CATH Classification

Domain Context

CATH Clusters

Superfamily main proteinase (3clpro) structure, domain 3
Functional Family Replicase polyprotein 1a

Enzyme Information

3.6.4.12
DNA helicase.
based on mapping to UniProt P0C6X7
ATP + H(2)O = ADP + phosphate.
-!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase).
3.6.4.13
RNA helicase.
based on mapping to UniProt P0C6X7
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).
3.1.13.-
Exoribonucleases producing 5'-phosphomonoesters.
based on mapping to UniProt P0C6X7
2.7.7.48
RNA-directed RNA polymerase.
based on mapping to UniProt P0C6X7
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 P0C6X7
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.
3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P0C6X7
2.1.1.-
Methyltransferases.
based on mapping to UniProt P0C6X7
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt P0C6X7
3.4.22.69
SARS coronavirus main proteinase.
based on mapping to UniProt P0C6X7
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
-!- SARS coronavirus main protease is the key enzyme in SARS coronavirus replicase polyprotein processing. -!- Belongs to peptidase family C30.

UniProtKB Entries (1)

P0C6X7
R1AB_CVHSA
Severe acute respiratory syndrome-related coronavirus
Replicase polyprotein 1ab

PDB Structure

PDB 1WOF
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Design of Wide-Spectrum Inhibitors Targeting Coronavirus Main Proteases.
Yang, H., Xie, W., Xue, X., Yang, K., Ma, J., Liang, W., Zhao, Q., Zhou, Z., Pei, D., Ziebuhr, J., Hilgenfeld, R., Yuen, K.Y., Wong, L., Gao, G., Chen, S., Chen, Z., Ma, D., Bartlam, M., Rao, Z.
Plos Biol.