Function and Biology Details
Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Protease (preferred)
PDBe Complex ID:
PDB-CPX-138017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Reverse transcriptase/ribonuclease H
Molecule details ›
Chains: A, B
Length: 560 amino acids
Theoretical weight: 64.56 KDa
Source organism: HIV-1 M:B_HXB2R
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 560 amino acids
Theoretical weight: 64.56 KDa
Source organism: HIV-1 M:B_HXB2R
Expression system: Escherichia coli
UniProt:
- Canonical:
P04585 (Residues: 588-1147; Coverage: 39%)
Sequence domains:
- Reverse transcriptase (RNA-dependent DNA polymerase)
- Reverse transcriptase thumb domain
- Reverse transcriptase connection domain
- RNase H
