Literature summary for 2.7.7.49 extracted from

Schneider, A.; Peter, D.; Schmitt, J.; Leo, B.; Richter, F.; Roesch, P.; Woehrl, B.M.; Hartl, M.J.
Structural requirements for enzymatic activities of foamy virus protease-reverse transcriptase (2014), Proteins, 82, 375-385.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Macaque simian foamy virus

Protein Variants

Protein Variants	Comment	Organism
additional information	introduction of N- and C-terminal deletions into simian foamy virus proteaase-reverse transcriptase. Both, the RNase H domain and the connection subdomain contribute substantially to polymerase integrity and stability as well as to polymerase activity and substrate binding. The 42 amino acids long region C-terminal of the protease domain is important for polymerase stability and activity. Protease activation via binding of PR-RT to viral RNA requires the presence of the full length virus proteaase-reverse transcriptase including the RNase H domain. Deletions either at the C- or N-terminus of protease-reverse transcriptase disturb the structural integrity of the proteins. Isolated reverse transcriptase domains RT(107-454) and PR-RT(1-454) exhibit very little polymerization and extension activity	Macaque simian foamy virus

Organism

Organism	UniProt	Comment	Textmining
Macaque simian foamy virus	-	-	-

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Release 2023.1 (January 2023)