CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
4 | Few Secondary Structures |
|
4.10 | Irregular |
|
4.10.90 | Foot-And-Mouth Disease Virus, subunit 4 |
|
4.10.90.10 | Capsid protein VP4 superfamily, Picornavirus |
Domain Context
CATH Clusters
| Superfamily | Capsid protein VP4 superfamily, Picornavirus |
| Functional Family | Genome polyprotein |
Enzyme Information
| 3.4.22.28 |
Picornain 3C.
based on mapping to UniProt P12296
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
-!- From entero-, rhino-, aphto- and cardioviruses. -!- Larger than the homologous virus picornain 2A. -!- Belongs to peptidase family C3.
|
| 2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P12296
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.
|
| 3.6.4.13 |
RNA helicase.
based on mapping to UniProt P12296
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).
|
UniProtKB Entries (1)
| P12296 |
POLG_ENMGO
Mengo virus
Genome polyprotein
|
PDB Structure
| PDB | 1MEC |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly.
Virology
|
