Literature summary for 3.4.22.49 extracted from

Winter, A.; Schmid, R.; Bayliss, R.
Structural insights into separase architecture and substrate recognition through computational modelling of caspase-like and death domains (2015), PLoS Comput. Biol., 11, e1004548 .

Search for more literature for 3.4.22.49

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q5IBC5	-	-
Caenorhabditis elegans	G5ED39	-	-
Homo sapiens	Q14674	-	-
Saccharomyces cerevisiae	Q03018	-	-
Saccharomyces cerevisiae ATCC 204508	Q03018	-	-

General Information

General Information	Comment	Organism
evolution	in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability	Arabidopsis thaliana
evolution	in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability	Saccharomyces cerevisiae
evolution	in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifies potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability	Caenorhabditis elegans
evolution	in-depth bioinformatical analysis of separase and generation of structural models of the two conserved domains that comprise the C-terminal region: a caspase-like domain and a putative death domain. This analysis provides insights into substrate recognition and identifis potential sites of protein-protein interactions. Both the death domain and caspase-like domain are well-conserved in separases, which suggests an evolutionary pressure to keep these two domains together, perhaps to enable separase activity and/or provide stability	Homo sapiens
physiological function	separase cleaves the proteins that maintain the cohesion between sister chromatids	Arabidopsis thaliana
physiological function	separase cleaves the proteins that maintain the cohesion between sister chromatids	Saccharomyces cerevisiae
physiological function	separase cleaves the proteins that maintain the cohesion between sister chromatids	Homo sapiens
physiological function	separase cleaves the proteins that maintain the cohesion between sister chromatids	Caenorhabditis elegans

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Release 2023.1 (January 2023)