ID   EF1B_CANAW              Reviewed;         213 AA.
AC   P78590; C4YH21;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=EFB1; ORFNames=CAWG_03362;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=8961551; DOI=10.1111/j.1574-6968.1996.tb08571.x;
RA   Maneu Flores V., Cervera A.M., Martinez J.P., Gozalbo D.;
RT   "Molecular cloning and characterization of a Candida albicans gene (EFB1)
RT   coding for the elongation factor EF-1 beta.";
RL   FEMS Microbiol. Lett. 145:157-162(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; X96517; CAA65366.1; -; Genomic_DNA.
DR   EMBL; CH672349; EEQ45053.1; -; Genomic_DNA.
DR   AlphaFoldDB; P78590; -.
DR   SMR; P78590; -.
DR   STRING; 5476.P78590; -.
DR   COMPLUYEAST-2DPAGE; P78590; -.
DR   EnsemblFungi; EEQ45053; EEQ45053; CAWG_03362.
DR   VEuPathDB; FungiDB:CAWG_03362; -.
DR   HOGENOM; CLU_050172_0_2_1; -.
DR   OMA; FEVKPWD; -.
DR   Proteomes; UP000001429; Chromosome 4, Supercontig 1.4.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd00292; EF1B; 1.
DR   Gene3D; 3.30.70.60; -; 1.
DR   InterPro; IPR036219; eEF-1beta-like_sf.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM01182; EF-1_beta_acid; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF54984; SSF54984; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Protein biosynthesis.
FT   CHAIN           1..213
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155040"
FT   REGION          67..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  23479 MW;  5C1976ADD4DB22CC CRC64;
     MSFSDFSKVE SIKSLNEFLA DKSYIDGTTA TQADVTVYKA FQKEFPQFTR WFNHIASFTE
     EFEDLPAGKA PAASGSAAAA AEEEDDEDVD LFGSDDEVDE EAEKLKQQRL AEYAAKKAAK
     GPKPAAKSIV TLDVKPWDDE TDLDELLTNV KAIEMEGLTW GAHQWIPVGF GIKKLQINLV
     VEDALVSLDD LQAAVEEDED HVQSTDIAAM QKL