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-107787 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CCR4-NOT transcription complex subunit 1
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 26.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: CCR4-NOT transcription complex subunit 1 CAF1-binding domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Length: 231 amino acids
Theoretical weight: 26.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A5YKK6 (Residues: 1093-1317; Coverage: 10%)
Sequence domains: CCR4-NOT transcription complex subunit 1 CAF1-binding domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Probable ATP-dependent RNA helicase DDX6
Molecule details ›
Chain: B
Length: 182 amino acids
Theoretical weight: 21.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 182 amino acids
Theoretical weight: 21.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P26196 (Residues: 307-483; Coverage: 37%)
Sequence domains: Helicase conserved C-terminal domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases
