Function and Biology Details
Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150306 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 20.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: NLI interacting factor-like phosphatase
Structure domains: HAD superfamily/HAD-like
Length: 181 amino acids
Theoretical weight: 20.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9GZU7 (Residues: 77-256; Coverage: 69%)
Sequence domains: NLI interacting factor-like phosphatase
Structure domains: HAD superfamily/HAD-like
DNA-directed RNA polymerase II subunit RPB1
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 905 Da
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
Length: 8 amino acids
Theoretical weight: 905 Da
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P24928 (Residues: 1796-1803; Coverage: 0%)
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
