CATH Classification

Domain Context

CATH Clusters

Functional Family Genome polyprotein

Enzyme Information
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P03306
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.
based on mapping to UniProt P03306
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.
RNA-directed RNA polymerase.
based on mapping to UniProt P03306
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
Picornain 3C.
based on mapping to UniProt P03306
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.

UniProtKB Entries (1)

Foot-and-mouth disease virus (strain A10-61)
Genome polyprotein

PDB Structure

External Links
Primary Citation
Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation.
Fry, E.E., Newman, J.W., Curry, S., Najjam, S., Jackson, T., Blakemore, W., Lea, S.M., Miller, L., Burman, A., King, A.M., Stuart, D.I.