ID   EF1G_CARAU              Reviewed;         442 AA.
AC   Q90YC0;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
GN   Name=eef1g;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   PubMed=12180134; DOI=10.1080/10425170290019865;
RA   Tokumoto M., Nagahama Y., Tokumoto T.;
RT   "A major substrate for MPF: cDNA cloning and expression of a polypeptide
RT   chain elongation factor 1gamma from goldfish (Carassius auratus).";
RL   DNA Seq. 13:27-31(2002).
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; AB056105; BAB64568.1; -; mRNA.
DR   AlphaFoldDB; Q90YC0; -.
DR   SMR; Q90YC0; -.
DR   Proteomes; UP000515129; 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   2: Evidence at transcript level;
KW   Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208819"
FT   DOMAIN          2..87
FT                   /note="GST N-terminal"
FT   DOMAIN          88..216
FT                   /note="GST C-terminal"
FT   DOMAIN          281..442
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          224..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  50424 MW;  793FEAC133B0995A CRC64;
     MAAGTLYTYP ENWRAFKAQI AAQYSGARLK IASASPAFTF GQTNRSPAFL SNFPLGKVPA
     YQGDDGFCLF ESNAIAHFLS NDALRGSTPQ ASAQVLQWVS FADSEIIPPA SAWVFPTLGI
     MQFNKQATEQ AKEEVKRVLA VLNQHLNTRT FLVGERVSLA DITVVCSLLW LYKQVLEPAF
     RQPYPNVTRW FLTCVNQPQF KAVLGEVKLC EKMAQFDAKK FAEMQPKKEA PAKKEKAGKE
     GGKQQQPQQE KKEKKKEEKK AAPAEEEMDE CEAALASEPK AKDPYAHLPK SSFVMDEFKR
     KYSNEDTLTV ALPYFWDHFD REGFSIWYAE YRFPEELTMS FMSCNLITGM FQRLDKLRKN
     AFASVILFGA NNDSCISGIW VFRGQELAFT LSEDWQIDYE SYTWRKLDVD SEECKTMVKE
     YFAWEGEFKH VGKSFNQGKI FK