CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Gag-Pro-Pol polyprotein

Enzyme Information

3.4.23.-
Aspartic endopeptidases.
based on mapping to UniProt P03362
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P03362
3.1.26.4
Ribonuclease H.
based on mapping to UniProt P03362
Endonucleolytic cleavage to 5'-phosphomonoester.
-!- Acts on RNA-DNA hybrids.
2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P03362
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 P03362
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 P03362

UniProtKB Entries (1)

P03362
POL_HTL1A
Human T-cell lymphotrophic virus type 1 (strain ATK)
Gag-Pro-Pol polyprotein

PDB Structure

PDB 2B7F
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of human T cell leukemia virus protease, a novel target for anticancer drug design
Li, M., Laco, G.S., Jaskolski, M., Rozycki, J., Alexandratos, J., Wlodawer, A., Gustchina, A.
Proc.Natl.Acad.Sci.Usa