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Database: UniProt
Entry: A0A9W9FHB9_9EURO
LinkDB: A0A9W9FHB9_9EURO
Original site: A0A9W9FHB9_9EURO 
ID   A0A9W9FHB9_9EURO        Unreviewed;      1005 AA.
AC   A0A9W9FHB9;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 7.
DE   RecName: Full=Cytokinesis regulator {ECO:0008006|Google:ProtNLM};
GN   ORFNames=N7456_006233 {ECO:0000313|EMBL:KAJ5100181.1};
OS   Penicillium angulare.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=116970 {ECO:0000313|EMBL:KAJ5100181.1, ECO:0000313|Proteomes:UP001149165};
RN   [1] {ECO:0000313|EMBL:KAJ5100181.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 30069 {ECO:0000313|EMBL:KAJ5100181.1};
RA   Petersen C.;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5100181.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 30069 {ECO:0000313|EMBL:KAJ5100181.1};
RX   PubMed=36726175;
RA   Petersen C., Sorensen T., Nielsen M.R., Sondergaard T.E., Sorensen J.L.,
RA   Fitzpatrick D.A., Frisvad J.C., Nielsen K.L.;
RT   "Comparative genomic study of the Penicillium genus elucidates a diverse
RT   pangenome and 15 lateral gene transfer events.";
RL   IMA Fungus 14:0-0(2023).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAJ5100181.1}.
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DR   EMBL; JAPQKH010000004; KAJ5100181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W9FHB9; -.
DR   OrthoDB; 19159at2759; -.
DR   Proteomes; UP001149165; Unassembled WGS sequence.
DR   GO; GO:1990334; C:Bfa1-Bub2 complex; IEA:InterPro.
DR   GO; GO:0044732; C:mitotic spindle pole body; IEA:TreeGrafter.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IEA:TreeGrafter.
DR   InterPro; IPR034586; Bfa1/Byr4.
DR   PANTHER; PTHR35140; MITOTIC CHECK POINT PROTEIN BFA1; 1.
DR   PANTHER; PTHR35140:SF1; MITOTIC CHECK POINT PROTEIN BFA1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP001149165}.
FT   REGION          35..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..795
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..226
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..247
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..310
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..423
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..449
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..513
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..598
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..613
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..716
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..733
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..769
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..918
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..941
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  109919 MW;  C1D18544C0616A57 CRC64;
     MDSPMNLTTR PEKDDQQIEC WDDDDDLQFN EGAQFRAASS TGSVTNSSFR PSGHRDSISS
     RRSARSDLDS NAGDEDWQVP LHDSDDFAKE EALASAKRAG IPIPANIPSS ALLGGAIKRL
     SNRKSKRTFV DDWTEDVELP GPDFILKIRN SPHTTFPDSI RQISSAVTSP VKSTASSNWN
     EDVSTRLQSA LAGLDRIQDE NDEPINRDVP ILKAPTPRSP QKPPTRVPAG DLLGTQESDD
     FDQDLELPPD HQPLQLSHRK DTTRSISPTF DDFDLEWSEG SIGVRVGGTA RDGRSVPSSS
     ISIASPSVSS CITGESDDGL DGLVFPDGPL DFAASLKKRE EDSPSENARK VKELPRASES
     MDSDDFFAGI DVDNGRAFAQ RKLNLNPNVK CKTEWPSSPT RRPATTLTFT NPGASTTSTT
     GSPRQFTRIP RLSGHEATLS TSLETVSESG APISKFQRPQ SRLGHSSQSS ISSLPASATS
     SASPLPTPPS RRLLGPRAAR NPAPAGNTPT PARLRTKRSL PSIRGTATAA TTTSLQRTPS
     HADGHVRPSA ARPKTPVERT SFPDSRTSGQ RVQPTFISAT ASERQSHHSS IKTYRPSRRQ
     SSDGSSGLLS PPQTSLPSRS SRPNSFRLSL DDSKSETISS TAKRTLTRPT RRRNFGDGTE
     LESFDDLPTS VSAESKFTKN ATGRAAPRPG HARLSQSRIN SISEPPTQIT TPPSISKPLN
     STPRFAQDTN ASRNAREQRI ASMNSRNRDA SSLGSFNSNW KPNPISRISP NAAPIRSRKS
     KSTNKSQSKP QLIKPMGAGM QEPKFVRGMR YNPNTFLWEG NENFGQEFDV ATAPRSPKPA
     PALISNVGNA NNVQTVGGMV FDPQRMCWLR ASPRDPRQQG RLVPEDEDDV FAGLDDLEDK
     AVGTKWTTKS PDDTSQPHVT GEEPSAGESS DEGPITEEFD VGPEFIRRQR AEEEKWRRKV
     NKWVGFNRED GNTHWRWAIR DLMTDGMTDP MVKQVVSYPT EIHDF
//
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