CATH Domain 1jldA00

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

Enzyme Information

3.1.-.-	Acting on ester bonds. based on mapping to UniProt P04584
3.1.13.2	Exoribonuclease H. based on mapping to UniProt P04584 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.
2.7.7.7	DNA-directed DNA polymerase. based on mapping to UniProt P04584 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.
3.4.23.47	HIV-2 retropepsin. based on mapping to UniProt P04584 Endopeptidase for which the P1 residue is preferably hydrophobic. -!- Responsible for the post-translational processing of the human immunodeficiency virus polyprotein. -!- Belongs to peptidase family A2.
2.7.7.-	Nucleotidyltransferases. based on mapping to UniProt P04584
3.1.26.13	Retroviral ribonuclease H. based on mapping to UniProt P04584 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.
2.7.7.49	RNA-directed DNA polymerase. based on mapping to UniProt P04584 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)

POL_HV2RO

Human immunodeficiency virus type 2 (ISOLATE ROD)

Gag-Pol polyprotein

PDB Structure

PDB	1JLD
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Potent HIV protease inhibitors containing a novel (hydroxyethyl)amide isostere. Beaulieu, P.L., Wernic, D., Abraham, A., Anderson, P.C., Bogri, T., Bousquet, Y., Croteau, G., Guse, I., Lamarre, D., Liard, F., Paris, W., Thibeault, D., Pav, S., Tong, L. J.Med.Chem.