Function and Biology Details
Reaction catalysed:
All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Separase-Securin complex (preferred)
PDBe Complex ID:
PDB-CPX-124507 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Separin homolog sep-1
Molecule details ›
Chain: 1
Length: 1262 amino acids
Theoretical weight: 144.32 KDa
Source organism: Caenorhabditis elegans
Expression system: Trichoplusia ni
UniProt:
Sequence domains: Peptidase family C50
Length: 1262 amino acids
Theoretical weight: 144.32 KDa
Source organism: Caenorhabditis elegans
Expression system: Trichoplusia ni
UniProt:
- Canonical:
G5ED39 (Residues: 1-1262; Coverage: 100%)
Sequence domains: Peptidase family C50
Securin-like protein
Molecule details ›
Chain: B
Length: 244 amino acids
Theoretical weight: 27.03 KDa
Source organism: Caenorhabditis elegans
Expression system: Trichoplusia ni
UniProt:
Length: 244 amino acids
Theoretical weight: 27.03 KDa
Source organism: Caenorhabditis elegans
Expression system: Trichoplusia ni
UniProt:
- Canonical: Q18235 (Residues: 1-244; Coverage: 100%)
