ID   EF1D_XENLA              Reviewed;         265 AA.
AC   P29693;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
DE   AltName: Full=P36;
GN   Name=eef1d;
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].
RC   TISSUE=Oocyte;
RX   PubMed=1508694; DOI=10.1093/nar/20.15.4091;
RA   Morales J., Cormier P., Mulner-Lorillon O., Poulhe R., Belle' R.;
RT   "Molecular cloning of a new guanine nucleotide-exchange protein, EF1
RT   delta.";
RL   Nucleic Acids Res. 20:4091-4091(1992).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 15-27; 112-118; 186-192 AND 226-259.
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   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; X66837; CAA47313.1; -; mRNA.
DR   PIR; S26280; S26280.
DR   RefSeq; NP_001081523.1; NM_001088054.2.
DR   AlphaFoldDB; P29693; -.
DR   SMR; P29693; -.
DR   BioGRID; 99230; 1.
DR   IntAct; P29693; 1.
DR   iPTMnet; P29693; -.
DR   DNASU; 397892; -.
DR   GeneID; 397892; -.
DR   KEGG; xla:397892; -.
DR   CTD; 397892; -.
DR   Xenbase; XB-GENE-958974; eef1d.S.
DR   OrthoDB; 1464823at2759; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 397892; Expressed in spleen 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; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Elongation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..265
FT                   /note="Elongation factor 1-delta"
FT                   /id="PRO_0000155049"
FT   REGION          31..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..149
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   265 AA;  29237 MW;  61A1898EC3F9E402 CRC64;
     MSAFVITTEQ VWLDKYKYDD AEKQYYENLS MGSASNKPHN SPQSAASALS NSGDGSELAA
     RVANLEQENQ SLHKVVKDLQ SAISKLESRL STLEKSSKSQ KPAAASQPAI EVAARVQKVQ
     VTPAAKEENG TGEDDDDDDD IDLFGSDNEE EDAEAARIRE ERLKQYAEKK SKKPGVIAKS
     SILLDVKPWD DETDMAKLEE CVRTVQMDGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT
     DILEEEITKF EDYVQSVDIA AFNKI