EF1G_DROME
ID EF1G_DROME Reviewed; 431 AA.
AC Q9NJH0; A4V3K9; Q6NL63; Q8IGT6; Q9NJH1; Q9VAM7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=eEF1gamma {ECO:0000312|FlyBase:FBgn0029176};
GN Synonyms=Ef1g {ECO:0000303|Ref.1};
GN ORFNames=CG11901 {ECO:0000312|FlyBase:FBgn0029176};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Canton-S;
RA Chaney L.C., Hitte C., Kinzy T., Horn M., Rabinow L.;
RT "Characterization of the Drosophila translational elongation factor 1 gamma
RT (EF1g).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAN71367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAS93749.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF148813; AAF26670.1; -; mRNA.
DR EMBL; AF148814; AAF26671.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56877.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN14165.1; -; Genomic_DNA.
DR EMBL; BT001612; AAN71367.1; ALT_INIT; mRNA.
DR EMBL; BT012478; AAS93749.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001189308.1; NM_001202379.2.
DR RefSeq; NP_652000.1; NM_143743.3.
DR RefSeq; NP_733280.1; NM_170401.3.
DR AlphaFoldDB; Q9NJH0; -.
DR SMR; Q9NJH0; -.
DR BioGRID; 69280; 34.
DR DIP; DIP-18800N; -.
DR IntAct; Q9NJH0; 3.
DR MINT; Q9NJH0; -.
DR STRING; 7227.FBpp0084761; -.
DR iPTMnet; Q9NJH0; -.
DR PaxDb; Q9NJH0; -.
DR PRIDE; Q9NJH0; -.
DR DNASU; 44791; -.
DR EnsemblMetazoa; FBtr0085392; FBpp0084761; FBgn0029176.
DR EnsemblMetazoa; FBtr0085393; FBpp0084762; FBgn0029176.
DR EnsemblMetazoa; FBtr0302442; FBpp0291632; FBgn0029176.
DR GeneID; 44791; -.
DR KEGG; dme:Dmel_CG11901; -.
DR UCSC; CG11901-RA; d. melanogaster.
DR CTD; 44791; -.
DR FlyBase; FBgn0029176; eEF1gamma.
DR VEuPathDB; VectorBase:FBgn0029176; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00390000007552; -.
DR HOGENOM; CLU_011226_3_1_1; -.
DR InParanoid; Q9NJH0; -.
DR OMA; TRWYETI; -.
DR OrthoDB; 1341490at2759; -.
DR PhylomeDB; Q9NJH0; -.
DR Reactome; R-DME-156842; Eukaryotic Translation Elongation.
DR SignaLink; Q9NJH0; -.
DR BioGRID-ORCS; 44791; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Ef1gamma; fly.
DR GenomeRNAi; 44791; -.
DR PRO; PR:Q9NJH0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0029176; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q9NJH0; baseline and differential.
DR Genevisible; Q9NJH0; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:FlyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; ISS:FlyBase.
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..431
FT /note="Elongation factor 1-gamma"
FT /id="PRO_0000208824"
FT DOMAIN 2..84
FT /note="GST N-terminal"
FT DOMAIN 86..212
FT /note="GST C-terminal"
FT DOMAIN 272..431
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 223..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 112
FT /note="V -> D (in Ref. 1; AAF26671)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="A -> T (in Ref. 5; AAS93749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48968 MW; 9303BACAA3E160D1 CRC64;
MVKGTLYTYP ENFRAYKALI AAQYSGAQVK VADNFKFGET NKSAEFLKKF PGGKVPAFET
AEGQYLSESN AIAYLLANEQ LRGGKCPFVQ AQVQQWISFA DNEIVPASCA WVFPLLGILP
QQKNSTAKQE AEAVLQQLNQ KLQDATFLAG ERITLADIVV FSSLLHLYEY VLEPSVRSAF
GNVNRWFVTI LNQKQVQAVV KDYKLCEKAL VFDPKKYAEF QAKTGAAKPQ QQAQQQKQEK
KPKEKKEAPK KAAEPAEELD AADEALAAEP KSKDPFDALP KGTFNFDDFK RVYSNEDEAK
SIPYFFDKFD AENYSIWFGE YKYNEELSKV FMSCNLITGM FQRLDKMRKA AFASVCLFGE
DGNSTISGIW VWRGQDLAFT LSPDWQIDYE VYDWKKLDAK SEETKKLVTQ YFSWSGTDKD
GRKFNQGKIF K