CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1840 | main proteinase (3clpro) structure, domain 3 |
|
1.10.1840.10 | main proteinase (3clpro) structure, domain 3 |
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
|
| 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.
|
| 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
|
UniProtKB Entries (1)
| P0C6X7 |
R1AB_CVHSA
Severe acute respiratory syndrome-related coronavirus
Replicase polyprotein 1ab
|
PDB Structure
| PDB | 2Z9L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis of mercury- and zinc-conjugated complexes as SARS-CoV 3C-like protease inhibitors.
Febs Lett.
|
