ID   EF1D_BOVIN              Reviewed;         280 AA.
AC   A5D989;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
GN   Name=EEF1D;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ12948.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT030508; ABQ12948.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001193549.1; NM_001206620.2.
DR   AlphaFoldDB; A5D989; -.
DR   SMR; A5D989; -.
DR   STRING; 9913.ENSBTAP00000019499; -.
DR   PaxDb; A5D989; -.
DR   PeptideAtlas; A5D989; -.
DR   PRIDE; A5D989; -.
DR   GeneID; 516473; -.
DR   KEGG; bta:516473; -.
DR   CTD; 1936; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   HOGENOM; CLU_050172_1_0_1; -.
DR   InParanoid; A5D989; -.
DR   OrthoDB; 1464823at2759; -.
DR   TreeFam; TF313134; -.
DR   Proteomes; UP000009136; 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; 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; SSF54984; SSF54984; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Elongation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   CHAIN           2..280
FT                   /note="Elongation factor 1-delta"
FT                   /id="PRO_0000326430"
FT   REGION          113..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q68FR9"
FT   MOD_RES         107
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         117
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P57776"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         129
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         162
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
SQ   SEQUENCE   280 AA;  31142 MW;  4BC1D4AAA1F5AC71 CRC64;
     MATNFLMHEK IWFDKFKYDD AERKFYEQMN GPVAGSSRQE NGASVILRDI ARARENIQKS
     LAGSSGPGAS SGPSGDHSEL VTRIASLEVE NQSLRGVVQD LQQAVSKLEA RLSALEKSSP
     AHRATTPQTQ HVSPMRQVEP PSRKAATATE DDEDDDIDLF GSDEEEDKEA TRLREERLRQ
     YAEKKAKKPA LVAKSSILLD VKPWDDETDM AQLEACVRSV QLDGLVWGSS KLVPVGYGIR
     KLQIQCVVED DKVGTDQLEE EITKFEEHVQ SVDIAAFNKI