Literature summary for 3.4.23.B11 extracted from

Lee, E.; Roy, J.; Jackson, D.; Clark, P.; Boyer, P.; Hughes, S.; Linial, M.
Foamy retrovirus integrase contains a pol dimerization domain required for protease activation (2011), J. Virol., 85, 1655-1661.

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Protein Variants

Protein Variants	Comment	Organism
additional information	a Pol mutant lacking the integrase domain has defects in protease activity and Pol packaging into virions. Introduction of a leucine zipper dimerization motif, zip, in an integrase truncation mutant can restore protease activity, leading to Pol processing in cells. However, these zip mutants neither cleave Gag nor incorporate Pol into virions. The integrase domain may be required for Pol dimerization, which is necessary for the creation of a functional protease active site	Simian foamy virus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
87500	-	x * 87500, HPLC followed by light scattering	Simian foamy virus

Organism

Organism	UniProt	Comment	Textmining
Simian foamy virus	-	chimpanzee foamy virus	-

Subunits

Subunits	Comment	Organism
monomer	x * 87500, HPLC followed by light scattering	Simian foamy virus

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Release 2023.1 (January 2023)