Function and Biology

CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE

Source organism: Human immunodeficiency virus 1
Biochemical function: nucleic acid binding
Biological process: DNA integration
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

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 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 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

InterPro InterPro annotations
IPR012337
Domain description: Ribonuclease H-like superfamily
Occurring in:
  1. Integrase
IPR038965
Domain description: Transposase InsF-like
Occurring in:
  1. Integrase
IPR001584
Domain description: Integrase, catalytic core
Occurring in:
  1. Integrase
IPR036397
Domain description: Ribonuclease H superfamily
Occurring in:
  1. Integrase

Structure domain

CATH CATH domain
3.30.420.10
Class: Alpha Beta
Architecture: 2-Layer Sandwich
Topology: Nucleotidyltransferase; domain 5
Homology: Ribonuclease H-like superfamily/Ribonuclease H
Occurring in:
  1. Integrase
1 copy of CATH domain 3.30.420.10 (Nucleotidyltransferase; domain 5) in Integrase in PDB 1bhl.
SCOP SCOP annotation
53107
Class: Alpha and beta proteins (a/b)
Fold: Ribonuclease H-like motif
Superfamily: Ribonuclease H-like
Occurring in:
  1. Integrase
1 copy of SCOP domain 53107 (Retroviral integrase, catalytic domain) in Integrase in PDB 1bhl.