CATH Classification

Domain Context

CATH Clusters

Superfamily 1.20.960.20
Functional Family Genome polyprotein

Enzyme Information

3.4.22.46
L-peptidase.
based on mapping to UniProt P03311
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.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P03311
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.
3.4.22.28
Picornain 3C.
based on mapping to UniProt P03311
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 P03311
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.

UniProtKB Entries (1)

P03311
POLG_FMDVS
Foot-and-mouth disease virus (strain C1-Santa Pau)
Genome polyprotein

PDB Structure

PDB 4X2B
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Multifunctionality of a picornavirus polymerase domain: nuclear localization signal and nucleotide recognition.
Ferrer-Orta, C., de la Higuera, I., Caridi, F., Sanchez-Aparicio, M.T., Moreno, E., Perales, C., Singh, K., Sarafianos, S.G., Sobrino, F., Domingo, E., Verdaguer, N.
J.Virol.