Function and Biology Details
Reaction catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137362 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Regulator of Ty1 transposition protein 103
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.57 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: CID domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Length: 142 amino acids
Theoretical weight: 16.57 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
Q05543 (Residues: 1-1, 3-131; Coverage: 32%)
Sequence domains: CID domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
DNA-directed RNA polymerase II subunit RPB1
Molecule details ›
Chain: B
Length: 16 amino acids
Theoretical weight: 1.97 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
Length: 16 amino acids
Theoretical weight: 1.97 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
- Canonical: P04050 (Residues: 1678-1693; Coverage: 1%)
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
