CATH Classification

Domain Context

CATH Clusters

Superfamily Trypsin-like serine proteases
Functional Family

Enzyme Information

3.4.22.44
Nuclear-inclusion-a endopeptidase.
based on mapping to UniProt P04517
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
-!- The potyviruses cause diseases in plants, and inclusion bodies appear in the host cell nuclei, protein a of these being the endopeptidase. -!- The enzyme finds practical use when encoded in vectors for the artificial expression of recombinant fusion proteins, since it can confer on them the capacity for autolytic cleavage. -!- It is also reported that transgenic plants expressing the enzyme are resistant to viral infection. -!- Belongs to peptidase family C4.
3.4.22.45
Helper-component proteinase.
based on mapping to UniProt P04517
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
-!- Known from many potyviruses. -!- The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities. -!- The N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. -!- Belongs to peptidase family C6.
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P04517
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.-.-
Acting on peptide bonds (peptidases).
based on mapping to UniProt P04517
3.6.4.-
Acting on ATP; involved in cellular and subcellular movement.
based on mapping to UniProt P04517

UniProtKB Entries (1)

P04517
POLG_TEV
Tobacco etch virus
Genome polyprotein

PDB Structure

PDB 1Q31
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of tobacco etch virus protease shows the protein C terminus bound within the active site.
Nunn, C.M., Jeeves, M., Cliff, M.J., Urquhart, G.T., George, R.R., Chao, L.H., Tscuchia, Y., Djordjevic, S.
J.Mol.Biol.