Function and Biology

STRUCTURE OF THE FMDV LEADER PROTEASE

Source organism: Foot-and-mouth disease virus (strain O1)
Biochemical function: cysteine-type endopeptidase activity
Biological process: viral protein processing
Cellular component: not assigned

EC 3.6.1.15: Nucleoside-triphosphate phosphatase

Reaction catalysed:
NTP + H(2)O = NDP + phosphate
Systematic name:
Unspecific diphosphate phosphohydrolase
Alternative Name(s):
  • NTPase
  • Nucleoside 5-triphosphatase
  • Nucleoside triphosphate hydrolase
  • Nucleoside triphosphate phosphohydrolase
  • Nucleoside-5-triphosphate phosphohydrolase
  • Nucleoside-triphosphatase

EC 3.4.22.46: L-peptidase

Reaction catalysed:
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-.
Systematic name:
-

EC 3.4.22.28: Picornain 3C

Reaction catalysed:
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.
Alternative Name(s):
  • 3C protease
  • 3C proteinase
  • Coxsackievirus 3C proteinase
  • Cysteine proteinase 3C
  • Foot-and-mouth protease 3C
  • Foot-and-mouth-disease virus proteinase 3C
  • Hepatitis A virus 3C proteinase
  • Picornavirus endopeptidase 3C
  • Poliovirus protease 3C
  • Poliovirus proteinase 3C
  • Protease 3C
  • Rhinovirus protease 3C
  • Rhinovirus proteinase 3C
  • Tomato ringspot nepovirus 3C-related protease

EC 2.7.7.48: RNA-directed RNA polymerase

Reaction catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Systematic name:
Nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Alternative Name(s):
  • 3D polymerase
  • PB1 proteins
  • PB2 proteins
  • Phage f2 replicase
  • Polymerase L
  • Q-beta replicase
  • RDRP
  • RNA nucleotidyltransferase (RNA-directed)
  • RNA replicase
  • RNA synthetase
  • RNA transcriptase
  • RNA-dependent RNA polymerase
  • RNA-dependent RNA replicase
  • RNA-dependent ribonucleate nucleotidyltransferase
  • Ribonucleic acid replicase
  • Ribonucleic acid-dependent ribonucleate nucleotidyltransferase
  • Ribonucleic acid-dependent ribonucleic acid polymerase
  • Ribonucleic replicase
  • Ribonucleic synthetase
  • Transcriptase

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF05408
Domain description: Foot-and-mouth virus L-proteinase
Occurring in:
  1. Leader protease
The deposited structure of PDB entry 1qol contains 8 copies of Pfam domain PF05408 (Foot-and-mouth virus L-proteinase) in Leader protease. Showing 1 copy in chain C.

InterPro InterPro annotations
IPR008739
Domain description: Peptidase C28, foot-and-mouth virus L-proteinase
Occurring in:
  1. Leader protease
IPR038765
Domain description: Papain-like cysteine peptidase superfamily
Occurring in:
  1. Leader protease

Structure domain

CATH CATH domain
3.90.70.10
Class: Alpha Beta
Architecture: Alpha-Beta Complex
Topology: Cathepsin B; Chain A
Homology: Cysteine proteinases
Occurring in:
  1. Leader protease
The deposited structure of PDB entry 1qol contains 8 copies of CATH domain 3.90.70.10 (Cathepsin B; Chain A) in Leader protease. Showing 1 copy in chain C.
SCOP SCOP annotation
54037
Class: Alpha and beta proteins (a+b)
Fold: Cysteine proteinases
Superfamily: Cysteine proteinases
Occurring in:
  1. Leader protease
The deposited structure of PDB entry 1qol contains 8 copies of SCOP domain 54037 (FMDV leader protease) in Leader protease. Showing 1 copy in chain C.