CATH Domain 1hvhA00

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.70	Cathepsin D, subunit A; domain 1
	2.40.70.10	Acid Proteases

Domain Context

CATH Clusters

Superfamily	Acid Proteases
Functional Family	Gag-Pol polyprotein

Enzyme Information

2.7.7.49	RNA-directed DNA polymerase. based on mapping to UniProt P04585 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.
2.7.7.-	Nucleotidyltransferases. based on mapping to UniProt P04585
2.7.7.7	DNA-directed DNA polymerase. based on mapping to UniProt P04585 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 P04585
3.1.13.2	Exoribonuclease H. based on mapping to UniProt P04585 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 P04585 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.
3.4.23.16	HIV-1 retropepsin. based on mapping to UniProt P04585 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.

UniProtKB Entries (1)

POL_HV1H2

HIV-1 M:B_HXB2R

Gag-Pol polyprotein

PDB Structure

PDB	1HVH
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Nonpeptide cyclic cyanoguanidines as HIV-1 protease inhibitors: synthesis, structure-activity relationships, and X-ray crystal structure studies. Jadhav, P.K., Woerner, F.J., Lam, P.Y., Hodge, C.N., Eyermann, C.J., Man, H.W., Daneker, W.F., Bacheler, L.T., Rayner, M.M., Meek, J.L., Erickson-Viitanen, S., Jackson, D.A., Calabrese, J.C., Schadt, M., Chang, C.H. J.Med.Chem.