ID   EF1B_PIG                Reviewed;         224 AA.
AC   P29412; Q7M397;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=EEF1B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RA   Amons R., Schipper A., van Damme H.T.F., Kriek J., Moeller W.;
RT   "The primary structure of elongation factor 1-beta from pig liver.";
RL   J. Protein Chem. 11:404-404(1992).
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   PIR; A61442; A61442.
DR   PeptideAtlas; P29412; -.
DR   PRIDE; P29412; -.
DR   InParanoid; P29412; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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; 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; PF00736; EF1_GNE; 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; Direct protein sequencing; Elongation factor; Isopeptide bond;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT   CHAIN           1..224
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155024"
FT   REGION          79..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         87
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O70251"
FT   MOD_RES         92
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
FT   CROSSLNK        146
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P24534"
SQ   SEQUENCE   224 AA;  24642 MW;  AE4FA09DAEDB41B3 CRC64;
     GFGDLKSPAG LQVLNDYLAD KSYIEGYVPS QADVAVFEAV SXPPPAXLXX XXXWYNHIKX
     YEKEKASLPG VKKALGKYGP ANVEDTTESG ATDSKDDDDI DLFXXXXXXX XXXAKXLREE
     RLAQYESKKA KKPALVAKSX XXXXVKPWDD EXXMAKLEEX VXSIQADGLV XXXXXLVPVG
     YGIKXXXXXX XXXDDKVGTD MLEEQITAFE DYVQSMDVAA FNKI