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.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Reverse transcriptase/ribonuclease H (preferred)
PDBe Complex ID:
PDB-CPX-145699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Reverse transcriptase/ribonuclease H
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 14.78 KDa
Source organism: Equine infectious anemia virus
Expression system: Escherichia coli
UniProt:
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
Length: 134 amino acids
Theoretical weight: 14.78 KDa
Source organism: Equine infectious anemia virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P11204 (Residues: 742-875; Coverage: 12%)
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
R32
Expression system: Escherichia coli
