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
| 2.7.7.49 |
RNA-directed DNA polymerase.
based on mapping to UniProt P16088
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.
|
| 3.1.13.2 |
Exoribonuclease H.
based on mapping to UniProt P16088
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 P16088
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.- |
Aspartic endopeptidases.
based on mapping to UniProt P16088
|
| 3.6.1.23 |
dUTP diphosphatase.
based on mapping to UniProt P16088
dUTP + H(2)O = dUMP + diphosphate.
|
| 3.1.-.- |
Acting on ester bonds.
based on mapping to UniProt P16088
|
| 2.7.7.- |
Nucleotidyltransferases.
based on mapping to UniProt P16088
|
UniProtKB Entries (1)
| P16088 |
POL_FIVPE
Feline immunodeficiency virus (isolate Petaluma)
Pol polyprotein
|
PDB Structure
| PDB | 5FIV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease
Proteins
|