ID   EF1B_RABIT              Reviewed;         225 AA.
AC   P34826;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=EEF1B; Synonyms=EF1B;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-106.
RC   STRAIN=New Zealand white;
RX   PubMed=8547318; DOI=10.1016/0167-4781(95)00166-2;
RA   Chen C.J., Traugh J.A.;
RT   "Expression of recombinant elongation factor 1 beta from rabbit in
RT   Escherichia coli. Phosphorylation by casein kinase II.";
RL   Biochim. Biophys. Acta 1264:303-311(1995).
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.
CC       {ECO:0000269|PubMed:8547318}.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; X74728; CAA52741.1; -; mRNA.
DR   PIR; S62693; S62693.
DR   RefSeq; NP_001075868.1; NM_001082399.1.
DR   AlphaFoldDB; P34826; -.
DR   BMRB; P34826; -.
DR   SMR; P34826; -.
DR   STRING; 9986.ENSOCUP00000019358; -.
DR   iPTMnet; P34826; -.
DR   PRIDE; P34826; -.
DR   GeneID; 100009286; -.
DR   KEGG; ocu:100009286; -.
DR   CTD; 1933; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   InParanoid; P34826; -.
DR   OrthoDB; 1464823at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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   Acetylation; Elongation factor; Isopeptide bond; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..225
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155023"
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         7
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         88
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O70251"
FT   MOD_RES         93
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         95
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         106
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:8547318"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   CROSSLNK        147
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
SQ   SEQUENCE   225 AA;  24749 MW;  EE8B095443DF148A CRC64;
     MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSGPPPADLC HALRWYNHIK
     SYEKEKASLP GIKKALGTYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE
     ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMVKLEE CVRSIQADGL VWGSSKLVPV
     GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI