ID   EF1D_ARTSA              Reviewed;         237 AA.
AC   P32192;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
OS   Artemia salina (Brine shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=85549;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8049261; DOI=10.1016/0167-4781(94)90187-2;
RA   Amons R., Guerrucci M.A., Karssies R.H., Morales J., Cormier P.,
RA   Moeller W., Belle R.;
RT   "The leucine-zipper in elongation factor EF-1 delta, a guanine-nucleotide
RT   exchange protein, is conserved in Artemia and Xenopus.";
RL   Biochim. Biophys. Acta 1218:346-350(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 101-165.
RA   van Bussel F.J., Janssen G.M.C.;
RL   Submitted (NOV-1993) to UniProtKB.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-31; 102-119; 152-162; 176-196 AND 218-228.
RX   PubMed=2207149; DOI=10.1016/0167-4781(90)90174-z;
RA   van Damme H.T.F., Amons R., Karssies R., Timmers C.J., Janssen G.M.C.,
RA   Moeller W.;
RT   "Elongation factor 1 beta of artemia: localization of functional sites and
RT   homology to elongation factor 1 delta.";
RL   Biochim. Biophys. Acta 1050:241-247(1990).
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}.
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   PIR; S47630; S47630.
DR   AlphaFoldDB; P32192; -.
DR   SMR; P32192; -.
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.
FT   CHAIN           1..237
FT                   /note="Elongation factor 1-delta"
FT                   /id="PRO_0000155050"
FT   REGION          97..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        153
FT                   /note="S -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="L -> I (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="F -> T (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="K -> S (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   237 AA;  26318 MW;  8D64A5A112446ABE CRC64;
     MRGDNFLYQE KFYYEDAERT FQEHLAGTYK PKPTAVTETL SGVLPSNTLK QLESAVALSN
     KVEALSSENK ELKKCIDGLQ GLLLGLRQRI ETLEGKTTGA KLAAPPQKEE EDDDVDLFGS
     DEESEEAEKV KAERIAAYQA KKSHKPTVIA KSSILLDIKP WDDETDMGAM EREVRSIAMD
     GLIWGASKLV PVAFGVKKLQ ISCVVEDDKV SVDELVEKIE AFEDYVQSVD IAAFNKI