CATH Classification

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.
Lea, S., Hernandez, J., Blakemore, W., Brocchi, E., Curry, S., Domingo, E., Fry, E., Abu-Ghazaleh, R., King, A., Newman, J., Stuart, D., Mateu, M.G.
Structure