EF1A2_DROME
ID EF1A2_DROME Reviewed; 462 AA.
AC P05303; Q9V9U8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
GN Name=eEF1alpha2 {ECO:0000312|FlyBase:FBgn0000557};
GN Synonyms=EF1a {ECO:0000303|PubMed:3131735},
GN Ef1alpha100E {ECO:0000312|FlyBase:FBgn0000557},
GN F2 {ECO:0000312|FlyBase:FBgn0000557};
GN ORFNames=CG1873 {ECO:0000312|FlyBase:FBgn0000557};
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].
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 [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;
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 (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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; X06870; CAA29994.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57185.1; -; Genomic_DNA.
DR EMBL; BT015202; AAT94431.1; -; mRNA.
DR PIR; S01193; S01193.
DR RefSeq; NP_524611.1; NM_079872.4.
DR RefSeq; NP_733449.1; NM_170570.1.
DR RefSeq; NP_996315.1; NM_206592.1.
DR RefSeq; NP_996316.1; NM_206593.1.
DR AlphaFoldDB; P05303; -.
DR SMR; P05303; -.
DR BioGRID; 68577; 14.
DR IntAct; P05303; 2.
DR MINT; P05303; -.
DR STRING; 7227.FBpp0085193; -.
DR PaxDb; P05303; -.
DR PRIDE; P05303; -.
DR DNASU; 43736; -.
DR EnsemblMetazoa; FBtr0085832; FBpp0085193; FBgn0000557.
DR EnsemblMetazoa; FBtr0085833; FBpp0085194; FBgn0000557.
DR EnsemblMetazoa; FBtr0085834; FBpp0089103; FBgn0000557.
DR EnsemblMetazoa; FBtr0085835; FBpp0089104; FBgn0000557.
DR GeneID; 43736; -.
DR KEGG; dme:Dmel_CG1873; -.
DR CTD; 43736; -.
DR FlyBase; FBgn0000557; eEF1alpha2.
DR VEuPathDB; VectorBase:FBgn0000557; -.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P05303; -.
DR OMA; SEKMAWF; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P05303; -.
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; P05303; -.
DR BioGRID-ORCS; 43736; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43736; -.
DR PRO; PR:P05303; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000557; Expressed in head capsule and 17 other tissues.
DR ExpressionAtlas; P05303; baseline and differential.
DR Genevisible; P05303; DM.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; ISS:FlyBase.
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 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..462
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000090907"
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:0000250"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT CONFLICT 116
FT /note="V -> D (in Ref. 1; CAA29994)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="C -> Y (in Ref. 1; CAA29994)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="K -> G (in Ref. 1; CAA29994)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="TE -> DG (in Ref. 1; CAA29994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50663 MW; FA9C9F5734A76BA4 CRC64;
MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGT
GEFEAGISKN GQTREHALLA FTLGVKQLIV GVNKMDSTEP PYSEARYEEI KKEVSSYIKK
IGYNPASVAF VPISGWHGDN MLEPSEKMPW FKGWSVERKE GKAEGKCLID ALDAILPPQR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG LLKPGMVVNF APVNLVTEVK SVEMHHEALT
EAMPGDNVGF NVKNVSVKEL RRGYVAGDSK NNPPRGAADF TAQVIVLNHP GQIANGYTPV
LDCHTAHIAC KFSEIKEKCD RRTGKTTETE PKAIKSGDAA IIVLVPSKPL CVESFQEFPP
LGRFAVRDMR QTVAVGVIKS VNFKETTSGK VTKAAEKAQK KK
