CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Truncated pol protein

Enzyme Information

2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P24740
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
-!- Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a primer which may be DNA or RNA. -!- See also EC 2.7.7.49.
2.7.7.49
RNA-directed DNA polymerase.
based on mapping to UniProt P24740
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of a DNA strand by one deoxynucleotide at a time. -!- Cannot initiate a chain de novo. -!- Requires a RNA or DNA primer. -!- DNA can also serve as template. -!- See also EC 2.7.7.7.
3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P24740
3.1.26.13
Retroviral ribonuclease H.
based on mapping to UniProt P24740
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.
-!- Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. -!- To perform this task the enzyme combines two distinct activities. -!- The polymerase domain (EC 2.7.7.49) occupies the N-terminal two- thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third. -!- The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.
3.1.13.2
Exoribonuclease H.
based on mapping to UniProt P24740
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
-!- This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.
3.4.23.16
HIV-1 retropepsin.
based on mapping to UniProt P24740
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
-!- Present in human immunodeficiency virus type 1. -!- Contributes to the maturation of the viral particle, and is a target of antiviral drugs. -!- Active enzyme is a dimer of identical 11-kDa subunits. -!- Similar enzymes occur in other retroviruses. -!- Belongs to peptidase family A2.
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P24740

UniProtKB Entries (1)

P24740
POL_HV1U4
Human immunodeficiency virus type 1 (STRAIN UGANDAN / ISOLATE U455)
Gag-Pol polyprotein

PDB Structure

PDB 3LZS
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Effect of Clade-Specific Sequence Polymorphisms on HIV-1 Protease Activity and Inhibitor Resistance Pathways.
Bandaranayake, R.M., Kolli, M., King, N.M., Nalivaika, E.A., Heroux, A., Kakizawa, J., Sugiura, W., Schiffer, C.A.
J.Virol.