ProRule PRU00863
General rule information
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| PURL | https://purl.expasy.org/prosite/rule/PRU00863 |
| Accession | PRU00863 |
| Dates | 10-AUG-2011 (Created)
21-NOV-2019 (Last updated, Version 7) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51531; FV_PR |
Name | Foamy virus protease (FV PR) domain |
| Function | The FV PR domain forms peptidase family A9 (spumapepsin family). Retrovriral PRs belong to the family of aspartic proteases and are active as homodimers, with the active site triplets (Asp-Thr/Ser-Gly; D-T/S-G) from both chain contributing to the symetric active site of the enzyme. |
| Scope(s) |
Viruses Spumavirus |
| Example(s) | P14350 (POL_FOAMV); |
Propagated annotation
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Comments
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| case <FT:2> | |
| SUBUNIT | The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. |
Keywords
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| Aspartyl protease | |
| Hydrolase | |
| Protease | |
| end case | |
Gene Ontology
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| GO:0004190; Molecular function:aspartic-type endopeptidase activity |
| GO:0016787; Molecular function:hydrolase activity |
| GO:0008233; Molecular function:peptidase activity |
Features
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| From: PS51531 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="Peptidase A9 #" | |||||||||
| ACT_SITE | 21 | 21 | /note="For protease activity" | D | ||||||||
Additional information
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| Size range | 130-153 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 [5] All [ 5 ]
- Retrieve set of proteins with 3D structure for this domain