CATH Classification

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.
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.

UniProtKB Entries (2)

P0CG47
UBB_HUMAN
Homo sapiens
Polyubiquitin-B
Q6TQR6
L_CCHFI
Crimean-Congo hemorrhagic fever virus strain IbAr10200
RNA-directed RNA polymerase L

PDB Structure

PDB 3ZNH
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
On Terminal Alkynes that Can React with Active-Site Cysteine Nucleophiles in Proteases.
Ekkebus, R., Van Kasteren, S.I., Kulathu, Y., Scholten, A., Berlin, I., Geurink, P.P., De Jong, A., Goerdayal, G., Neefjes, J., Heck, A.J.R., Komander, D., Ovaa, H.
J.Am.Chem.Soc.