CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.10 | Thrombin, subunit H | |
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
Superfamily | Trypsin-like serine proteases |
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.
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UniProtKB Entries (1)
P0C6X7 |
R1AB_CVHSA
Severe acute respiratory syndrome-related coronavirus
Replicase polyprotein 1ab
|
PDB Structure
PDB | 5B6O |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
SARS-CoV 3CL protease cleaves its C-terminal autoprocessing site by novel subsite cooperativity
Proc. Natl. Acad. Sci. U.S.A.
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