Protein Variants | Comment | Organism |
---|---|---|
K476C | the mutation disrupts the chemical cross-linking while maintaining activity | Human immunodeficiency virus 1 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | required for the cross-linking of the modified substrate to RNase H | Human immunodeficiency virus 1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA-RNA hybrid duplex + H2O | Human immunodeficiency virus 1 | - |
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Human immunodeficiency virus 1 | - |
HIV-1 | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid | two activities are present in the reverse transcriptase: polymerase and RNase H. RNase H is required for removal of the viral RNA, primer formation and removal for the synthesis of the (+) strand DNA, and specific removal of the primer tRNA used in the synthesis of the (-) strand DNA. | Human immunodeficiency virus 1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DNA-RNA hybrid duplex + H2O | - |
Human immunodeficiency virus 1 | oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety | - |
? | |
DNA-RNA hybrid duplex + H2O | the RNase H domain of reverse transcriptase catalyses the cleavage of the RNA within DNA-RNA hybrids, both in a polymerase-dependent or independent fashion. Polymerase-dependent: Cleavage occurring at a distance of 18-20 nucleotides behind DNA polymerization. Polymerase-independent: cleavage of the viral RNA for the initiation of second DNA strand synthesis and for removal of the primer tRNA. | Human immunodeficiency virus 1 | oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety | - |
? |