CATH Classification

Domain Context

CATH Clusters

Superfamily Ribonuclease H-like superfamily/Ribonuclease H
Functional Family Pro-Pol polyprotein

Enzyme Information

3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P14350
3.4.23.-
Aspartic endopeptidases.
based on mapping to UniProt P14350
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P14350
2.7.7.49
RNA-directed DNA polymerase.
based on mapping to UniProt P14350
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.
3.1.26.4
Ribonuclease H.
based on mapping to UniProt P14350
Endonucleolytic cleavage to 5'-phosphomonoester.
-!- Acts on RNA-DNA hybrids.
2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P14350
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.

UniProtKB Entries (1)

P14350
POL_FOAMV
Human spumaretrovirus
Pro-Pol polyprotein

PDB Structure

PDB 3OYE
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance.
Hare, S., Vos, A.M., Clayton, R.F., Thuring, J.W., Cummings, M.D., Cherepanov, P.
Proc.Natl.Acad.Sci.USA