CATH Domain 4gw6A00

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	POL polyprotein

Enzyme Information

2.7.7.7	DNA-directed DNA polymerase. based on mapping to UniProt P12497 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.
3.1.13.2	Exoribonuclease H. based on mapping to UniProt P12497 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.
3.4.23.16	HIV-1 retropepsin. based on mapping to UniProt P12497 Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. -!- Present in human immunodeficiency virus type 1. -!- Contributes to the maturation of the viral particle, and is a target of antiviral drugs. -!- Active enzyme is a dimer of identical 11-kDa subunits. -!- Similar enzymes occur in other retroviruses. -!- Belongs to peptidase family A2.
3.1.26.13	Retroviral ribonuclease H. based on mapping to UniProt P12497 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.
2.7.7.-	Nucleotidyltransferases. based on mapping to UniProt P12497
2.7.7.49	RNA-directed DNA polymerase. based on mapping to UniProt P12497 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 P12497

UniProtKB Entries (1)

POL_HV1N5

Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)

Gag-Pol polyprotein

PDB Structure

PDB	4GW6
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors. Feng, L., Sharma, A., Slaughter, A., Jena, N., Koh, Y., Shkriabai, N., Larue, R.C., Patel, P.A., Mitsuya, H., Kessl, J.J., Engelman, A., Fuchs, J.R., Kvaratskhelia, M. J.Biol.Chem.