Function and Biology Details
Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Initiation factor eIF-4 gamma, MA3
- Helicase, C-terminal domain-like
- P-loop containing nucleoside triphosphate hydrolase
- Helicase superfamily 1/2, ATP-binding domain
- Armadillo-type fold
- ATP-dependent RNA helicase DEAD-box, conserved site
- DEAD/DEAH box helicase domain
- ATP-dependent RNA helicase eIF4A, DEAD-box helicase domain
2 more domains
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158103 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Eukaryotic initiation factor 4A-I
Molecule details ›
Chains: A, C, D, F
Length: 388 amino acids
Theoretical weight: 44.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 388 amino acids
Theoretical weight: 44.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P60842 (Residues: 20-406; Coverage: 95%)
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Programmed cell death protein 4
Molecule details ›
Chains: B, E
Length: 307 amino acids
Theoretical weight: 34.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: MA3 domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Length: 307 amino acids
Theoretical weight: 34.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q53EL6 (Residues: 163-469; Coverage: 66%)
Sequence domains: MA3 domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
