CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.110 | Alphavirus nsP2 protease domain |
Domain Context
CATH Clusters
| Superfamily | Alphavirus nsP2 protease domain |
| Functional Family |
Enzyme Information
| 2.7.7.- |
Nucleotidyltransferases.
based on mapping to UniProt P27282
|
| 2.1.1.- |
Methyltransferases.
based on mapping to UniProt P27282
|
| 2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P27282
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
-!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.
|
| 3.4.22.- |
Cysteine endopeptidases.
based on mapping to UniProt P27282
|
| 3.6.4.13 |
RNA helicase.
based on mapping to UniProt P27282
ATP + H(2)O = ADP + phosphate.
-!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).
|
| 3.1.3.33 |
Polynucleotide 5'-phosphatase.
based on mapping to UniProt P27282
A 5'-phosphopolynucleotide + H(2)O = a polynucleotide + phosphate.
-!- Does not act on nucleoside monophosphates. -!- Induced in Escherichia coli by T-even phages.
|
| 3.1.3.84 |
ADP-ribose 1''-phosphate phosphatase.
based on mapping to UniProt P27282
ADP-D-ribose 1''-phosphate + H(2)O = ADP-D-ribose + phosphate.
-!- The enzyme is highly specific for ADP-D-ribose 1''-phosphate. -!- Involved together with EC 3.1.4.37 in the breakdown of adenosine diphosphate ribose 1'',2''-cyclic phosphate (Appr>p), a by-product of tRNA splicing. -!- Formerly EC 3.1.3.n2.
|
| 2.7.7.19 |
Polynucleotide adenylyltransferase.
based on mapping to UniProt P27282
ATP + RNA(n) = diphosphate + RNA(n+1).
-!- Also acts slowly with CTP. -!- Catalyzes template-independent extension of the 3'-end of a DNA strand by one nucleotide at a time. -!- Cannot initiate a chain de novo. -!- The primer, depending on the source of the enzyme, may be an RNA or DNA fragment or oligo(A) bearing a 3'-OH terminal group. -!- See also EC 2.7.7.6.
|
| 3.6.1.15 |
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P27282
NTP + H(2)O = NDP + phosphate.
-!- The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. -!- Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD. -!- The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
|
UniProtKB Entries (1)
| P27282 |
POLN_EEVVT
Venezuelan equine encephalitis virus (strain Trinidad donkey)
Polyprotein P1234
|
PDB Structure
| PDB | 5EZS |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Kinetic, Mutational, and Structural Studies of the Venezuelan Equine Encephalitis Virus Nonstructural Protein 2 Cysteine Protease.
Biochemistry
|
