ID   EF1G_SCHPO              Reviewed;         409 AA.
AC   P40921; O14005;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 153.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
GN   Name=tef3; ORFNames=SPAC29A4.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 226-244.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=8244022; DOI=10.1016/0378-1119(93)90184-5;
RA   Momoi H., Yamada H., Ueguchi C., Mizuno T.;
RT   "Sequence of a fission yeast gene encoding a protein with extensive
RT   homology to eukaryotic elongation factor-1 gamma.";
RL   Gene 134:119-122(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(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; D14606; BAA03456.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB10129.1; -; Genomic_DNA.
DR   PIR; JT0764; JT0764.
DR   PIR; T38487; T38487.
DR   RefSeq; NP_594880.1; NM_001020309.3.
DR   AlphaFoldDB; P40921; -.
DR   SMR; P40921; -.
DR   FunCoup; P40921; 749.
DR   STRING; 284812.P40921; -.
DR   iPTMnet; P40921; -.
DR   PaxDb; 284812-P40921; -.
DR   KEGG; spo:2542298; -.
DR   PomBase; SPAC29A4.02c; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; KOG1627; Eukaryota.
DR   HOGENOM; CLU_011226_3_0_1; -.
DR   InParanoid; P40921; -.
DR   OMA; AACNWVF; -.
DR   PhylomeDB; P40921; -.
DR   PRO; PR:P40921; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; ISO:PomBase.
DR   GO; GO:0002182; P:cytoplasmic translational elongation; IDA:PomBase.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR   CDD; cd03044; GST_N_EF1Bgamma; 1.
DR   FunFam; 1.20.1050.10:FF:000006; Elongation factor 1 gamma; 1.
DR   FunFam; 3.40.30.10:FF:000142; Elongation factor 1 gamma; 1.
DR   FunFam; 3.30.70.1010:FF:000001; Elongation factor 1-gamma 1; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 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   PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR   PANTHER; PTHR43986:SF11; ELONGATION FACTOR 1-GAMMA; 1.
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   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SMART; SM01183; EF1G; 1.
DR   SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..409
FT                   /note="Elongation factor 1-gamma"
FT                   /id="PRO_0000208830"
FT   DOMAIN          2..81
FT                   /note="GST N-terminal"
FT   DOMAIN          86..212
FT                   /note="GST C-terminal"
FT   DOMAIN          251..409
FT                   /note="EF-1-gamma C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT   REGION          219..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        246
FT                   /note="R -> A (in Ref. 2; CAB10129)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  45786 MW;  A49CB947A9F66DF0 CRC64;
     MSVGTVYGKI GSPRVLFCVS VAAVAGVEVE HVDVQPHNFP ADLAAKFPLQ KMPVFVGKDG
     FPLSETLAIA FYLASLNKTR ALNGTTAEEK AKVLQYCSFT NSELPGAFRP IIAPRVFGAP
     YDEQAAKEAE TAIALIFARF DEELASKTYL VGSRLTLADI FFTCFLKFGA TYVLTKSYLA
     KYTHIYRYYQ TIYHQAKLDA ITEPLKFIDQ PLPIIKAENK EAAPAKKAEK KKDEKKKNAP
     KPQAERPAKP PKHPLASAPN GSFDIEEYKR VYSNQDTRSG ALPWFFEHFD PENYSVWKVD
     YSYPEDLKQP VFMTNNLIGG FFQRLEASRK YIFGCCVVIG ENGDNTITGA FVIKGHDYVP
     AFDVAPDWGS YTFTKLDINK PEDKAFIEDA WAWDKPIEGR EVADGKVCK
//