CATH Classification

Domain Context

CATH Clusters

Superfamily 2.70.40.10
Functional Family Pol polyprotein

Enzyme Information

3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P11204
2.7.7.-
Nucleotidyltransferases.
based on mapping to UniProt P11204
2.7.7.49
RNA-directed DNA polymerase.
based on mapping to UniProt P11204
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.
3.4.23.-
Aspartic endopeptidases.
based on mapping to UniProt P11204
3.1.13.2
Exoribonuclease H.
based on mapping to UniProt P11204
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.
-!- This is a secondary reaction to the RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end performed by EC 3.1.26.13.
3.1.26.13
Retroviral ribonuclease H.
based on mapping to UniProt P11204
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
-!- Retroviral reverse transcriptase is a multifunctional enzyme responsible for viral replication. -!- To perform this task the enzyme combines two distinct activities. -!- The polymerase domain (EC 2.7.7.49) occupies the N-terminal two- thirds of the reverse transcriptase whereas the ribonuclease H domain comprises the C-terminal remaining one-third. -!- The RNase H domain of Moloney murine leukemia virus and Human immunodeficiency virus display two metal binding sites.

UniProtKB Entries (1)

P11204
POL_EIAV9
Equine infectious anemia virus (CLONE 1369)
Pol polyprotein

PDB Structure

PDB 1DUN
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex.
Dauter, Z., Persson, R., Rosengren, A.M., Nyman, P.O., Wilson, K.S., Cedergren-Zeppezauer, E.S.
J.Mol.Biol.