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 |
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 | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Structural basis for functional tetramerization of lentiviral integrase
Plos Pathog.
|