ID   EF1B_XENLA              Reviewed;         227 AA.
AC   P30151;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
DE   AltName: Full=p30;
GN   Name=eef1b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-26; 148-154 AND
RP   208-220.
RC   TISSUE=Ovary;
RX   PubMed=8441685; DOI=10.1093/nar/21.3.743;
RA   Cormier P., Osborne B., Morales J., Bassez T., Minella O., Mulner O.,
RA   Belle R., Mulner-Lorillon O.;
RT   "Elongation factor 1 contains two homologous guanine-nucleotide exchange
RT   proteins as shown from the molecular cloning of beta and delta subunits.";
RL   Nucleic Acids Res. 21:743-743(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 18-26; 148-154 AND 208-220.
RX   PubMed=2676593; DOI=10.1016/0014-5793(89)81069-5;
RA   Belle R., Derancourt J., Poulhe R., Capony J.-P., Ozon R.,
RA   Mulner-Lorillon O.;
RT   "A purified complex from Xenopus oocytes contains a p47 protein, an in vivo
RT   substrate of MPF, and a p30 protein respectively homologous to elongation
RT   factors EF-1 gamma and EF-1 beta.";
RL   FEBS Lett. 255:101-104(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 148-153 AND 207-220.
RX   PubMed=1869528; DOI=10.1016/s0021-9258(18)98559-5;
RA   Janssen G.M.C., Morales J., Schipper A., Labbes J.C., Mulner-Lorillon O.,
RA   Belle R., Moeller W.;
RT   "A major substrate of maturation promoting factor identified as elongation
RT   factor 1 beta gamma delta in Xenopus laevis.";
RL   J. Biol. Chem. 266:14885-14888(1991).
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   -!- 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; X69764; CAA49418.1; -; mRNA.
DR   PIR; S30223; S30223.
DR   RefSeq; NP_001084134.1; NM_001090665.1.
DR   AlphaFoldDB; P30151; -.
DR   SMR; P30151; -.
DR   BioGRID; 100651; 1.
DR   IntAct; P30151; 2.
DR   DNASU; 399326; -.
DR   GeneID; 399326; -.
DR   KEGG; xla:399326; -.
DR   CTD; 399326; -.
DR   Xenbase; XB-GENE-966960; eef1b2.L.
DR   OrthoDB; 1464823at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 399326; Expressed in oocyte and 19 other tissues.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Elongation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..227
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155026"
FT   DOMAIN          2..90
FT                   /note="GST C-terminal"
FT   REGION          83..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         108
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        210
FT                   /note="T -> G (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   227 AA;  25175 MW;  D040FF5A9E48D702 CRC64;
     MGFGDLKSPA GLKVLKEFLA DKSYIEGYVP SQADVAVFDA LSAAPPADLF HALRWYNHIK
     SYEKQKSSLP GVKKALGNYG PVNIEDTTGS AAKETKEEDD DDIDLFGSDD EEESEDAKRV
     RDERLAQYEA KKSKKPTLIA KSSILLDVKP WDDETDMGKL EECLRSIQMD GLLWGSSKLV
     PVGYGIKKLQ IQCVVEDDKV GTDVLEEKIT AFEDFVQSMD VAAFNKI