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
2.7.7.49
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.
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P14350

UniProtKB Entries (1)

P14350
POL_FOAMV
Human spumaretrovirus
Pro-Pol polyprotein

PDB Structure

PDB 2LSN
External Links
Method SOLUTION NMR
Organism
Primary Citation
The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.
Leo, B., Schweimer, K., Rosch, P., Hartl, M.J., Wohrl, B.M.
Retrovirology
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