EF1A1_DROME
ID EF1A1_DROME Reviewed; 463 AA.
AC P08736; C6TP87; Q0E9B9; Q9V631;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Elongation factor 1-alpha 1 {ECO:0000312|FlyBase:FBgn0284245};
DE Short=EF-1-alpha-1 {ECO:0000312|FlyBase:FBgn0284245};
DE AltName: Full=50 kDa female-specific protein;
GN Name=eEF1alpha1 {ECO:0000312|FlyBase:FBgn0284245};
GN Synonyms=Ef1alpha48D {ECO:0000312|FlyBase:FBgn0284245},
GN EF1B {ECO:0000312|FlyBase:FBgn0284245}, F1 {ECO:0000303|PubMed:16593598};
GN ORFNames=CG8280 {ECO:0000312|FlyBase:FBgn0284245};
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].
RX PubMed=16593598; DOI=10.1073/pnas.82.17.5795;
RA Walldorf U., Hovemann B., Bautz E.K.F.;
RT "F1 and F2: two similar genes regulated differently during development of
RT Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5795-5799(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S; TISSUE=Embryo, and Pupae;
RX PubMed=3131735; DOI=10.1093/nar/16.8.3175;
RA Hovemann B., Richter S., Walldorf U., Cziepluch C.;
RT "Two genes encode related cytoplasmic elongation factors 1 alpha (EF-1
RT alpha) in Drosophila melanogaster with continuous and stage specific
RT expression.";
RL Nucleic Acids Res. 16:3175-3194(1988).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 292-311, AND ETHANOLAMINYLATION AT GLU-301.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
RN [8]
RP IDENTIFICATION OF FUNCTION BY SIMILARITY.
RX PubMed=3135536; DOI=10.1093/nar/16.13.6191;
RA Henikoff S., Wallace J.C.;
RT "Detection of protein similarities using nucleotide sequence databases.";
RL Nucleic Acids Res. 16:6191-6204(1988).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; M11744; AAA28526.1; -; Genomic_DNA.
DR EMBL; X06869; CAA29993.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58608.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56119.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56120.1; -; Genomic_DNA.
DR EMBL; BT011039; AAR30199.1; -; mRNA.
DR EMBL; BT099573; ACU43535.1; -; mRNA.
DR PIR; S00676; S00676.
DR RefSeq; NP_001286321.1; NM_001299392.1.
DR RefSeq; NP_001286322.1; NM_001299393.1.
DR RefSeq; NP_477375.1; NM_058027.5.
DR RefSeq; NP_725085.1; NM_165850.3.
DR AlphaFoldDB; P08736; -.
DR SMR; P08736; -.
DR BioGRID; 62056; 62.
DR IntAct; P08736; 5.
DR MINT; P08736; -.
DR STRING; 7227.FBpp0304260; -.
DR PaxDb; P08736; -.
DR PRIDE; P08736; -.
DR DNASU; 36271; -.
DR EnsemblMetazoa; FBtr0088035; FBpp0087142; FBgn0284245.
DR EnsemblMetazoa; FBtr0331927; FBpp0304260; FBgn0284245.
DR EnsemblMetazoa; FBtr0345022; FBpp0311272; FBgn0284245.
DR EnsemblMetazoa; FBtr0345023; FBpp0311273; FBgn0284245.
DR GeneID; 36271; -.
DR KEGG; dme:Dmel_CG8280; -.
DR CTD; 36271; -.
DR FlyBase; FBgn0284245; eEF1alpha1.
DR VEuPathDB; VectorBase:FBgn0284245; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P08736; -.
DR OMA; YNEARFE; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P08736; -.
DR Reactome; R-DME-156842; Eukaryotic Translation Elongation.
DR Reactome; R-DME-3371511; HSF1 activation.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8876725; Protein methylation.
DR SignaLink; P08736; -.
DR ChiTaRS; Ef1alpha48D; fly.
DR GenomeRNAi; 36271; -.
DR PRO; PR:P08736; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0284245; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; P08736; baseline and differential.
DR Genevisible; P08736; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..463
FT /note="Elongation factor 1-alpha 1"
FT /id="PRO_0000090906"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000305|PubMed:8500545"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT CONFLICT 114..116
FT /note="LIV -> QID (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="G -> D (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="I -> V (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
FT CONFLICT 215..217
FT /note="KVE -> EVG (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="I -> V (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="K -> L (in Ref. 1; AAA28526 and 2; CAA29993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50307 MW; 33ECDCDB4DAE8BBA CRC64;
MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETAKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGT
GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSSEP PYSEARYEEI KKEVSSYIKK
IGYNPAAVAF VPISGWHGDN MLEPSTNMPW FKGWKVERKE GNADGKTLID ALDAILPPAR
PTDKALRLPL QDVYKIGGIG TVPVGRVETG VLKPGTVVVF APANITTEVK SVEMHHEALQ
EAVPGDNVGF NVKNVSVKEL RRGYVAGDSK ANPPKGAADF TAQVIVLNHP GQIANGYTPV
LDCHTAHIAC KFAEIKEKVD RRSGKTTEEN PKFIKSGDAA IVNLVPSKPL CVEAFQEFPP
LGRFAVRDMR QTVAVGVIKA VNFKDASGGK VTKAAEKATK GKK
