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:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138567 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA-directed RNA polymerase L
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.48 KDa
Source organism: Orthonairovirus haemorrhagiae
Expression system: Escherichia coli
UniProt:
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Length: 171 amino acids
Theoretical weight: 19.48 KDa
Source organism: Orthonairovirus haemorrhagiae
Expression system: Escherichia coli
UniProt:
- Canonical:
Q6TQR6 (Residues: 1-169; Coverage: 4%)
Sequence domains: OTU-like cysteine protease
Structure domains: Cathepsin B; Chain A
Ubiquitin-like protein ISG15
Molecule details ›
Chain: B
Length: 156 amino acids
Theoretical weight: 17.12 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: 156 amino acids
Theoretical weight: 17.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P05161 (Residues: 1-156; Coverage: 95%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
