PROSITE documentation PDOC51531Foamy virus protease (FV PR) domain profile
Spumaviruses or foamy viruses (FVs) are a group of complex retroviruses that have been isolated from a number of animal species and are believed to be apathogenic in their animal host [E1]. FVs express a pol-specific transcript that codes for a Pol polyprotein that consists of the protease (PR), reverse transcriptase, robonuclease H , and the integrase domains. 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. Transient FV PR domain homodimers are formed under native condition but are only present as a minor transient species, which is not detectable by traditional methods. Dimerization of FV RT might be triggered by additional viral or cellular factors [1,2,3,4]. The FV PR domain forms peptidase family A9 (spumapepsin family) [E2].
The FV PR domain consists of seven β-strands and a helical turn (see <pdb:2JYS>). The β-strands form a closed barrel-like β-sheet with the strand order β1-β2-β7-β3-β6-β5-β1. The strands β1 and β7 are arranged in parallel, while all other strands are arranged in an anti-parallel manner [3].
The profile we developed covers the entire FV PR domain.
Last update:March 2011 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Konvalinka J. Loechelt M. Zentgraf H. Fluegel R.M. Kraeusslich H.-G. |
| Title | Active foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein. | |
| Source | J. Virol. 69:7264-7268(1995). | |
| PubMed ID | 7474150 |
| 2 | Authors | Pfrepper K.-I. Rackwitz H.-R. Schnoelzer M. Heid H. Loechelt M. Fluegel R.M. |
| Title | Molecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease. | |
| Source | J. Virol. 72:7648-7652(1998). | |
| PubMed ID | 9696869 |
| 3 | Authors | Hartl M.J. Woehrl B.M. Roesch P. Schweimer K. |
| Title | The solution structure of the simian foamy virus protease reveals a monomeric protein. | |
| Source | J. Mol. Biol. 381:141-149(2008). | |
| PubMed ID | 18597783 | |
| DOI | 10.1016/j.jmb.2008.05.064 |
| 4 | Authors | Hartl M.J. Schweimer K. Reger M.H. Schwarzinger S. Bodem J. Rosch P. Wohrl B.M. |
| Title | Formation of transient dimers by a retroviral protease. | |
| Source | Biochem. J. 427:197-203(2010). | |
| PubMed ID | 20136635 | |
| DOI | 10.1042/BJ20091451 |
| E1 | Title | https://viralzone.expasy.org/10?outline=all_by_protein |
| E2 | Title | https://www.ebi.ac.uk/merops/cgi-bin/famsum?family=A9 |
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