Cloned (Comment) | Organism |
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Macaque simian foamy virus |
Protein Variants | Comment | Organism |
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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 | UniProt | Comment | Textmining |
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Macaque simian foamy virus | - |
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