DOMAIN | from | to | /note="Peptidase A2 #" | |||||||||
case <OC:Retroviridae> | ||||||||||||
ACT_SITE | 6 | 6 | /note="Protease; shared with dimeric partner" | act_site | D | |||||||
else | ||||||||||||
ACT_SITE | 6 | 6 | /note="@TARGET_ACTIVITY_VISIBILITY|For protease activity@" | act_site | D | |||||||
end case |
Additional information
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Size range | 40-82 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
Eukaryota [28] Viruses [142] All [ 170 ]
- Retrieve set of proteins with 3D structure for this domain