CATH Classification

Domain Context

CATH Clusters

Superfamily Cysteine proteinases
Functional Family

Enzyme Information
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
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.
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.
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)

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

PDB Structure

External Links
Organism Escherichia
Primary Citation
Investigating the Substrate Specificity and Oligomerisation of the Leader Protease of Foot and Mouth Disease Virus using NMR
Cencic, R., Mayer, C., Juliano, M.A., Juliano, L., Konrat, R., Kontaxis, G., Skern, T.