ID   EF1G_PIG                Reviewed;         432 AA.
AC   Q29387; Q8SPX8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
DE   Flags: Fragment;
GN   Name=EEF1G;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kokuho T.;
RT   "cDNA cloning of porcine eukaryotic elongation factor(eEF)-1 gamma-like
RT   protein.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-142.
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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; AF480162; AAL85414.1; -; mRNA.
DR   EMBL; F14608; CAA23152.1; -; mRNA.
DR   AlphaFoldDB; Q29387; -.
DR   BMRB; Q29387; -.
DR   SMR; Q29387; -.
DR   STRING; 9823.ENSSSCP00000013894; -.
DR   PaxDb; Q29387; -.
DR   PeptideAtlas; Q29387; -.
DR   PRIDE; Q29387; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   HOGENOM; CLU_011226_3_1_1; -.
DR   InParanoid; Q29387; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q29387; SS.
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   CHAIN           <1..432
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208815"
FT   DOMAIN          <1..82
FT                   /note="GST N-terminal"
FT   DOMAIN          83..211
FT                   /note="GST C-terminal"
FT   DOMAIN          271..432
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          216..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         207
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         396
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT   MOD_RES         429
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   MOD_RES         429
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        248
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   CROSSLNK        280
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P26641"
FT   NON_TER         1
SQ   SEQUENCE   432 AA;  49624 MW;  05AA91DDA100BFBC CRC64;
     LYTYPENWRA FKALIAAQYS GAQVRVLSAP PHFHFGQTNH TPEFLRKFPA GKVPAFEGDD
     GFCVFESNAI AYYVSNEELR GSTPEAAAQV VQWVSFADSD IVPPASTWVF PTLGIMHYNK
     QATENAKDEV RRVLGLLDAH LKTRTFLVGE RVTLADITVV CTLLWLYKQV LEPSFRQAFP
     NTNRWFLTCI NQPQFRAVLG EVKLCEKMAQ FDAKKFAESQ PKKDTPRKEK GSREEKQKPQ
     AERKEEKKAA APAPEEELDE CEQALAAEPK AKDPFAHLPK STFVLDEFKR KYSNEDTLSV
     ALPYFWEHFD KDGWSLWYSE YRFPEELTQT FMSCNLITGM FQRLDKLRKN AFASVILFGT
     NNSSSISGVW VFRGQELAFP LSPDWQVDYE SYTWRKLDPG SEETQTLVRE YFSWEGAYQH
     VGKAFNQGKI FK