CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.70.270
Functional Family Gag-Pol polyprotein

Enzyme Information

2.7.7.7
DNA-directed DNA polymerase.
based on mapping to UniProt P03355
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.
3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P03355
3.1.26.4
Ribonuclease H.
based on mapping to UniProt P03355
Endonucleolytic cleavage to 5'-phosphomonoester.
-!- Acts on RNA-DNA hybrids.
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P03355
3.4.23.-
Aspartic endopeptidases.
based on mapping to UniProt P03355
2.7.7.49
RNA-directed DNA polymerase.
based on mapping to UniProt P03355
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.

UniProtKB Entries (1)

P03355
POL_MLVMS
Moloney murine leukemia virus isolate Shinnick
Gag-Pol polyprotein

PDB Structure

PDB 1D0E
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structures of an N-terminal fragment from Moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: functional implications for template-primer binding to the fingers domain
Najmudin, S., Cote, M.L., Sun, D., Yohannan, S., Montano, S.P., Gu, J., Georgiadis, M.M.
J.Mol.Biol.