Function and Biology Details
Reactions catalysed:
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153195 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
mRNA-capping enzyme subunit alpha
Molecule details ›
Chains: A, B
Length: 403 amino acids
Theoretical weight: 47.03 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 403 amino acids
Theoretical weight: 47.03 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P40997 (Residues: 1-402; Coverage: 100%)
Sequence domains:
Structure domains:
DNA-directed RNA polymerase II subunit rpb1
Molecule details ›
Chains: P, Q
Length: 21 amino acids
Theoretical weight: 2.66 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Not provided
UniProt:
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
Length: 21 amino acids
Theoretical weight: 2.66 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Not provided
UniProt:
- Canonical: P36594 (Residues: 1732-1752; Coverage: 1%)
Sequence domains: RNA polymerase Rpb1 C-terminal repeat
