EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.22.49 | Arabidopsis thaliana | Q5IBC5 | - |
- |
3.4.22.49 | Caenorhabditis elegans | G5ED39 | - |
- |
3.4.22.49 | Homo sapiens | Q14674 | - |
- |
3.4.22.49 | Saccharomyces cerevisiae | Q03018 | - |
- |
3.4.22.49 | Saccharomyces cerevisiae ATCC 204508 | Q03018 | - |
- |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.22.49 | 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 |
3.4.22.49 | 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 |
3.4.22.49 | 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 |
3.4.22.49 | 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 |
3.4.22.49 | physiological function | separase cleaves the proteins that maintain the cohesion between sister chromatids | Arabidopsis thaliana |
3.4.22.49 | physiological function | separase cleaves the proteins that maintain the cohesion between sister chromatids | Saccharomyces cerevisiae |
3.4.22.49 | physiological function | separase cleaves the proteins that maintain the cohesion between sister chromatids | Homo sapiens |
3.4.22.49 | physiological function | separase cleaves the proteins that maintain the cohesion between sister chromatids | Caenorhabditis elegans |