CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Pro-Pol polyprotein

Enzyme Information

2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P23074
2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P23074
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 P23074
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 P23074
3.4.23.-
Aspartic endopeptidases.
based on mapping to UniProt P23074
3.1.26.4
Ribonuclease H.
based on mapping to UniProt P23074
Endonucleolytic cleavage to 5'-phosphomonoester.
-!- Acts on RNA-DNA hybrids.

UniProtKB Entries (1)

P23074
POL_SFV1
Macaque simian foamy virus
Pro-Pol polyprotein

PDB Structure

PDB 2JYS
External Links
Method SOLUTION NMR
Organism
Primary Citation
The solution structure of the simian foamy virus protease reveals a monomeric protein
Hartl, M.J., Woehrl, B.M., Roesch, P., Schweimer, K.
J.Mol.Biol.