Function and Biology

Apo-crystal structure of a wild-type South African HIV-1 subtype C protease at 2.4 angstrom

Source organism: Human immunodeficiency virus 1
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

EC 3.1.26.13: Retroviral ribonuclease H

Reaction catalysed:
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.
Systematic name:
-
Alternative Name(s):
  • HIV RNase H
  • RT/RNase H
  • Retroviral reverse transcriptase RNaseH

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00077
Domain description: Retroviral aspartyl protease
Occurring in:
  1. Truncated pol polyprotein
The deposited structure of PDB entry 8ci7 contains 1 copy of Pfam domain PF00077 (Retroviral aspartyl protease) in Truncated pol polyprotein. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR021109
Domain description: Aspartic peptidase domain superfamily
Occurring in:
  1. Truncated pol polyprotein
IPR001969
Domain description: Aspartic peptidase, active site
Occurring in:
  1. Truncated pol polyprotein
IPR001995
Domain description: Peptidase A2A, retrovirus, catalytic
Occurring in:
  1. Truncated pol polyprotein
IPR034170
Domain description: Retropepsin-like catalytic domain
Occurring in:
  1. Truncated pol polyprotein
IPR018061
Domain description: Retropepsins
Occurring in:
  1. Truncated pol polyprotein