ID   BIMB_EMENI              Reviewed;        2067 AA.
AC   P33144; C8V9Q5; Q5ASE7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Separin;
DE            EC=3.4.22.49;
DE   AltName: Full=Cell division-associated protein bimB;
DE   AltName: Full=Separase;
GN   Name=bimB; ORFNames=AN8783;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A773;
RX   PubMed=1639810; DOI=10.1016/s0021-9258(19)49597-5;
RA   May G.S., McGoldrick C.A., Holt C.L., Denison S.H.;
RT   "The bimB3 mutation of Aspergillus nidulans uncouples DNA replication from
RT   the completion of mitosis.";
RL   J. Biol. Chem. 267:15737-15743(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Required for nuclear division. Could function in the mitotic
CC       spindle.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=All bonds known to be hydrolyzed by this endopeptidase have
CC         arginine in P1 and an acidic residue in P4. P6 is often occupied by
CC         an acidic residue or by a hydroxy-amino-acid residue, the
CC         phosphorylation of which enhances cleavage.; EC=3.4.22.49;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33297.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CBF78027.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=EAA60576.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M83232; AAA33297.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AACD01000161; EAA60576.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BN001303; CBF78027.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A42854; A42854.
DR   RefSeq; XP_682052.1; XM_676960.1.
DR   AlphaFoldDB; P33144; -.
DR   SMR; P33144; -.
DR   STRING; 162425.CADANIAP00006279; -.
DR   EnsemblFungi; EAA60576; EAA60576; AN8783.2.
DR   GeneID; 2868364; -.
DR   KEGG; ani:AN8783.2; -.
DR   eggNOG; KOG1849; Eukaryota.
DR   HOGENOM; CLU_000454_0_0_1; -.
DR   InParanoid; P33144; -.
DR   OrthoDB; 178448at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051307; P:meiotic chromosome separation; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR005314; Peptidase_C50.
DR   InterPro; IPR030397; SEPARIN_core_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR12792; PTHR12792; 1.
DR   PROSITE; PS51700; SEPARIN; 1.
PE   4: Predicted;
KW   Cell cycle; Cell division; Chromosome partition; Hydrolase; Mitosis;
KW   Nucleus; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..2067
FT                   /note="Separin"
FT                   /id="PRO_0000205902"
FT   DOMAIN          1880..1975
FT                   /note="Peptidase C50"
FT   REGION          51..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1316..1363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1449..1478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1331..1363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1964
