CATH Classification

Domain Context

CATH Clusters

Superfamily Cysteine proteinases
Functional Family Genome polyprotein

Enzyme Information

2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P03305
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.
3.6.1.15
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P03305
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 P03305
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 P03305
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)

P03305
POLG_FMDVO
Foot-and-mouth disease virus (strain O1)
Genome polyprotein

PDB Structure

PDB 4QBB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Foot-and-mouth disease virus leader proteinase: Structural insights into the mechanism of intermolecular cleavage.
Steinberger, J., Grishkovskaya, I., Cencic, R., Juliano, L., Juliano, M.A., Skern, T.
Virology