BUD3_ASHGO
ID BUD3_ASHGO Reviewed; 1478 AA.
AC Q9HF61; Q75EV2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Bud site selection protein 3 homolog;
GN Name=BUD3; OrderedLocusNames=AAL016C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RA Dietrich F.S., Voegeli S., Rebischung C., Mohr C., Gaffney T.D.,
RA Philippsen P.;
RT "Sequence of chromosome III intergenic region between BUD3 and GBP2
RT including previously unidentified gene, which is the ortholog of YCL012C in
RT Saccharomyces cerevisiae.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12612612; DOI=10.1038/sj.embor.embor727;
RA Wendland J.;
RT "Analysis of the landmark protein Bud3 of Ashbya gossypii reveals a novel
RT role in septum construction.";
RL EMBO Rep. 4:200-204(2003).
CC -!- FUNCTION: Required for proper septum positioning and septum
CC construction during septation. Acts as a landmark to mark sites for
CC future septation, and as part of a scaffold that recruits components of
CC the contractile ring to the site of septation. Not required to
CC determine the site of lateral branch formation.
CC {ECO:0000269|PubMed:12612612}.
CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:12612612}. Cell
CC septum {ECO:0000269|PubMed:12612612}. Note=Localizes close to the
CC hyphal tip and transiently localizes to septal sites. Initially forms a
CC single ring which subsequently splits into two distinct rings as the
CC septum forms, and disappears after septum completion.
CC -!- SIMILARITY: Belongs to the BUD3 family. {ECO:0000305}.
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DR EMBL; AF210625; AAG41242.1; -; Genomic_DNA.
DR EMBL; AE016814; AAS50350.1; -; Genomic_DNA.
DR RefSeq; NP_982526.1; NM_207879.1.
DR AlphaFoldDB; Q9HF61; -.
DR STRING; 33169.AAS50350; -.
DR EnsemblFungi; AAS50350; AAS50350; AGOS_AAL016C.
DR GeneID; 4618640; -.
DR KEGG; ago:AGOS_AAL016C; -.
DR eggNOG; ENOG502QSNK; Eukaryota.
DR HOGENOM; CLU_001458_0_0_1; -.
DR InParanoid; Q9HF61; -.
DR OMA; VELQYKW; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IEA:EnsemblFungi.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR GO; GO:0007120; P:axial cellular bud site selection; IEA:EnsemblFungi.
DR GO; GO:0000755; P:cytogamy; IEA:EnsemblFungi.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR Gene3D; 1.20.900.10; -; 1.
DR InterPro; IPR021895; Bud3_N.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR Pfam; PF12015; DUF3507; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Reference proteome.
FT CHAIN 1..1478
FT /note="Bud site selection protein 3 homolog"
FT /id="PRO_0000065015"
FT REGION 732..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 144
FT /note="D -> N (in Ref. 1; AAG41242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 165702 MW; 938894AFFBC5CA79 CRC64;
MLTAKQDEVG RELRVATGTS LIEYPVKDWL LRRQPTEWEA LLGEAAIFSG QDELLWGPFV
ACVYREPRTT RLNCLFMDRI GVMHLHSVDV SDTSRFYPAV ENLRPEYRTQ VVRRCLAVGL
LKKYVLLDPS AVRLIRAELP YDYDQTTAGD LANTCELVEG QAARDVGQLL VRLGLVQPRH
VRSLMLDVVY ENHADVVDAN NKLVYYLGEQ LEQLFDPLTE YSPEPTELSY RVPDQVRTSL
SDEMPLMVSI CEELLQLQTN FTLSLVGFLQ KFLIPLRIKA LNEQVPGLST VKLNNIFPPT
IDEVTRINCI FLDALKAALP YGSLEVLKAC SITAPYFYKA YTRHEAATKF FSRDIKSFLS
TFGKSLSDLN FYSEIKLDTL IHGPQEKLTK LKLIIDRLFD SKDWETNEEQ KEADRCYRSI
CDVIDSFGKD EPPNTYDTRV FTPSGKILTE LAKGWPAELQ YKWLKRRVVG VFDVISVTDP
ESRDIVVIFS DYIVFLHVIN GNLYYSGDSK KPLISDVLMN SLINEVPLPP KIPKLEVLSH
SYIDDVVVST YGKNSLRFDT LNAERPSSVA YTLASSSVEA SYVADLCTKA RILEKDTAFH
LFKTAIDSFH VYSTAHESEA YKTERIKSPF VLFLNIPDSI GALQDHNATV GLFASLNKND
KVTLVRLGLD GSREESFASL DNFLSLIIEE LLIFYPSYLS SATSPLFQQL MQINEQLVQT
LLDPKGVHSA SKSKCALRTS KKKKMPANLV STNDNSRTLS PGTIISRTPR TISTITPKQE
KRKSVGQASN SPARGSISTT PRKHKRESIL GKISGLFHKK DKKENKRNSV GSDTRNRHDN
GSVHILRNSS SSFRELESPR QMKRFSSVVH TAVPSSSKRR TSGISPSKGT VNLRALQDAE
NDDNADISKI PIPEGESLFD DTIRVDGVDA DFYAQKDRLS KIYNHDLYGE VVPSAPGSKN
VNVVSGATRE QEKQQNTQKA IARELLASVD QQKRQPTHSA PAESQIVIPG LPQSNVPQIN
FGRSPSFIEL FGGMRLVLDE NDESVNWRRL CSERSLNEKY QIRPATYAGC ISGELAPPVG
IISDQRDSNL SGDNDADTPL PMHSSNKSIL SDETLEKGEF ERDFAISTPK SQTVSDVNAR
RETWGYSHSH DEEIDSEKRA NTKPVSAPAP NVIPGLIITA NSPTKPWHKE NTRIKVSDVR
SEGTDVSYIS SLKKSSNRLV ELSVNSQEDF EDERHTPVIE PIQNPEAPSL IENTETAPVA
SNSSNEETLS KLLGSQGVID LTEETIDYSS INRKHASIQT AYPVLDDVEF STFHMSFGDM
KAEDSHLANQ RESYLFSNST IAGKKDESHG PVFYKLPDFV ADDSYLGYSA VDQHAKHERN
TEIGEEDEAM WVSPSKLDIF DLSKQPESVY KRTSIPAKHA ELLSKMRKDG SVKFEESMFI
RDNSYVYLGQ FLSADEVIEQ QDKKLAANTD EMDSARRL
