ID   EF1B_XENTR              Reviewed;         228 AA.
AC   Q6DET9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=eef1b;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC077005; AAH77005.1; -; mRNA.
DR   RefSeq; NP_001006877.1; NM_001006876.2.
DR   AlphaFoldDB; Q6DET9; -.
DR   SMR; Q6DET9; -.
DR   STRING; 8364.ENSXETP00000052826; -.
DR   PaxDb; Q6DET9; -.
DR   DNASU; 448658; -.
DR   GeneID; 448658; -.
DR   KEGG; xtr:448658; -.
DR   CTD; 1933; -.
DR   Xenbase; XB-GENE-966955; eef1b2.
DR   eggNOG; KOG1668; Eukaryota.
DR   InParanoid; Q6DET9; -.
DR   OrthoDB; 1464823at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000010098; Expressed in ovary and 27 other tissues.
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..228
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155027"
FT   DOMAIN          2..90
FT                   /note="GST C-terminal"
FT   REGION          70..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..112
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         109
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   228 AA;  25315 MW;  EB5101F32DCA2EAF CRC64;
     MGFGDLKSPA GLKVLNEFLA DKSYIEGYVP SQADVAVFDA LSGAPPADLF HALRWYNHIK
     SYEKQKSSLP GVKKPLGNYG PVNIEDTTGS TAKDTKEEDD DDDIDLFGSD DEEENEESKR
     VREERLAQYE AKKSKKPALI AKSSILLDVK PWDDETDMAK LEECVRSIQM EGLVWGASKL
     VPVGYGIKKL QIQCVVEDDK VGTDVLEENI TAFEDFVQSM DVAAFNKI