CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.10 | Roll | 
|   | 3.10.20 | Ubiquitin-like (UB roll) | 
|   | 3.10.20.540 | Papain-like viral protease, N-terminal domain | 
Domain Context
CATH Clusters
| Superfamily | 3.10.20.540 | 
| Functional Family | 
Enzyme Information
| 3.6.4.12 | DNA helicase. based on mapping to UniProt K9N7C7 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). | 
| 3.4.19.12 | Ubiquitinyl hydrolase 1. based on mapping to UniProt K9N7C7 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 K9N7C7 | 
| 3.4.22.- | Cysteine endopeptidases. based on mapping to UniProt K9N7C7 | 
| 3.1.13.- | Exoribonucleases producing 5'-phosphomonoesters. based on mapping to UniProt K9N7C7 | 
| 2.7.7.48 | RNA-directed RNA polymerase. based on mapping to UniProt K9N7C7 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. | 
| 3.4.22.69 | SARS coronavirus main proteinase. based on mapping to UniProt K9N7C7 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. | 
| 2.1.1.- | Methyltransferases. based on mapping to UniProt K9N7C7 | 
| 3.6.4.13 | RNA helicase. based on mapping to UniProt K9N7C7 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). | 
UniProtKB Entries (2)
| K9N7C7 | R1AB_CVEMC Betacoronavirus England 1 Replicase polyprotein 1ab | 
| P0CG47 | UBB_HUMAN Homo sapiens Polyubiquitin-B | 
PDB Structure
| PDB | 4WUR | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin. Virol Sin | 
