ID   EF1B_CHICK              Reviewed;         225 AA.
AC   Q9YGQ1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=EEF1B;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn;
RA   Ghatpande S.K., Siddiqui M.A.Q.;
RT   "Developmental expression of chicken peptide elongation factor 1-beta.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP. {ECO:0000250}.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation affects the GDP/GTP exchange rate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; AF103726; AAD16874.1; -; mRNA.
DR   RefSeq; NP_990232.1; NM_204901.1.
DR   AlphaFoldDB; Q9YGQ1; -.
DR   BMRB; Q9YGQ1; -.
DR   SMR; Q9YGQ1; -.
DR   PaxDb; Q9YGQ1; -.
DR   GeneID; 395723; -.
DR   KEGG; gga:395723; -.
DR   CTD; 1933; -.
DR   VEuPathDB; HostDB:geneid_395723; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   InParanoid; Q9YGQ1; -.
DR   PRO; PR:Q9YGQ1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Elongation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..225
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155025"
FT   DOMAIN          2..84
FT                   /note="GST C-terminal"
FT   REGION          80..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  24762 MW;  41C8CDB3D28139FB CRC64;
     MGFGDLKSAA GLRVLNDFLA DKSYIEGYVP SQADIAVFEA VGAPPPADLF HALRWYNHIK
     SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
     ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV
     GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI