Function and Biology

Crystal structure of nelfinavir (NFV) complexed with a multidrug variant (ACT) (V82T/I84V) of HIV-1 protease

Source organism: HIV-1 M:B_ARV2/SF2
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

EC 3.4.23.16: HIV-1 retropepsin

Reaction catalysed:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Alternative Name(s):
  • Gag protease
  • HIV aspartyl protease
  • HIV proteinase
  • HIV-1 protease
  • HIV-2 protease
  • Human immunodeficiency virus type 1 protease
  • Retroproteinase

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

EC 3.1.13.2: Exoribonuclease H

Reaction catalysed:
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Systematic name:
-

EC 2.7.7.7: DNA-directed DNA polymerase

Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Systematic name:
Deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed)
Alternative Name(s):
  • DNA duplicase
  • DNA nucleotidyltransferase
  • DNA nucleotidyltransferase (DNA-directed)
  • DNA polymerase
  • DNA polymerase I
  • DNA polymerase II
  • DNA polymerase III
  • DNA polymerase alpha
  • DNA polymerase beta
  • DNA polymerase gamma
  • DNA replicase
  • DNA-dependent DNA polymerase
  • Deoxynucleate polymerase
  • Deoxyribonucleate nucleotidyltransferase
  • Deoxyribonucleic acid duplicase
  • Deoxyribonucleic acid polymerase
  • Deoxyribonucleic duplicase
  • Deoxyribonucleic polymerase
  • Deoxyribonucleic polymerase I
  • Duplicase
  • Klenow fragment
  • Sequenase
  • Taq DNA polymerase
  • Taq Pol I
  • Tca DNA polymerase

EC 2.7.7.49: RNA-directed DNA polymerase

Reaction catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Systematic name:
Deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed)
Alternative Name(s):
  • DNA nucleotidyltransferase (RNA-directed)
  • RNA revertase
  • RNA-dependent DNA polymerase
  • RNA-dependent deoxyribonucleate nucleotidyltransferase
  • RNA-instructed DNA polymerase
  • RT
  • Reverse transcriptase
  • Revertase

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. Protease
The deposited structure of PDB entry 3el5 contains 2 copies of Pfam domain PF00077 (Retroviral aspartyl protease) in Protease. Showing 1 copy in chain A.

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

Structure domain

CATH CATH domain
2.40.70.10
Class: Mainly Beta
Architecture: Beta Barrel
Topology: Cathepsin D, subunit A; domain 1
Homology: Acid Proteases
Occurring in:
  1. Protease
The deposited structure of PDB entry 3el5 contains 2 copies of CATH domain 2.40.70.10 (Cathepsin D, subunit A; domain 1) in Protease. Showing 1 copy in chain A.