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Database: UniProt
Entry: A0A0D0A7A1_9AGAM
LinkDB: A0A0D0A7A1_9AGAM
Original site: A0A0D0A7A1_9AGAM 
ID   A0A0D0A7A1_9AGAM        Unreviewed;       882 AA.
AC   A0A0D0A7A1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   02-APR-2025, entry version 25.
DE   RecName: Full=Protein byr4 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PISMIDRAFT_21066 {ECO:0000313|EMBL:KIK30372.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK30372.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK30372.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK30372.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN833687; KIK30372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D0A7A1; -.
DR   HOGENOM; CLU_009682_0_0_1; -.
DR   OrthoDB; 297219at2759; -.
DR   Proteomes; UP000054018; 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:0001100; P:negative regulation of exit from mitosis; IEA:InterPro.
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:UP000054018}.
FT   REGION          153..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..177
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..268
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..311
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..365
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..822
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   882 AA;  95227 MW;  B60F915C3996BB34 CRC64;
     MTAVPAPITL QSREEWHDAD FDLPEGDHIR SLVVESDKED EDDGMDWDTE LDFGKTGGAK
     AKAVVSAMAA RNGLPGLGSG GMVTIRPPLT CQEEEEEEED EEGVSTIKVA HLPKATVCRP
     PPTTIDEDFE SAFALPSDLT QLSLAPLPLS HRSSKNSLEW GDKDQTSSSQ SSDAYSTLGF
     ADACSSNSAS SISLPGTEES DCEENESELE GLVIPLGLFE SCQSGKHLKK LLEIKKKTQI
     ADHRVKPAYP DPEDDFETGL VIEDDDDFNP SRLVSAKQPQ YPATRSKSVP ARAPPPARPP
     SRLRAARAKS PVNPPISSAR QLQRIKLSSS PPPPAPISSR TYKEALVTVP PTSTSTLLSP
     KPGSLRGQKS HSGLKPPTPP SQRKGLTRKA SLSSLMETST SQAGGSGTVS AVGSSMITKP
     TRYDAPTAAS RAKSHTGSTS RLHALDFMVP PARPSTPSSN PAALRLTMPT SLRVKSRPSL
     ASVFPGSSPN PSPQLTHRAT SPIPPRPPST SSLRKGGAST QMPSSAPSIA PKLLRRPKRQ
     RTYGDGTELD GFDDLPTDRE KECKFRVQPR ATSRSIINGA PKSSDKEKET GTMRKKGRKD
     GRSPTPATFT PSINTLRRTG RFELSKISAP TVEPVLRKKK DASSPVLGHT RRKPTLIRHL
     GAPGGPKGVN FLVVCGMRWN PLTLRWEGND QVLRDFDAVV GTSTRPALIT HLTGSSIGSP
     VGSFASGARK VGNMIFDPVR MCWISTLPPD EEEPDVFADL ADDEDEEAWE TKGGTIRASQ
     QSSITPATQD TSGHRSSIVV TAPSPARSRT RTNSESESDR GSRASIVYDV ADDFVEVCRS
     AEVRHRSEMR GWRSQASRQT DPFAEPNRSF LYEIRALATR KY
//
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