ID A0AAF0DDD4_9EURO Unreviewed; 994 AA.
AC A0AAF0DDD4;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=Cytokinesis regulator {ECO:0008006|Google:ProtNLM};
GN ORFNames=PRK78_001768 {ECO:0000313|EMBL:WEW56325.1};
OS Emydomyces testavorans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Nannizziopsiaceae; Emydomyces.
OX NCBI_TaxID=2070801 {ECO:0000313|EMBL:WEW56325.1, ECO:0000313|Proteomes:UP001219355};
RN [1] {ECO:0000313|EMBL:WEW56325.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=16-2883 {ECO:0000313|EMBL:WEW56325.1};
RA Hoyer L.;
RT "Emydomyces testavorans Genome Sequence.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP120627; WEW56325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAF0DDD4; -.
DR Proteomes; UP001219355; Chromosome 1.
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:UP001219355}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..47
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..477
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..618
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..892
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..935
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 108671 MW; 88EC349EDCF39595 CRC64;
MDISPSRLRK PEPQEIECWD DDEDLQCVDD IYFRTTSSAT SVTGSSTRPS GHRDSVSSRR
SCRSDRDSNY GDEESWQLLL NDQDEFGTED AIASAKNAGI PIPDGIPKSA LLGGTIKRLG
GRKGKRALGD DWSDDLDLVG LNGELELRFK HEATSPDSLL HLSSLPTSPS KSRDLEFSTN
SIDHSLALKP LFNDLDKFRD TEEDASFDDV PTIKLAKSRT PPTSNPFAIS TSTKPSAQEE
NIENDLVLPS DGEPLRLSTR QEDSKTPDAL GDEFDAEWAE GSIGVRFGGT KRERFSAHSS
TVTALSPSVS SCLTAESEDE GFDGLILPDG PLDLRNLLQK RRESALPATT GFPPESDPPK
QPDPMTEDFF SGIEIGDGEV FDTEKLTLNR NIKRKVERPV SPVRRGATTI TFSRTAGTRI
PRLSGLERPH STHLEPVSES GAPVSKFARP ASRLGGHATH SSLSNISVSS TSSVSSNPQN
RRPASSRSSK DTLRSEPTTT TVQLLKAQRS SPGLRNYNTG IASALQRSPG RQENNGTVRT
TLSPRPKTPV DRSNADSRLG SQRRSVPFIP AGASPNQSRH ASLKTNRQFR RADSDSSGDI
FTHHRSTSRV SSSSALSDTT RRGSADLPAG SFTATAKHTV TKPNRKRQFG DGTELDIFDD
LPTSATIESK FVKTPIKRGP PRALRNRLSQ SGIPMPLKME GPGSSVAMSP SRQDFTPRFA
RDTNASKQRI ASMNHNQNQK ERETGPLTPI SVNWKSQPFG RPPSSPSMIR NRPGHRHRDS
LSRPQLIKPM GSGVHEPKSV KGMKYNPTLY RWEGNENATA AFDAPLPSSL SKSSLALISN
IGGISGAQVV GSMVFDPQRM CWLKLGSPLP GKTGTTVPPD EDDVFAGLDD LEDRPQKPNT
DSRALSAVGN ADPGDLLTGD DKSGDSSDDW PITEEFDVGP EFIKRQRTEE EKWRRKVSKW
VSEDRKNLGE GWRWAIRDLV KTDGAFNVLT SDKR
//