| IED ID | IndEnz0002002423 |
| Enzyme Type ID | protease002423 |
| Protein Name |
Separin EC 3.4.22.49 Cell untimely torn protein 1 Separase |
| Gene Name | cut1 SPCC5E4.04 |
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota Taphrinomycotina Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces Schizosaccharomyces pombe (Fission yeast) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
| Enzyme Sequence | MSTRSIVTSKVSWTPEKFISALSYPEHCSITLVKRLKASVKLKDLKQNISRDAPSWTFEHLFVAFKCAVSNLAKQWAELSTTDKEKTRRMFCTPSRLNTAHRPEVFYLLECCTYILEQMQVVTKNTSHLYDCIRSGVSICNRLLDMEIFEPAISLLMKTHKNLIILLTYRDHDAIPTATLLNPTLDVSEIQLESCLFVPMVPASYFLNIGTIVVTFQLNVLRCLSLSQINGLSLNTINNLQSEDGPFQWIERSFPSQVQLANSRREILARLLTRFSMIQNNALQSFKLLILSIALWLNILSSQRADDKEFDVNQLETRILQLFSKVVQLCKSEDIEGSILNKDMTQLHHLLENLSKESRLHILLQLSQLYYKYNDFQLSAAYVIRGYSLSFEDISFKLKFLLFSFRLSIHDNSICFPFNLIQELSSLQQLFVENALPYSEALHLLDSIERSFRLFNDSTVFDDTVFALNISEILSWILSSVVRDILVEDELLNLQLKIRKFLMFTFHIIRSFSELTKFQSSLEGCLNLAAYYEDAEFPQKLSNHLYNLCVKSSNVNYARECISLSIKIAVSHKLTNDETYLLKILKNFQLRYHDSLQLQEKCDVLHTTFNQLDLYVGTTSVGKSSVLDNILKRIFNSLTSINDSNIEKLLESISYSLLKLFFKCANEGSRYNASAALSFKLSLMLHEKEEVLLLKTNVSCVLANHGYNDIKFEEMVLCVIKGDQNLLEHNSNNNAKLALNESLLCSWENLLCYRRAEDDSRILTIIESWTIFISRFSSVISRCSFTDFEINSILNFFFCFLHTVEPSGKLTFELAFLEIFYELFNCLLHLQFSKYLVIIGTLLSDKYMTLGFSGKAHLFYTKCYSYLRQCKSSPFINFWNVSYGKYLILTGNTDKGILQLKKYSLSSEEDFNSNGLSRTVSLNLLLYERIQLSDALFQLGYTTVSLGFIMQNLKVIKGLFSKSSKEHFNGGKYITWRLFAVSAHSNVCAARIYEHMGQAREAEFFYRQACSISEKMPFSCFSATFQLRLCSLLTRAGKLEKGEKILFDLTEAMKSTDTYHKLLWNYGAAEVCATKSELDGAICHYSECVKLLEIIKSEYYLFFNRNREKSLTKGIKRLSLSSQPTFVTESNTTEFDDWSILQNTAANLLRLISMFELKRGNLEIAKALMTDSTKCSIASFFNIVSANILKSKLIVCEADSTLFGDPVLRTLPDSVISLPGISHKFQKNQSKTKALGENTGFRKGSKRLDYLRERLKINLQNVRLSCEIIFSNAYERSSVCVCREVNELISYSTIMQSALTTIGETTDVDSSSASFFLEIPKALGFHRRREAQKFRNQHKELHFSSLEQILNSRLSIPDVRTFQDNFIDSLPSIWNVVSITINNSGEDLFISKIRKGHSPLIFRLPLQRHNSRDADEEILVFTKAQTELFRIISKSNQMAQNGKHYTRREDKETWWKERRHLDQCLQQLLENIEISWLGGFKGIFNPHKIDTSLFAKFSSQFQNIIAKNFNMDKKTPVPTLSPEILELFITLGKPGYEGYEQLLEDLIYFILDIFQFRGLHFAYDEIDTDQLSMDLQDALNAYFNNYVSEENRSHTVLVLDKSVHQFPWESLPCLNRQSVSRVPSLSILRDILSQSFVVNGEYVEVRKEAGSYILNPSLDLKHTQEMFEHKLVEGGWKGLIASQPSNRDFIKMLSGNDFFLYFGHGGGEQYTTSYDLATLKRCAVTILMGCSSGALYECGSFEPWGTPLDYLSAGCPTLVANLWDVTDKDIDRFSLKMLESWGLFENKAPFVNSTSICTAVSESRSCCHLRYLNGAAPVIYGIPAYIIP |
| Enzyme Length | 1828 |
| Uniprot Accession Number | P18296 |
| Absorption | |
| Active Site | ACT_SITE 1730 |
| Activity Regulation | ACTIVITY REGULATION: It is inactivated via its interaction with cut2, which probably covers its active site. Cut2 degradation at anaphase, liberates it and triggers rad21 cleavage. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.22.49; |
| DNA Binding | |
| EC Number | 3.4.22.49 |
| Enzyme Function | FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation. {ECO:0000269|PubMed:12390246}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Mutagenesis (3); Sequence conflict (6) |
| Keywords | Cell cycle;Cell division;Chromosome partition;Cytoplasm;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14511667; 14532136; 15161942; 15507118; 16453724; 16483313; 17032733; 20473289; 22645648; 23697806; 24583014; 29996109; 30072439; 7957061; 8395535; 9168469; 9635190; 9649518; 9802907; |
| Motif | |
| Gene Encoded By | |
| Mass | 209,434 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.49; |