ID A0A1B9FZA4_9TREE Unreviewed; 1058 AA.
AC A0A1B9FZA4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 10-JUN-2026, entry version 28.
DE RecName: Full=GTPase activator {ECO:0008006|Google:ProtNLM};
GN ORFNames=I302_107177 {ECO:0000313|EMBL:WVW85140.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:WVW85140.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:WVW85140.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:WVW85140.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:WVW85140.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:WVW85140.1};
RA Coelho M.A., David-Palma M., Shea T., Bowers K., McGinley-Smith S.,
RA Mohammad A.W., Gnirke A., Yurkov A.M., Nowrousian M., Sun S., Cuomo C.A.,
RA Heitman J.;
RT "Comparative genomics of Cryptococcus and Kwoniella reveals pathogenesis
RT evolution and contrasting modes of karyotype evolution via chromosome
RT fusion or intercentromeric recombination.";
RL Submitted (FEB-2024) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP144545; WVW85140.1; -; Genomic_DNA.
DR RefSeq; XP_019045169.1; XM_019192172.1.
DR GeneID; 30209956; -.
DR KEGG; kbi:30209956; -.
DR VEuPathDB; FungiDB:I302_05557; -.
DR OrthoDB; 19159at2759; -.
DR Proteomes; UP000092730; Chromosome 5.
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:UP000092730}.
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..54
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..125
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..252
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..386
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..468
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..603
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..697
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..802
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..812
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..990
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1058 AA; 115047 MW; 893AAFF16E49EABB CRC64;
MSPIPPPAGA FVPSDDWTED PSFDLSPSAH HFALPTSPSS SSTSSTSHRS YSNTRQHTSS
PLRQSYTGVT KGTIKLKKRE DVEELLDFDE DFDLPSTQPN NHSTSKLSLS RPRSSTSSSI
TRTIIGNGPS GIGTITKLNS SPVSQPNIMK GTVKARALAI EKSWEADVDF DDDIPTIIPS
KTSSIRRLTL SPPRKGFMPP PDALDELGFD LEEEDQATLK AGATIKAMLP PPKSRRDSTI
KSSKSNTNLN LNVIPVPSTP PNQDPDSIEL ESDFALPLNL TNLTLATQPQ HTRRNSNKPR
ISNASTTTTA TTAESWDSPG SSSHKKGWGW GSEDSPGHSE AHKRRSETSA TSISDALPET
PNESKLKTRN LLVEPDDDLD GADDIENGLV LPSPTFFSNK RSKELNLILD KKRKPQFAPS
PQAHRANTHD DSLRRGHHQD DFFEDGLVLD EPGVELSKHR LKEKKRARDK YPISTLKQRS
AGGPSTSTTK SVAKEREKAW EKQRERDWGR TTPINNNNNA GSAGVRERTH SSLGLSFRSN
SASATTLLKD GGSKRVDSPS LLTGREKESM RSRSGHIHSM LPPPPPIPPT STSSQAPTAT
PSSRLRHQKS HYHLAAQPTP PPSLTRKQSL ASLQDAIADR TFTPSSGVGV GDTPRYHNST
SRLTMPTSSS KAKTRPPINS IFPISSHTPQ SSASSSSFMH PPQHSSHKDG AKRMVDMPKR
HKTWGDGSEL DGIDDLTIDD DHHKSTIKGS AISGLGLGKP SRRGHEPPSS SRLTAKPTPA
PSEHTERRKK SGSGTTSTTT TTAKRKNRKP ALIKHFGVAD KKKVVGDMTW NPSTLRWEGN
ESILRDFDTI SVVSARPALI THYTGSSVGG VSSPVGAAPS APRIVGDMQF DPVQMKWVSI
LSPEEDEPDP FEGMADDEDD EFGFGSGGTI TRSSGRKLVT IGSGGGGGKI SIAGSSNWTA
ISRLASESSV ITSTTTNTNF SSASTSTNQN MDWDDREEGD GGLVSEELWR ECKSAEERHK
KEMKGWVMRG SSSSSEMRER ERKEEKRLWE IRNLAMKS
//
