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.
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
Protease (preferred)
PDBe Complex ID:
PDB-CPX-147605 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Molecule details ›
Chains: A, B
Length: 133 amino acids
Theoretical weight: 14.37 KDa
Source organism: Feline immunodeficiency virus (isolate Petaluma)
Expression system: Trichoplusia ni
UniProt:
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
Length: 133 amino acids
Theoretical weight: 14.37 KDa
Source organism: Feline immunodeficiency virus (isolate Petaluma)
Expression system: Trichoplusia ni
UniProt:
- Canonical:
P16088 (Residues: 711-843; Coverage: 12%)
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
