CATH Domain 2jqgR00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.70	Cathepsin B; Chain A
	3.90.70.10	Cysteine proteinases

Domain Context

CATH Clusters

Superfamily	Cysteine proteinases
Functional Family

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)

POLG_FMDVO

Foot-and-mouth disease virus (strain O1)

Genome polyprotein

PDB Structure

PDB	2JQG
External Links	PDBSum Proteopedia
Method	SOLUTION NMR
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. J.Mol.Biol.