CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.90 | Alpha-Beta Complex | |
3.90.70 | Cathepsin B; Chain A | |
3.90.70.80 |
Domain Context
CATH Clusters
Superfamily | 3.90.70.80 |
Functional Family | RNA-directed RNA polymerase L |
Enzyme Information
2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt Q6TQR6
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.
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3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q6TQR6
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.
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UniProtKB Entries (1)
Q6TQR6 |
L_CCHFI
Crimean-Congo hemorrhagic fever virus strain IbAr10200
RNA-directed RNA polymerase L
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PDB Structure
PDB | 5V5G |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants.
PLoS Pathog.
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