ID   EF1D_SHEEP              Reviewed;         277 AA.
AC   Q717R8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
GN   Name=EEF1D;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Dorset; TISSUE=Adipose tissue;
RA   Kenoutis C., Katinakis P., Argyrokastritis A., Rogdakis E.;
RL   Submitted (SEP-2002) 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   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; AF544990; AAQ11745.1; -; mRNA.
DR   RefSeq; NP_001009449.1; NM_001009449.1.
DR   AlphaFoldDB; Q717R8; -.
DR   SMR; Q717R8; -.
DR   STRING; 9940.ENSOARP00000000109; -.
DR   PRIDE; Q717R8; -.
DR   GeneID; 443504; -.
DR   KEGG; oas:443504; -.
DR   CTD; 1936; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   Proteomes; UP000002356; 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; 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..277
FT                   /note="Elongation factor 1-delta"
FT                   /id="PRO_0000326431"
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   277 AA;  30821 MW;  9BB89E7768EF0D40 CRC64;
     MATNFLVHEK IWFDKFKYDD AERKFYEQMN GPVAGSSRQE NGASVILRDI ARARENIQKS
     LAGSAGPGAS SGPSGDHSEL VTRIASLEVE NQSLRGVVQD LQQAVSKLEA RLSALEKSSP
     AHRATTPQTQ HVSPMRQVEP PSRKAATATE DDEDDDIDLF GSDEEEDKEA ARLREERLRQ
     YAEKKAKKPA LVAKSSILLD VKPWDDETDM AQLEACVRSV QLDGLVWGSS KLVPVGYGIR
     KLQIQCVVEC RWGRPLERSH QVEEHVQSVD IAAFNKI