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Database: UniProt
Entry: A0A1W2TCD4_ROSNE
LinkDB: A0A1W2TCD4_ROSNE
Original site: A0A1W2TCD4_ROSNE 
ID   A0A1W2TCD4_ROSNE        Unreviewed;      1032 AA.
AC   A0A1W2TCD4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   10-JUN-2026, entry version 22.
DE   SubName: Full=Cytokinesis regulator {ECO:0000313|EMBL:GAP85624.1};
GN   ORFNames=SAMD00023353_1301130 {ECO:0000313|EMBL:GAP85624.1};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP85624.1, ECO:0000313|Proteomes:UP000054516};
RN   [1] {ECO:0000313|EMBL:GAP85624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP85624.1};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DF977458; GAP85624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TCD4; -.
DR   STRING; 77044.A0A1W2TCD4; -.
DR   OMA; DWGEGSL; -.
DR   OrthoDB; 19159at2759; -.
DR   Proteomes; UP000054516; 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:UP000054516}.
FT   REGION          30..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..971
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..48
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..251
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..311
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..523
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..829
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..964
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  114797 MW;  A1265006B54E16D1 CRC64;
     MESLQLKPRK PVEEIVENWD DDDFMIGDDG DLAFRNHSTA SSTHATSNSR RRDSRSSFRS
     DRDSLPSDDH QVHLPGDDEK STLDAIAAAT DAGIPIPVNV PPSALVGGTI KRLGVRKIKK
     IFQEDWGDEL VLPAPGQTLR LKTQDGNKFP DAFPQVSSPT SPVRAMTFLP TLAQLSPPST
     GQRKSLAAPI NLEKFRDTDD DDDMFGDSHS TIKASKFQVK GRPVSLITPP TPSPPQISKE
     TDDDFENDLE LPSDGKLKLS SKRDIPKTPS LHANDDFDWG EGSLGTRFGG TRRDAFSNRS
     SSVSAMSPSI ASSFTAESED EFFDGLIFPI GPLDLGERLK RRKQSRSPGR LDLSKPQQAN
     KRPSSPKISS PTRYSAKSAS PNPKSPRRGG LASRAFQVNR DEEDLVSGLD LGEGNVFRFA
     KPTVHRNVKV KEARPVSPVR PKAAVSITFT NKPINAISSR LPRPMIGHER SHTQSSLEPV
     SESGDPIPQK PPRRPQSRLS GHSAHSAHSS VSSVHTPTTP SSTQSNFPPT PRRKELCQKA
     SAGALRTEPT TTSAQLLRLK RSLPAMRHGQ PPAKHVINRT DRPPSRGDSR TDVYRPQSSL
     RPKTPVERTR PVYESGAAQA RKGQVPFLPA GASQSQSHHV NAKNLRSFRR HDSEQGPEIR
     PISRALSRNG LRSPSPRRSK TDKSTPEPAW QQINKPRRVR HFGDGHELDA FDDLPTSAQI
     ESRYTKQPSG SGNRINIRNK IYQNVLPDRN TFSPVLPYSQ SRLEAQPRFA RDTAASRIAR
     ETSLAQRAQP TSSFVPLNLQ RVTQLSSRAN INSHVSLNHG RSKKSRKPQQ LKPHLISNLN
     SAKDSKVING MRYNPTTYRW EGNETALNAF DIPASSPATT PLPQSTTRER ETTTPRPVLI
     TNINTKKETR RIGDMVFDPQ NMCWLEIKTS TPTGLQSDDP MAGFAALEEE DPFKDIPDLE
     DKKPSRSASG RVSDIREDWL VGEEFDVGPE FVRRQHEEEA RWRRKCEKWT GKVSRNRVDW
     RWTIRDIVMQ AP
//
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