ID   EF1G_BOVIN              Reviewed;         440 AA.
AC   Q3SZV3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
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;
GN   Name=EEF1G;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; BC102691; AAI02692.1; -; mRNA.
DR   RefSeq; NP_001035577.1; NM_001040487.2.
DR   AlphaFoldDB; Q3SZV3; -.
DR   BMRB; Q3SZV3; -.
DR   SMR; Q3SZV3; -.
DR   STRING; 9913.ENSBTAP00000015716; -.
DR   PaxDb; Q3SZV3; -.
DR   PeptideAtlas; Q3SZV3; -.
DR   PRIDE; Q3SZV3; -.
DR   GeneID; 326581; -.
DR   KEGG; bta:326581; -.
DR   CTD; 1937; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   InParanoid; Q3SZV3; -.
DR   OrthoDB; 1341490at2759; -.
DR   Proteomes; UP000009136; Unplaced.
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   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..440
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000284654"
FT   DOMAIN          2..87
FT                   /note="GST N-terminal"
FT   DOMAIN          88..216
FT                   /note="GST C-terminal"
FT   DOMAIN          279..440
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          221..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..263
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         404
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         437
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         437
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        256
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CROSSLNK        288
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
SQ   SEQUENCE   440 AA;  50378 MW;  295A874E422B825C 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
     KLKPQAERKE GKEEKKAAAP APEEELDECE QALAAEPKAK DPFAHLPKST FVLDEFKRKY
     SNEDTLSVAL PYFWDHFDKD GWSLWYSEYR FPEELTQTFM SCNLITGMFQ RLDKLRKNAF
     ASVILFGTNN SSSISGVWDF RGQELAFPLS PDWQVDYESY TWRKLDPGSE ETQTLVREYF
     CWEGAFQHVG KAFNQGKIFK