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 P49303
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.
|
3.6.1.15 |
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P49303
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.
|
2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P49303
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.
|
3.4.22.46 |
L-peptidase.
based on mapping to UniProt P49303
Autocatalytically cleaves itself from the polyprotein of the foot- and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
-!- Best known from foot-and-mouth disease virus, but occurs in other aphthoviruses and cardioviruses. -!- Destruction of initiation factor eIF-4G has the effect of shutting off host-cell protein synthesis while allowing synthesis of viral proteins to continue. -!- The tertiary structure reveals a distant relationship to papain and, consistent with this, compound E-64 is inhibitory. -!- Belongs to peptidase family C28.
|
UniProtKB Entries (3)
Q65095 |
Q65095_9PICO
Foot-and-mouth disease virus
Foot and mouth disease virus VP1 capsid protein
|
P49303 |
POLG_FMDVZ
Foot-and-mouth disease virus A22/550/Azerbaijan/65
Genome polyprotein
|
P15072 |
POLG_FMDVT
Foot-and-mouth disease virus C1
Genome polyprotein
|
PDB Structure
PDB | 1FMD |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Mesocricetus |
Primary Citation |
The structure and antigenicity of a type C foot-and-mouth disease virus.
Structure
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