| IED ID | IndEnz0002005461 |
| Enzyme Type ID | protease005461 |
| Protein Name |
Separin EC 3.4.22.49 Cell division-associated protein bimB Separase |
| Gene Name | bimB AN8783 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MAVTSFPADSLASMESVKQTVRSTSTCSAATVLSLQTLFRSAGEMETTLRRTARGTKATATNATASSRAKTTRTKSTSTSTTRTKTPAQDVSTFTSTSASLADTRLSNQEKLVLATEVFNSTLKTLSDAVKTVMSISKEKKDASPTKRGTTTKGRVKTSQPDLTDNENGVSAVAECARLSLSCLRMLRTDAMVDGGLPNLQLEQGACVLAGRLLALGLNDAAYKELRGLKRRIQSYLEELPSGRKRTGRKDAEDGEETAKERMSDLLSFSDIANARSIHGLLVSFQSNALRLIAAEKRPATVQKLVPSLQLTDESSPANVIMASIDSGALTKDKAAVQLQLLSSTVLSLSASGASTGKERLRPSIVLSLQLLALEIRCMSWKLSGHACEDNKEMWDPLARYIGAFAQATKSIEKAEFAVIYKNIVRLQSAFSKTQNCATRSTDNLSVARIATILGQLAQDAGCFDEALQLFTESLNPLSSSQCLGMATVRCKIAALHFQAFKSSVKLPGDVSDAVSQATAALSISLKGSSHDLDELLVQAAKLKKLAMGWFGDLISKGQGSQCENVVFPRICEFLSSFVRFLRRYIGRRPENDELNDREIFQKRIDAAQNIVLAAVDSTIAIGKLSVMSQRPAWEETVSTLLDCQRLLATIEPFDEVDVATADSIDQALVKLSNLFWSRYLKEKEAGKNARELLPLLKQSAYLLSGCSPSQRATGFAPLKYERLAHTYIEGNMVSEAEVAFRQSITDHIAAGALDKIASSTDGCFPHQMNQDPKRSGFTLGRVLSAYLKVKLRNKRSAVNEIFDDETLPSVQRGHVLEWQLGILTEIHGTSNNDNVFRSVFAEVATRLFKVYPAEQHPVRRLRVLLSGLRFALEQPGFLDSSLLQRFADEGRKGLDDDDYQDDDDIKSLAVYLKNSVRLTLGLQQGSLGPEELELIVSTWTSILRFCHDLKSLVACVGNVEYFLLQMKAVVDYTEIHGLWKFQLSTLELVLRVTELHGAGTFSEAIIVLSRLVLQYCRMGFCIKAHSLLSRADGYIANHEVSCLARLSYELARVGFLLETGDNQKAATVLSTARMIYEKHQATEDLDACSVLTKISWERLVADAAFMSSRLSFAQGSIKDALYFAKLSVRLNCRIWAKVEKLAQKKQEKAVVGDSSELEIVVEGMAKLEVSQTSSTYSQGAPFWPHIGSHHSSLLHLANLSAHHGLFQDAIYYGEQALKINKSLNANVRLIASQAHLGSHWILGGHISEGQQLLASAKALSDKLGSSIELVSLRLSLAALHRVEGDYRNEYRTLREAEKLLGGLFESQADSADIPDLEEKMDKLRVRPKSRSTRQPATTATRRTRSATTSARSTPKPPQSVEATNASNTLLQMKSEILLQQAASLRAQREFEAASTLLSDARKFAVTRNSRISVHLGESEHLLADAIRNFANHAVYCVLPESTISLPSLEPKAASESSSKSATRKTRAPTRGTRTKAQAATEDFSVMLSKAGDCLNGIFDTATQLGSTLDSHSASRLMSRISMLSHVTASPNHILWPHSPANMNEVGRIGAFARERAAIRIDKRLADYCDPLLWPRSELESEGVSPDFTKEYVDILPDNWNVLSLSLSADRAEFVVSRLHRGCSPFLLRLPLRRGNSEDEEEQFTFEDGRDEMKELIRLANESAHAAKLQVDRQMKKEWWKNREALDRRMENLLQNIENVWFGGFRGIFSPIPLCEKSLARFASAFENILENHLPSRRKGSRAQGPKLTLHPNVLELFVGVKGLDDQEDPEDTLMDLLYFVVDILQFQGERNAYDEVDFDMMVVETLDAVRAYHEAAKDQATQRPNNTVLVLDKSLHLFPWESLPCLQGLPVCRVPSLECLRDRVLHLRSGKQSALSIDRRNGTYILNPTGDLKTTQETFEKDLSSLKGWTGMVNRQPTEDEFKDSLQSKSLFLYFGHGSGAQYIRGRTVKRLDRCAVAFLMGCSSGTLTEAGEYEPYGTPMNYLQAGSPALVATLWDVTDKDIDRFAKATFEHWGLIGNGHRGNEGIGEAGVALDAAVSQSRGACVLKYLNGAAPVVYGVPGVFLH |
| Enzyme Length | 2067 |
| Uniprot Accession Number | P33144 |
| Absorption | |
| Active Site | ACT_SITE 1964; /evidence=ECO:0000250 |
| Activity Regulation | |
| 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: Required for nuclear division. Could function in the mitotic spindle. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (3); Domain (1); Frameshift (3); Region (4); Sequence conflict (2) |
| Keywords | Cell cycle;Cell division;Chromosome partition;Hydrolase;Mitosis;Nucleus;Protease;Reference proteome;Thiol protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 227,831 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |