ID   EF1G_HORSE              Reviewed;         437 AA.
AC   A2Q127;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
GN   Name=EEF1G;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Thoroughbred; TISSUE=Tendon;
RA   Hasegawa T., Hayashi K., Kagawa Y., Akiyama Y., Suzuki Y., Sugano S.,
RA   Ishida N.;
RT   "Cloning of genes expressed in equine tendon.";
RL   Submitted (FEB-2007) 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}.
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DR   EMBL; AB292250; BAF46268.1; -; mRNA.
DR   RefSeq; NP_001075254.1; NM_001081785.1.
DR   AlphaFoldDB; A2Q127; -.
DR   BMRB; A2Q127; -.
DR   SMR; A2Q127; -.
DR   STRING; 9796.ENSECAP00000012558; -.
DR   PaxDb; A2Q127; -.
DR   PeptideAtlas; A2Q127; -.
DR   PRIDE; A2Q127; -.
DR   GeneID; 100009686; -.
DR   KEGG; ecb:100009686; -.
DR   CTD; 1937; -.
DR   HOGENOM; CLU_011226_3_1_1; -.
DR   InParanoid; A2Q127; -.
DR   OMA; TRWYETI; -.
DR   OrthoDB; 1341490at2759; -.
DR   TreeFam; TF314343; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006414; P:translational elongation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Elongation factor; Isopeptide bond; Protein biosynthesis;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CHAIN           2..437
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000286045"
FT   DOMAIN          2..87
FT                   /note="GST N-terminal"
FT   DOMAIN          88..216
FT                   /note="GST C-terminal"
FT   DOMAIN          276..437
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          221..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         147
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         212
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         401
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         434
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         434
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        253
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CROSSLNK        285
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
SQ   SEQUENCE   437 AA;  50049 MW;  DC9F0CDF139E68C2 CRC64;
     MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
     FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
     MHHNKQATEN AKEEVRRILG LLDAHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
     RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
     KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
     DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
     ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEEAQ TLVREYFSWE
     GAFQHVGKAF NQGKIFK