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Database: UniProt
Entry: A0A5N5WYQ4_9EURO
LinkDB: A0A5N5WYQ4_9EURO
Original site: A0A5N5WYQ4_9EURO 
ID   A0A5N5WYQ4_9EURO        Unreviewed;       985 AA.
AC   A0A5N5WYQ4;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   02-APR-2025, entry version 12.
DE   RecName: Full=Cytokinesis regulator {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BDV29DRAFT_176581 {ECO:0000313|EMBL:KAB8072825.1};
OS   Aspergillus leporis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=41062 {ECO:0000313|EMBL:KAB8072825.1, ECO:0000313|Proteomes:UP000326565};
RN   [1] {ECO:0000313|EMBL:KAB8072825.1, ECO:0000313|Proteomes:UP000326565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 151.66 {ECO:0000313|EMBL:KAB8072825.1,
RC   ECO:0000313|Proteomes:UP000326565};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML732238; KAB8072825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N5WYQ4; -.
DR   OrthoDB; 19159at2759; -.
DR   Proteomes; UP000326565; 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:UP000326565}.
FT   REGION          42..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..240
FT                   /note="Basic and 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        403..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..482
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..543
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..588
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..600
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        615..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        708..718
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  107475 MW;  44B9BA474A5CCA26 CRC64;
     MESLTLQVQH GDEETIECWD DDDDLQCYED IHLRTASSAT SVTNLSVRRS GHRDSISSRR
     SGRSDIDSNA GGDEDWQVQL LDNEEGVNEE AIASAKNAGI PLPANLPRSA LVGGTIKRLG
     RRKPKQNFVD DWSEDVEFPG PGAVLELKSP HEASFPESLR QISSATTSPV KASASPFWGD
     EISSRLQSTF SGLDKYQVDD SVDDSVDDVP TIKAPRSRSP RGTGFLNDSR PDDQNDALEK
     FDEDFELPTD DFSLQLSHRK VNSGIASPTP DDLDVDWSEG SIGVRFGGTT RDYRSNPSSS
     VSVVSPSASS CLTAESEDEG LEGLIIPDGP LDLETSLKKR QDSKHVSLSH SEPVKTSHEP
     PSADDFFSGL EIEDDNVFHS RKLSINPNVK CKTECPGSPA RRSATTLTFT NTTVSPKTRI
     PRLSGHDRPH STHLETVSES GAPLSKFRSP PGRAGGHSSH SSLSSLAPSG STSVSPIPST
     PSRRLPGTRI PKGSVGGERV TAGSKLLKTK RSMPSMRNTQ QAATPTFQRL PSHQDGLNFS
     TIRPKTPVDR IDDARSLSRK SQAPFIPAGA SENQSHHASV KSYRHSRRTN SDSSNDTFNS
     QAPSRLSRSG RHDVFSNNTN DSSPETQVAS AKRTLTRPTR RRNFGDGTEL ASFDDLPTSS
     SAESRFVKLP SGRGVPRSLK SRLNRSQTIS SRVETPTPQQ TVLGISSKAE DSTPRFARDT
     NASRNAREQR IASLTFNSKN RDSNPLTSLN AIWKAQTVPR VPSSSTTLRS RKNRPAVAGC
     KPHLIKPLGT GVQEPKSVNG MQYNPASFRW EGNEGLIQEF EPTPPKSPKP APALITNVGT
     MQNVQVVGGM VFDPQRMCWL KLAPLQPGTK GLVAVEDDDD VFAGLGELVE KAGSSGMRNS
     GAYDDLGLGA SGDDRSCGDS SDEWPMTEEF DVGPEFIRRQ RAEEEKWRRK VDKWVNFDRM
     KFGDGWRWAI RDLVQFNSAR DHCGG
//
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