CATH Classification

Domain Context

CATH Clusters

Superfamily Leucine Aminopeptidase, subunit E, domain 1
Functional Family Orf1a polyprotein

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).
3.4.22.69
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.
3.1.-.-
Acting on ester bonds.
based on mapping to UniProt P0C6X7
3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt P0C6X7
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.
2.1.1.-
Methyltransferases.
based on mapping to UniProt P0C6X7

UniProtKB Entries (1)

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

PDB Structure

PDB 2ACF
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose-1''-phosphate dephosphorylation by a conserved domain of nsP3.
Saikatendu, K.S., Joseph, J.S., Subramanian, V., Clayton, T., Griffith, M., Moy, K., Velasquez, J., Neuman, B.W., Buchmeier, M.J., Stevens, R.C., Kuhn, P.
Structure