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:
hetero trimer (preferred)
Assembly name:
Protease and peptide (preferred)
PDBe Complex ID:
PDB-CPX-136874 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protease
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.75 KDa
Source organism: Human immunodeficiency virus 1
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.75 KDa
Source organism: Human immunodeficiency virus 1
UniProt:
- Canonical:
P03369 (Residues: 491-589; Coverage: 7%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Protease
Molecule details ›
Chain: B
Length: 99 amino acids
Theoretical weight: 10.73 KDa
Source organism: Human immunodeficiency virus 1
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.73 KDa
Source organism: Human immunodeficiency virus 1
UniProt:
- Canonical: P03369 (Residues: 491-589; Coverage: 7%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
