Function and Biology Details
Reaction catalysed:
(1a) ATP + [RNA ligase]-L-lysine = [RNA ligase]-N(6)-(5'-adenylyl)-L-lysine + diphosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Metallophosphoesterase (preferred)
PDBe Complex ID:
PDB-CPX-107082 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallophosphoesterase
Molecule details ›
Chains: A, B, C, D
Length: 393 amino acids
Theoretical weight: 45.1 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: PNKP adenylyltransferase domain, ligase domain
Structure domains: DNA ligase/mRNA capping enzyme
Length: 393 amino acids
Theoretical weight: 45.1 KDa
Source organism: Acetivibrio thermocellus ATCC 27405
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A3DJ38 (Residues: 479-870; Coverage: 45%)
Sequence domains: PNKP adenylyltransferase domain, ligase domain
Structure domains: DNA ligase/mRNA capping enzyme
