ID   EF1G_PRUAV              Reviewed;         422 AA.
AC   Q9FUM1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
OS   Prunus avium (Cherry) (Cerasus avium).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=42229;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu Z., Wiersma P.A.;
RT   "A full length cDNA for translation elongation factor 1-gamma cloned from
RT   sweet cherry fruit.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components. {ECO:0000250}.
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC       gamma. {ECO:0000250}.
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; AF297712; AAG17901.1; -; mRNA.
DR   AlphaFoldDB; Q9FUM1; -.
DR   SMR; Q9FUM1; -.
DR   PRIDE; Q9FUM1; -.
DR   Proteomes; UP000515124; Unplaced.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   Gene3D; 3.30.70.1010; -; 1.
DR   InterPro; IPR044628; EF-1-gamma_plant.
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   PANTHER; PTHR44372; PTHR44372; 1.
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   2: Evidence at transcript level;
KW   Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..422
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208829"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          87..215
FT                   /note="GST C-terminal"
FT   DOMAIN          262..422
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          210..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  47986 MW;  6A03408886C82167 CRC64;
     MALVLHAGKT NKNAFKTLIV AEYTGVKVEL APDFEMGVTN KTPEYLKLNP IGKVPLLETP
     DGPIFESNAI ARYVARLKAD NPLIGSSLID YAHIEQWIDF GSLEIDANII SWFRPRFGYA
     VYLPPAEEAA ISALKRALGA LNTHLASNTY LVGHFVTLAD IIVTCNLFFG FTKLMIKSFT
     SEFPHVERYF WTLVNQPKFK KVLGDVKQTE SVPPVPSAKK PSQPKETKSK AKEEPKKEAK
     KEPAKPKAEA AEEVEEAPKP KPKNPLDLLP PSNMVLDDWK RLYSNTKTNF REVAIKGFWD
     MYDPEGYSLW FCEYKYNDEN TVSFVTLNKV GGFLQRMDLA RKYAFGKMLV IGSEPPFKVK
     GLWLFRGQEI PPFVMEECYD MELYNWTKVD LSDENQKERV NQVIEDQEPF EGEALLDAKC
     FK