CATH Classification

Domain Context

CATH Clusters

Superfamily 2.60.120.20
Functional Family Genome polyprotein

Enzyme Information

2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt Q155Z9
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.
3.6.4.13
RNA helicase.
based on mapping to UniProt Q155Z9
ATP + H(2)O = ADP + phosphate.
-!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).
3.4.22.28
Picornain 3C.
based on mapping to UniProt Q155Z9
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.
3.4.19.12
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q155Z9
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.

UniProtKB Entries (1)

Q155Z9
POLG_SVV1
Seneca Valley virus USA/SSV-001
Genome polyprotein

PDB Structure

PDB 3CJI
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of Seneca Valley Virus-001: an oncolytic picornavirus representing a new genus
Venkataraman, S., Reddy, S.P., Loo, J., Idamakanti, N., Hallenbeck, P.L., Reddy, V.S.
Structure
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