ID A0A1B9I905_9TREE Unreviewed; 1014 AA.
AC A0A1B9I905;
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=I206_105129 {ECO:0000313|EMBL:WWC71176.1};
OS Kwoniella pini CBS 10737.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296096 {ECO:0000313|EMBL:WWC71176.1, ECO:0000313|Proteomes:UP000094020};
RN [1] {ECO:0000313|EMBL:WWC71176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10737 {ECO:0000313|EMBL:WWC71176.1};
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:WWC71176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10737 {ECO:0000313|EMBL:WWC71176.1};
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; CP144524; WWC71176.1; -; Genomic_DNA.
DR RefSeq; XP_019013173.1; XM_019154433.1.
DR GeneID; 30171040; -.
DR KEGG; kpin:30171040; -.
DR OrthoDB; 19159at2759; -.
DR Proteomes; UP000094020; Chromosome 6.
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:UP000094020}.
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..65
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..124
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..590
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..684
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 110874 MW; 09232A386F53ADDE CRC64;
MSPVPPPPPA GAFVPSDDWS EDPSFDLSPS AHHFALPTSP SSSSTSSTSH RSHHSISSTS
QHASSPLRQS YTTKGTIKLK KGQDIEELLD GFDDDFDLPD TLPNQTLTGK SRPRPSISSS
ITRTVVGNGP TGIGTITKLG STTTKTPIIK GMDKSRALAI ERSWEADVDF EDALSSLPIE
ALPLRSASSS SVIRRMTLSP PRKGFMPSAD ALDDLGFDLE DEDQATLKAG ATLKAMLPPR
NDPTLRPSRS TNNIINVPST PPAQDPDSIE LESDFALPLN LTNLTLATQP RQSSKLSKQS
KPRQSDASTT TNNTESWGSP SSGAKKWGWG SEDSPSNSGI NKRRSETSAT SISDCLPETS
NESRSKDILV QPNDELGLDE EENMENGLVL PSPTFFSNKR SKELNSILDK KRKPQYAPTV
PNHHQHTSNQ SFKRGHQADD SFEDGLVLDE PGVELSKHRL RSQKQARDKF PSSTLKMNST
TLETGASATR GIAKEREKAR EKQREQGWGR VTPVPLNPSR ERTQSSLGLS FRSNSASATT
LLRENTKRVD SPSLTGREKE SMRSRSGHIH SMLPPPIPST SQLPPLPPPT ISQQTPTSRL
RHQKSHYHIA APPQSPSLTR KQSLASLQDA LADKTFTITD TPRYQFSTSR LTMPTSSSKA
KSRPPISSIF PTSISGPSSS SMSIANQYNP SQRGESVRKV VDMPRRNKTW GDGSELDGID
DLDIDDDHKS TIKGSGISGI GLGKPGRRSL ETSHPFHRTT LVSTKSPPVS SDLTEKRKKS
GSGTTLAKRK HRKPALIKHF GVADKKKVVG EMTWNPSTLR WEGNESILRD FDTVSSSARP
ALITHYTGSS IGGLSSPVGS TASAPRIVGD MQFDPVHMKW ISILSPEDDE PDPFEGMADD
EDEDLGGGTI TRSSGKKFLN KFVTTSNNWT SRLISESSIA SSTTTQNSLN STAWEGANLI
SDELWKECKS AEERHKKEMK GWIMRSTSSS TEIRERERKE SKRLWEIRNL AMKS
//