CATH Domain 5uoqB00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.420	Nucleotidyltransferase; domain 5
	3.30.420.10	Ribonuclease H-like superfamily/Ribonuclease H

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)

POL_FOAMV

Human spumaretrovirus

Pro-Pol polyprotein

PDB Structure

PDB	5UOQ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Discovery and optimization of 2-pyridinone aminal integrase strand transfer inhibitors for the treatment of HIV. Schreier, J.D., Embrey, M.W., Raheem, I.T., Barbe, G., Campeau, L.C., Dubost, D., McCabe Dunn, J., Grobler, J., Hartingh, T.J., Hazuda, D.J., Klein, D., Miller, M.D., Moore, K.P., Nguyen, N., Pajkovic, N., Powell, D.A., Rada, V., Sanders, J.M., Sisko, J., Steele, T.G., Wai, J., Walji, A., Xu, M., Coleman, P.J. Bioorg. Med. Chem. Lett.