CATH Classification

Domain Context

CATH Clusters

Superfamily 2.60.120.20
Functional Family Genome polyprotein

Enzyme Information

3.6.1.15
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.
3.4.22.46
L-peptidase.
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.
3.4.22.28
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.
2.7.7.48
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 2.7.7.6.

UniProtKB Entries (1)

P03306
POLG_FMDV1
Foot-and-mouth disease virus (strain A10-61)
Genome polyprotein

PDB Structure

PDB 1ZBE
External Links
Method X-RAY DIFFRACTION
Organism
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.
J.Gen.Virol.
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