Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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).
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
RNA-directed RNA polymerase L and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-158824 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L
Molecule details ›
Chains: A, C, E, G
Length: 185 amino acids
Theoretical weight: 21.01 KDa
Source organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Expression system: Escherichia coli
UniProt:
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Length: 185 amino acids
Theoretical weight: 21.01 KDa
Source organism: Crimean-Congo hemorrhagic fever virus strain IbAr10200
Expression system: Escherichia coli
UniProt:
- Canonical:
Q6TQR6 (Residues: 1-183; Coverage: 5%)
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin
Molecule details ›
Chains: B, D, F, H
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 75 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P62979 (Residues: 1-75; Coverage: 48%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
