ID   EF1GA_XENLA             Reviewed;         436 AA.
AC   P26642; Q91374;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Elongation factor 1-gamma-A;
DE            Short=EF-1-gamma-A;
DE   AltName: Full=eEF-1B gamma-A;
DE   AltName: Full=p47;
GN   Name=eef1g-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=1754404; DOI=10.1093/nar/19.23.6644;
RA   Cormier P., Osborne H.B., Morales J., Bassez T., Poulhe R., Mazabraud A.,
RA   Mulner-Lorillon O., Belle R.;
RT   "Molecular cloning of Xenopus elongation factor 1 gamma, major M-phase
RT   promoting factor substrate.";
RL   Nucleic Acids Res. 19:6644-6644(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=8111972; DOI=10.1002/dvg.1020140605;
RA   Morales J., Bassez T., Cormier P., Mulner-Lorillon O., Belle R.,
RA   Osborne H.B.;
RT   "Expression of elongation factor 1 alpha (EF-1 alpha) and 1 beta gamma (EF-
RT   1 beta gamma) are uncoupled in early Xenopus embryos.";
RL   Dev. Genet. 14:440-448(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 38-48; 72-79; 268-274; 388-394 AND 415-419.
RX   PubMed=2676593; DOI=10.1016/0014-5793(89)81069-5;
RA   Belle R., Derancourt J., Poulhe R., Capony J.-P., Ozon R.,
RA   Mulner-Lorillon O.;
RT   "A purified complex from Xenopus oocytes contains a p47 protein, an in vivo
RT   substrate of MPF, and a p30 protein respectively homologous to elongation
RT   factors EF-1 gamma and EF-1 beta.";
RL   FEBS Lett. 255:101-104(1989).
RN   [4]
RP   PHOSPHORYLATION.
RX   PubMed=2546822; DOI=10.1016/0014-5793(89)81458-9;
RA   Mulner-Lorillon O., Poulhe R., Cormier P., Labbe J.C., Doree M., Belle R.;
RT   "Purification of a p47 phosphoprotein from Xenopus laevis oocytes and
RT   identification as an in vivo and in vitro p34cdc2 substrate.";
RL   FEBS Lett. 251:219-224(1989).
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.
CC   -!- PTM: Phosphorylated by CDK1. {ECO:0000269|PubMed:2546822}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000305}.
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DR   EMBL; X62508; CAA44367.1; -; mRNA.
DR   EMBL; S69724; AAB29957.1; -; mRNA.
DR   PIR; I51237; I51237.
DR   PIR; S20060; S20060.
DR   AlphaFoldDB; P26642; -.
DR   SMR; P26642; -.
DR   IntAct; P26642; 2.
DR   Proteomes; UP000186698; Genome assembly.
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; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..436
FT                   /note="Elongation factor 1-gamma-A"
FT                   /id="PRO_0000208820"
FT   DOMAIN          2..87
FT                   /note="GST N-terminal"
FT   DOMAIN          88..221
FT                   /note="GST C-terminal"
FT   DOMAIN          275..436
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          221..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        77
FT                   /note="H -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="G -> E (in Ref. 2; AAB29957)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="Missing (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   436 AA;  49791 MW;  8785C1E80578B131 CRC64;
     MAGGTLYTYP DNWRAYKPLI AAQYSGFPIK VASSAPEFQF GVTNKTPEFL KKFPLGKVPA
     FEGKDGFCLF ESSAIAHYVG NDELRGTTRL HQAQVIQWVS FSDSHIVPPA SAWVFPTLGI
     MQYNKQATEQ AKEGIKTVLG VLDSHLQTRT FLVGERITLA DITVTCSLLW LYKQVLEPSF
     RQPFGNVTRW FVTCVNQPEF RAVLGEVKLC DKMAQFDAKK FAEMQPKKET PKKEKPAKEP
     KKEKEEKKKA APTPAPAPED DLDESEKALA AEPKSKDPYA HLPKSSFIMD EFKRKYSNED
     TLTVALPYFW EHFDKEGWSI WYAEYKFPEE LTQAFMSCNL ITGMFQRLDK LRKTGFASVI
     LFGTNNNSSI SGVWVFRGQD LAFTLSEDWQ IDYESYNWRK LDSGSEECKT LVKEYFAWEG
     EFKNVGKPFN QGKIFK