| Type: | Domain | Name: | SEPARIN core domain |
| Description: | This entry represents the SEPARIN core domain.In eukaryotic cells, replicated DNA strands remain physically connected until their segregation to opposite poles of the cell during anaphase. This "sisterchromatid cohesion" is essential for the alignment of chromosomes on the mitotic spindle during metaphase. Cohesion depends on the multisubunit cohesincomplex, which possibly forms the physical bridges connecting sisters. The separins (separases) cleave the Scc1p subunit of the cohesin complex, allowingthe separation of sister chromatids in anaphase. Separins are highly conserved in all eukaryotes but have not been detected in prokaryotes [, ].All known separin homologues possess a conserved C-terminal "separin" domain. The separin core domain contains a conserved histidine and cyteine residue,which are hallmarks of cysteine proteases. These two residues are invariably surrounded by small residues (glycine or serine), and each is preceded byamino acid sequences that are predicted to form hydrophobic beta sheets. This pattern is characteristic of cysteine endopeptidases of the CD clan,which includes caspases, legumains, gingipains, clostripains, anf GPI-anchor amidases. The histidine end cysteine residues are likely to form the separindomain's catalytic dyad [, ]. The separin core domain forms the peptidase C50family. | Short Name: | SEPARIN_core_dom |
