BUD4_ASHGO
ID BUD4_ASHGO Reviewed; 1259 AA.
AC Q751K7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Bud site selection protein 4 homolog;
GN Name=BUD4; OrderedLocusNames=AGL306C;
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 [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 [2]
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).
CC -!- FUNCTION: May be involved in the septin organization at the site of
CC septation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000250}. Note=Localizes to two
CC distinct rings on septal sites. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BUD4 family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54185.1; -; Genomic_DNA.
DR RefSeq; NP_986361.1; NM_211423.1.
DR AlphaFoldDB; Q751K7; -.
DR STRING; 33169.AAS54185; -.
DR PRIDE; Q751K7; -.
DR EnsemblFungi; AAS54185; AAS54185; AGOS_AGL306C.
DR GeneID; 4622654; -.
DR KEGG; ago:AGOS_AGL306C; -.
DR eggNOG; ENOG502REBM; Eukaryota.
DR HOGENOM; CLU_257732_0_0_1; -.
DR InParanoid; Q751K7; -.
DR OMA; GSFARCK; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0007120; P:axial cellular bud site selection; IBA:GO_Central.
DR GO; GO:0097271; P:protein localization to bud neck; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Reference proteome.
FT CHAIN 1..1259
FT /note="Bud site selection protein 4 homolog"
FT /id="PRO_0000330078"
FT DOMAIN 1128..1239
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 185..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 140622 MW; 32E8AC3CE5AB7B54 CRC64;
MDEQSSGQDV DQSLDTLLKE IDLKMQLRDG EEGRRASAQS EGSLRLPAVR MLERGMVASA
SHKSVTFDEE PPSVHEYSVV MDSSAGTSEC AEEEREGADG YECAADTMRV LYDEDTDSSC
MGSERALAGP AAEGIVPEGY KEADLLGTER AGSGTPSLSY DDAAGLGSPP HVIFTIKPTS
PLNAYDRGSW EPLQSNTAMD TPPRGGTAVS QHGLFAKAPK LPAIPSPNSR RRVSYAGSDS
YPSDDSATDK RSLTDKTVPD NRGENERGGF GYENSDRNPS IETGTTDEYQ SAGEYKSMSS
SEANDDSKTE ASVEDLRISN KPQRDTTIQD LHATTLPRSS STLIPPALPP LDPSFFGRLA
RSPSYSPIRD RGSSEGSVGE HDSSLEQDHE LGMGQQSART NSSASGNSSD SVMVKPLSLF
SNSQVDSLHL GAPAPDNSTP NKEALPSACP PDAMKSIGTQ TSILEDKAES GPSQSSATSE
KSVMLPNFPR FESFFDDSYP FGHDSDRSNN SVSYSKRTLK PSNYLSIWHL QEAQMRHDSP
AFSANSQFSC KMVGESKRTS LESSRLSAKY ESRFKFKFKP KLVSRRRIYY NKDQWRNFQE
PPTRYYSNCT ESDHISSDVP GTPVSPSIKS RNLCHGRTRG NMKMVERVNS LCSANERLSS
AGNGDETFLS ASSNLDVTSR RPSVDIISEI STKDLLPKIK QDSDGFNELI KTFVDHDEQS
QQTDSTIASY RRGTRDTTIY HIWEHSIQEN SISDYGNSPT AGKGTISKLL DNHEVEFDGK
NSFVTGLGII KKTDQDSRVD VLRIDSTQGI EAIQSFSPYS YRNAFDPVTP TKSAYHGCEA
LQASQMGTPF RPAISTTLQA QSGLGHKRPA VERPTTAQLG NYVSAEMSPE VQEPAEETKK
RTDLQDNGQL YFVFVGIEQL ALRDIERHSA ECSIEFDNGN NVVQSEWLPL PKSGSMSLNQ
EYSVIIAEES LPNMIITLKC RYKSPKKELV EITEKVPLKS KCCGLGKPKY KQVKKLLRRE
MDFDEWDYKI AQDGSFARCK EQIDEELLKN VRYKKQQFRW TLLSEWERDH SKEHKRKRAW
ELPRLPAHPA GALVVDMCYL PRTSRFEKFP KTLQIARRVV NKFKEQKAIA MEGFMWQEGG
DTEVLKRRYF TLNGTQLVAH HEITKKPKAM INLLRVEKLL TEAEISREML SSSSRCFTDL
VLLHECFVLF FENGEEIMFN PDTKTEKLEW IEKLRKVIEL NRFHQPWVKK FLNSSENIL
