ID   EF1G_ARTSA              Reviewed;         430 AA.
AC   P12261;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
OS   Artemia salina (Brine shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=85549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3666137; DOI=10.1016/0014-5793(87)80532-x;
RA   Maessen G.D.F., Amons R., Zeelen J.P., Moeller W.;
RT   "Primary structure of elongation factor 1 gamma from Artemia.";
RL   FEBS Lett. 223:181-186(1987).
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components.
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC       gamma.
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DR   EMBL; M28020; AAC83401.1; -; mRNA.
DR   AlphaFoldDB; P12261; -.
DR   SMR; P12261; -.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.70.1010; -; 1.
DR   InterPro; IPR001662; EF1B_G_C.
DR   InterPro; IPR036433; EF1B_G_C_sf.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00647; EF1G; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SMART; SM01183; EF1G; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF89942; SSF89942; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Elongation factor; Protein biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..430
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208822"
FT   DOMAIN          2..84
FT                   /note="GST N-terminal"
FT   DOMAIN          85..213
FT                   /note="GST C-terminal"
FT   DOMAIN          271..430
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          232..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  49309 MW;  2AEA4ED040B3B383 CRC64;
     MVAGKLYTYP ENFRAFKALI AAQYSGAKLE IAKSFVFGET NKSDAFLKSF PLGKVPAFES
     ADGHCIAESN AIAYYVANET LRGSSDLEKA QIIQWMTFAD TEILPASCTW VFPVLGIMQF
     NKQATARAKE DIDKALQALD DHLLTRTYLV GERITLADIV VTCTLLHLYQ HVLDEAFRKS
     YVNTNRWFIT LINQKQVKAV IGDFKLCEKA GEFDPKKYAE FQAAIGSGEK KKTEKAPKAV
     KAKPEKKEVP KKEQEEPADA AEEALAAEPK SKDPFDEMPK GTFNMDDFKR FYSNNEETKS
     IPYFWEKFDK ENYSIWYSEY KYQDELAKVY MSCNLITGMF QRIEKMRKQA FASVCVFGED
     NDSSISGIWV WRGQDLAFKL SPDWQIDYES YDWKKLDPDA QETKDLVTQY FTWTGTDKQG
     RKFNQGKIFK