P33144 · BIMB_EMENI

Function

function

Required for nuclear division. Could function in the mitotic spindle.

Catalytic activity

  • 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 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

120672004006008001,0001,2001,4001,6001,8002,000
TypeIDPosition(s)Description
Active site1964

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitotic spindle
Cellular Componentmitotic spindle pole body
Cellular Componentnucleus
Molecular Functioncysteine-type endopeptidase activity
Biological Processcell division
Biological Processmeiotic chromosome separation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Separin
  • EC number
  • Alternative names
    • Cell division-associated protein bimB
    • Separase

Gene names

    • Name
      bimB
    • ORF names
      AN8783

Organism names

Accessions

  • Primary accession
    P33144
  • Secondary accessions
    • C8V9Q5
    • Q5ASE7

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002059021-2067Separin

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region51-91Disordered
Compositional bias52-91Polar residues
Region140-167Disordered
Compositional bias149-167Polar residues
Region1316-1363Disordered
Compositional bias1331-1363Polar residues
Region1449-1478Disordered
Domain1880-1975Peptidase C50

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    2,067
  • Mass (Da)
    227,831
  • Last updated
    2009-05-26 v2
  • Checksum
    3D711A90E1C0E38E
MAVTSFPADSLASMESVKQTVRSTSTCSAATVLSLQTLFRSAGEMETTLRRTARGTKATATNATASSRAKTTRTKSTSTSTTRTKTPAQDVSTFTSTSASLADTRLSNQEKLVLATEVFNSTLKTLSDAVKTVMSISKEKKDASPTKRGTTTKGRVKTSQPDLTDNENGVSAVAECARLSLSCLRMLRTDAMVDGGLPNLQLEQGACVLAGRLLALGLNDAAYKELRGLKRRIQSYLEELPSGRKRTGRKDAEDGEETAKERMSDLLSFSDIANARSIHGLLVSFQSNALRLIAAEKRPATVQKLVPSLQLTDESSPANVIMASIDSGALTKDKAAVQLQLLSSTVLSLSASGASTGKERLRPSIVLSLQLLALEIRCMSWKLSGHACEDNKEMWDPLARYIGAFAQATKSIEKAEFAVIYKNIVRLQSAFSKTQNCATRSTDNLSVARIATILGQLAQDAGCFDEALQLFTESLNPLSSSQCLGMATVRCKIAALHFQAFKSSVKLPGDVSDAVSQATAALSISLKGSSHDLDELLVQAAKLKKLAMGWFGDLISKGQGSQCENVVFPRICEFLSSFVRFLRRYIGRRPENDELNDREIFQKRIDAAQNIVLAAVDSTIAIGKLSVMSQRPAWEETVSTLLDCQRLLATIEPFDEVDVATADSIDQALVKLSNLFWSRYLKEKEAGKNARELLPLLKQSAYLLSGCSPSQRATGFAPLKYERLAHTYIEGNMVSEAEVAFRQSITDHIAAGALDKIASSTDGCFPHQMNQDPKRSGFTLGRVLSAYLKVKLRNKRSAVNEIFDDETLPSVQRGHVLEWQLGILTEIHGTSNNDNVFRSVFAEVATRLFKVYPAEQHPVRRLRVLLSGLRFALEQPGFLDSSLLQRFADEGRKGLDDDDYQDDDDIKSLAVYLKNSVRLTLGLQQGSLGPEELELIVSTWTSILRFCHDLKSLVACVGNVEYFLLQMKAVVDYTEIHGLWKFQLSTLELVLRVTELHGAGTFSEAIIVLSRLVLQYCRMGFCIKAHSLLSRADGYIANHEVSCLARLSYELARVGFLLETGDNQKAATVLSTARMIYEKHQATEDLDACSVLTKISWERLVADAAFMSSRLSFAQGSIKDALYFAKLSVRLNCRIWAKVEKLAQKKQEKAVVGDSSELEIVVEGMAKLEVSQTSSTYSQGAPFWPHIGSHHSSLLHLANLSAHHGLFQDAIYYGEQALKINKSLNANVRLIASQAHLGSHWILGGHISEGQQLLASAKALSDKLGSSIELVSLRLSLAALHRVEGDYRNEYRTLREAEKLLGGLFESQADSADIPDLEEKMDKLRVRPKSRSTRQPATTATRRTRSATTSARSTPKPPQSVEATNASNTLLQMKSEILLQQAASLRAQREFEAASTLLSDARKFAVTRNSRISVHLGESEHLLADAIRNFANHAVYCVLPESTISLPSLEPKAASESSSKSATRKTRAPTRGTRTKAQAATEDFSVMLSKAGDCLNGIFDTATQLGSTLDSHSASRLMSRISMLSHVTASPNHILWPHSPANMNEVGRIGAFARERAAIRIDKRLADYCDPLLWPRSELESEGVSPDFTKEYVDILPDNWNVLSLSLSADRAEFVVSRLHRGCSPFLLRLPLRRGNSEDEEEQFTFEDGRDEMKELIRLANESAHAAKLQVDRQMKKEWWKNREALDRRMENLLQNIENVWFGGFRGIFSPIPLCEKSLARFASAFENILENHLPSRRKGSRAQGPKLTLHPNVLELFVGVKGLDDQEDPEDTLMDLLYFVVDILQFQGERNAYDEVDFDMMVVETLDAVRAYHEAAKDQATQRPNNTVLVLDKSLHLFPWESLPCLQGLPVCRVPSLECLRDRVLHLRSGKQSALSIDRRNGTYILNPTGDLKTTQETFEKDLSSLKGWTGMVNRQPTEDEFKDSLQSKSLFLYFGHGSGAQYIRGRTVKRLDRCAVAFLMGCSSGTLTEAGEYEPYGTPMNYLQAGSPALVATLWDVTDKDIDRFAKATFEHWGLIGNGHRGNEGIGEAGVALDAAVSQSRGACVLKYLNGAAPVVYGVPGVFLH

Sequence caution

The sequence AAA33297.1 differs from that shown. Reason: Frameshift
The sequence CBF78027.1 differs from that shown. Reason: Frameshift
The sequence EAA60576.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias52-91Polar residues
Compositional bias149-167Polar residues
Sequence conflict512in Ref. 1; AAA33297
Sequence conflict520in Ref. 1; AAA33297
Compositional bias1331-1363Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M83232
EMBL· GenBank· DDBJ
AAA33297.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift
AACD01000161
EMBL· GenBank· DDBJ
EAA60576.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift
BN001303
EMBL· GenBank· DDBJ
CBF78027.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp