Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148978 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP-dependent RNA helicase DBP5
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 21.25 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 188 amino acids
Theoretical weight: 21.25 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical:
P20449 (Residues: 297-482; Coverage: 39%)
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
mRNA export factor GLE1
Molecule details ›
Chain: B
Length: 297 amino acids
Theoretical weight: 34.58 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
Sequence domains: GLE1-like protein
Structure domains: GLE1-like
Length: 297 amino acids
Theoretical weight: 34.58 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
- Canonical: Q12315 (Residues: 244-538; Coverage: 55%)
Sequence domains: GLE1-like protein
Structure domains: GLE1-like
