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.
Endonucleolytic cleavage to 5'-phosphomonoester.
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Ribonuclease HI, p15 (preferred)
PDBe Complex ID:
PDB-CPX-138003 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI; p15
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 16.92 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
Length: 150 amino acids
Theoretical weight: 16.92 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P04585 (Residues: 1014-1093, 1105-1148; Coverage: 9%) - Canonical: P0A7Y4 (Residues: 79-103; Coverage: 16%)
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
