Literature summary for 3.1.26.13 extracted from

Ghosh, M.; Howard, K.J.; Cameron, C.E.; Benkovic, S.J.; Hughes, S.H.; Le Grice, S.F.
Truncating alpha-helix E of p66 human immunodeficiency virus reverse transcriptase modulates RNase H function and impairs DNA strand transfer (1995), J. Biol. Chem., 270, 7068-7076.

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Protein Variants

Protein Variants	Comment	Organism
G544Stop	C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected	Human immunodeficiency virus 1
P537Stop	C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected	Human immunodeficiency virus 1
V552Stop	C-terminal truncation of p66 polypeptide. Mutant retains endonuclease activity but lacks the directional processing feature of wild-type and barely supports transfer of nascent (-)-stranded DNA between RNA templates	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	-	-	-

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Release 2023.1 (January 2023)