CATH Domain 3hphB01

×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.10	Orthogonal Bundle
	1.10.10	Arc Repressor Mutant, subunit A
	1.10.10.200	Integrase, N-terminal zinc-binding domain

Domain Context

CATH Clusters

Superfamily	1.10.10.200
Functional Family

Enzyme Information

2.7.7.-	Nucleotidyltransferases. based on mapping to UniProt P35956
3.4.23.-	Aspartic endopeptidases. based on mapping to UniProt P35956
3.6.1.23	dUTP diphosphatase. based on mapping to UniProt P35956 dUTP + H(2)O = dUMP + diphosphate.
3.1.13.2	Exoribonuclease H. based on mapping to UniProt P35956 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.
2.7.7.49	RNA-directed DNA polymerase. based on mapping to UniProt P35956 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 P35956 Endonucleolytic cleavage to 5'-phosphomonoester. -!- Acts on RNA-DNA hybrids.
3.1.-.-	Acting on ester bonds. based on mapping to UniProt P35956
2.7.7.7	DNA-directed DNA polymerase. based on mapping to UniProt P35956 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.

UniProtKB Entries (2)

O75475	PSIP1_HUMAN Homo sapiens PC4 and SFRS1-interacting protein
P35956	POL_VILVK Visna/maedi virus EV1 KV1772 Gag-Pol polyprotein

PDB Structure

PDB	3HPH
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Structural basis for functional tetramerization of lentiviral integrase Hare, S., Di Nunzio, F., Labeja, A., Wang, J., Engelman, A., Cherepanov, P. Plos Pathog.