ID   BUD3_DEBHA              Reviewed;        1345 AA.
AC   Q6BIF0; B5RUQ3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Bud site selection protein 3;
GN   Name=BUD3; OrderedLocusNames=DEHA2G11000g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Co-assembles with BUD4 at bud sites. BUD4 and BUD3 may
CC       cooperate to recognize a spatial landmark (the neck filaments) during
CC       mitosis and they subsequently become a landmark for establishing the
CC       axial budding pattern in G1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BUD3 family. {ECO:0000305}.
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DR   EMBL; CR382139; CAR65947.1; -; Genomic_DNA.
DR   RefSeq; XP_002770613.1; XM_002770567.1.
DR   AlphaFoldDB; Q6BIF0; -.
DR   STRING; 4959.XP_002770613.1; -.
DR   PRIDE; Q6BIF0; -.
DR   EnsemblFungi; CAR65947; CAR65947; DEHA2G11000g.
DR   GeneID; 8999172; -.
DR   KEGG; dha:DEHA2G11000g; -.
DR   VEuPathDB; FungiDB:DEHA2G11000g; -.
DR   eggNOG; ENOG502QSNK; Eukaryota.
DR   HOGENOM; CLU_004185_0_0_1; -.
DR   InParanoid; Q6BIF0; -.
DR   OMA; HEANLKN; -.
DR   OrthoDB; 664242at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR021895; Bud3_N.
DR   InterPro; IPR000219; DH-domain.
DR   Pfam; PF12015; DUF3507; 1.
DR   SMART; SM00325; RhoGEF; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Reference proteome.
FT   CHAIN           1..1345
FT                   /note="Bud site selection protein 3"
FT                   /id="PRO_0000295639"
FT   REGION          843..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          951..998
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        962..978
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1345 AA;  154212 MW;  747537FC3340EEB5 CRC64;
     MSVYHRYASG EYDKTYFEKA SESRKHDDKV GRIQISPLLG QFSTSDTLYK FKEKSIEEWL
     AIFPKAAYFK GYDESLFGNV IIMVYENSHT GKLNTTSFSK FGVTSYDNLV LDARSRFWPS
     CENLLPSYQK SNVRRSLAIT NLKNYNKLVN SPGNFYVNKS WDETYAGSLA NNMQLISEKK
     PEKFGLKLLE LGLLQTHCIQ STVLDVIYDN ASSETSDKIV EENNKLVFLI GSQLEQLFDP
     LLEYSPEIME FSYTVPVDAI SPQIKNNELI NTIISELLTV QTNFTMRLVN LLQNFIIPLR
     IHVLAATSSS GITKINQVFP PTIDEITRIN CILHDSLKKA SAFGYVEIMK AVGTIMPYFY
     KAFIRHEANL KNFRDNLAKF HSKNNKKIFE NTMINKGNLG IRDIDSIVAG SLLELPKLKL
     ILVRLKDSII FEKTKLSNFE DDPSNEFFTI EKYFNSAVDV IDAFGFEEEN NQTKIDIRQR
     VFTPTGKILT ELASNWPPEL QYGWLARKVV GIYEMRNIKP LNDTFYDLDI LIIFSDHILF
     LTIVDDSYYN ERNNESMKNL CVSDILMHSL VNDKPLPNLK SLPTMEVNCW CIINEVITTT
     YKGVSPITSK TQEFLKFVNI SKTGFKNNNA ENSTISKNYE ILDGSDRGNV DGCKIIELIN
     KSTVLNKRKP FHLFRSNDPK LHIYSIAQEL SAYQEESCKS PMALYLNLSI HDPKKYFEEN
     QTVHFVLNAS FINDHQIHMV GFNRAETFEL NEIISSNDLQ VCLKEVIVKN FSLLFNTFSN
     ISKMLTQGYA YDINYCANIF TQIDEIKLNE HRQEIAKNKS TDSISRPKTR NVSEIISIPE
     VYMNKISPSN TNTRDQRSQQ RRTEKRLSTR SKNNSRDVEV KKSSQERPDK RNSMIKKVFR
     SLRRSFDGIE NSTPKTEIHE NNNTSKLQDS SSFSGKKNEY TSLYKPVPQL QTKEQKHVHE
     QVQVQEQGQG QGQGQEQEQG QEQEKEQEQS FSEANIPRDI DNYTGIQMRK ECNNSVQQSR
     NTSGSLDVNS HFEFPPHLDS SFGSNNNTII LVNDNENRHK NRPAPEKISI LDSTDDHSSN
     IPRRSENVGY GKFNVEDFYD DGEANWVSIS NENYSLLNAE IRALKEEAHM DTEDIIELND
     SDNITEDEMR DVYESKDFDA FYTPQNQSVA QFGDNPTSLK NENREMSTQS LASSEIIEVF
     GKQIDSNFRS DYIPNLNENL HSINSNKKFG FQNDHRFSVL TSSDDEFFSS DDFASSLPIE
     RQENKKSHSP MIMNSSSSDA TIINENFEEK LLPATPIDCD DKVLPSSQIH KNMQSSSIRS
     DSFSTTYESM TYLSEILNGH LNFSD