PROSITE documentation PDOC51531
Foamy 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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

FV_PR, PS51531; Foamy virus protease (FV PR) domain profile  (MATRIX)


1AuthorsKonvalinka J. Loechelt M. Zentgraf H. Fluegel R.M. Kraeusslich H.-G.
TitleActive foamy virus proteinase is essential for virus infectivity but not for formation of a Pol polyprotein.
SourceJ. Virol. 69:7264-7268(1995).
PubMed ID7474150

2AuthorsPfrepper K.-I. Rackwitz H.-R. Schnoelzer M. Heid H. Loechelt M. Fluegel R.M.
TitleMolecular characterization of proteolytic processing of the Pol proteins of human foamy virus reveals novel features of the viral protease.
SourceJ. Virol. 72:7648-7652(1998).
PubMed ID9696869

3AuthorsHartl M.J. Woehrl B.M. Roesch P. Schweimer K.
TitleThe solution structure of the simian foamy virus protease reveals a monomeric protein.
SourceJ. Mol. Biol. 381:141-149(2008).
PubMed ID18597783

4AuthorsHartl M.J. Schweimer K. Reger M.H. Schwarzinger S. Bodem J. Rosch P. Wohrl B.M.
TitleFormation of transient dimers by a retroviral protease.
SourceBiochem. J. 427:197-203(2010).
PubMed ID20136635



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