FT                   /evidence="ECO:0000250"
FT   CONFLICT        512
FT                   /note="S -> P (in Ref. 1; AAA33297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520
FT                   /note="A -> R (in Ref. 1; AAA33297)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2067 AA;  227831 MW;  3D711A90E1C0E38E CRC64;
     MAVTSFPADS LASMESVKQT VRSTSTCSAA TVLSLQTLFR SAGEMETTLR RTARGTKATA
     TNATASSRAK TTRTKSTSTS TTRTKTPAQD VSTFTSTSAS LADTRLSNQE KLVLATEVFN
     STLKTLSDAV KTVMSISKEK KDASPTKRGT TTKGRVKTSQ PDLTDNENGV SAVAECARLS
     LSCLRMLRTD AMVDGGLPNL QLEQGACVLA GRLLALGLND AAYKELRGLK RRIQSYLEEL
     PSGRKRTGRK DAEDGEETAK ERMSDLLSFS DIANARSIHG LLVSFQSNAL RLIAAEKRPA
     TVQKLVPSLQ LTDESSPANV IMASIDSGAL TKDKAAVQLQ LLSSTVLSLS ASGASTGKER
     LRPSIVLSLQ LLALEIRCMS WKLSGHACED NKEMWDPLAR YIGAFAQATK SIEKAEFAVI
     YKNIVRLQSA FSKTQNCATR STDNLSVARI ATILGQLAQD AGCFDEALQL FTESLNPLSS
     SQCLGMATVR CKIAALHFQA FKSSVKLPGD VSDAVSQATA ALSISLKGSS HDLDELLVQA
     AKLKKLAMGW FGDLISKGQG SQCENVVFPR ICEFLSSFVR FLRRYIGRRP ENDELNDREI
     FQKRIDAAQN IVLAAVDSTI AIGKLSVMSQ RPAWEETVST LLDCQRLLAT IEPFDEVDVA
     TADSIDQALV KLSNLFWSRY LKEKEAGKNA RELLPLLKQS AYLLSGCSPS QRATGFAPLK
     YERLAHTYIE GNMVSEAEVA FRQSITDHIA AGALDKIASS TDGCFPHQMN QDPKRSGFTL
     GRVLSAYLKV KLRNKRSAVN EIFDDETLPS VQRGHVLEWQ LGILTEIHGT SNNDNVFRSV
     FAEVATRLFK VYPAEQHPVR RLRVLLSGLR FALEQPGFLD SSLLQRFADE GRKGLDDDDY
     QDDDDIKSLA VYLKNSVRLT LGLQQGSLGP EELELIVSTW TSILRFCHDL KSLVACVGNV
     EYFLLQMKAV VDYTEIHGLW KFQLSTLELV LRVTELHGAG TFSEAIIVLS RLVLQYCRMG
     FCIKAHSLLS RADGYIANHE VSCLARLSYE LARVGFLLET GDNQKAATVL STARMIYEKH
     QATEDLDACS VLTKISWERL VADAAFMSSR LSFAQGSIKD ALYFAKLSVR LNCRIWAKVE
     KLAQKKQEKA VVGDSSELEI VVEGMAKLEV SQTSSTYSQG APFWPHIGSH HSSLLHLANL
     SAHHGLFQDA IYYGEQALKI NKSLNANVRL IASQAHLGSH WILGGHISEG QQLLASAKAL
     SDKLGSSIEL VSLRLSLAAL HRVEGDYRNE YRTLREAEKL LGGLFESQAD SADIPDLEEK
     MDKLRVRPKS RSTRQPATTA TRRTRSATTS ARSTPKPPQS VEATNASNTL LQMKSEILLQ
     QAASLRAQRE FEAASTLLSD ARKFAVTRNS RISVHLGESE HLLADAIRNF ANHAVYCVLP
     ESTISLPSLE PKAASESSSK SATRKTRAPT RGTRTKAQAA TEDFSVMLSK AGDCLNGIFD
     TATQLGSTLD SHSASRLMSR ISMLSHVTAS PNHILWPHSP ANMNEVGRIG AFARERAAIR
     IDKRLADYCD PLLWPRSELE SEGVSPDFTK EYVDILPDNW NVLSLSLSAD RAEFVVSRLH
     RGCSPFLLRL PLRRGNSEDE EEQFTFEDGR DEMKELIRLA NESAHAAKLQ VDRQMKKEWW
     KNREALDRRM ENLLQNIENV WFGGFRGIFS PIPLCEKSLA RFASAFENIL ENHLPSRRKG
     SRAQGPKLTL HPNVLELFVG VKGLDDQEDP EDTLMDLLYF VVDILQFQGE RNAYDEVDFD
     MMVVETLDAV RAYHEAAKDQ ATQRPNNTVL VLDKSLHLFP WESLPCLQGL PVCRVPSLEC
     LRDRVLHLRS GKQSALSIDR RNGTYILNPT GDLKTTQETF EKDLSSLKGW TGMVNRQPTE
     DEFKDSLQSK SLFLYFGHGS GAQYIRGRTV KRLDRCAVAF LMGCSSGTLT EAGEYEPYGT
     PMNYLQAGSP ALVATLWDVT DKDIDRFAKA TFEHWGLIGN GHRGNEGIGE AGVALDAAVS
     QSRGACVLKY LNGAAPVVYG VPGVFLH