EF2_DROME
ID EF2_DROME Reviewed; 844 AA.
AC P13060; A0A023GPJ5; Q9I7H2; Q9V9R0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Eukaryotic translation elongation factor 2 {ECO:0000312|FlyBase:FBgn0000559};
DE AltName: Full=Elongation factor 2 {ECO:0000303|PubMed:2508059};
DE Short=EF-2 {ECO:0000305};
GN Name=eEF2 {ECO:0000303|PubMed:23636399, ECO:0000312|FlyBase:FBgn0000559};
GN Synonyms=EF2 {ECO:0000303|PubMed:2508059},
GN Ef2b {ECO:0000312|FlyBase:FBgn0000559};
GN ORFNames=CG2238 {ECO:0000312|FlyBase:FBgn0000559};
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=2508059; DOI=10.1093/nar/17.18.7303;
RA Grinblat Y., Brown N.H., Kafatos F.C.;
RT "Isolation and characterization of the Drosophila translational elongation
RT factor 2 gene.";
RL Nucleic Acids Res. 17:7303-7314(1989).
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, AND ALTERNATIVE SPLICING.
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 STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) IN COMPLEX WITH THE 80S
RP RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expression commences during embryonic germ band
CC elongation and persists throughout development and in the adult.
CC Highest level of expression observed in late embryonic, late larval and
CC early pupal stages. {ECO:0000269|PubMed:2508059}.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates eEF2.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X15805; CAA33804.1; -; mRNA.
DR EMBL; AE014134; AAF57226.2; -; Genomic_DNA.
DR EMBL; AE014134; AAG22125.3; -; Genomic_DNA.
DR EMBL; AE014134; AAN11135.2; -; Genomic_DNA.
DR EMBL; AY075481; AAL68292.1; -; mRNA.
DR PIR; S05988; S05988.
DR RefSeq; NP_525105.2; NM_080366.3.
DR RefSeq; NP_724357.2; NM_165394.3.
DR RefSeq; NP_724358.2; NM_165395.2.
DR PDB; 4V6W; EM; 6.00 A; Az=1-844.
DR PDBsum; 4V6W; -.
DR AlphaFoldDB; P13060; -.
DR SMR; P13060; -.
DR BioGRID; 61367; 158.
DR DIP; DIP-19881N; -.
DR IntAct; P13060; 6.
DR MINT; P13060; -.
DR STRING; 7227.FBpp0305182; -.
DR PaxDb; P13060; -.
DR PRIDE; P13060; -.
DR DNASU; 35422; -.
DR EnsemblMetazoa; FBtr0085911; FBpp0085265; FBgn0000559.
DR EnsemblMetazoa; FBtr0085912; FBpp0085266; FBgn0000559.
DR EnsemblMetazoa; FBtr0332966; FBpp0305182; FBgn0000559.
DR GeneID; 35422; -.
DR KEGG; dme:Dmel_CG2238; -.
DR CTD; 1938; -.
DR FlyBase; FBgn0000559; eEF2.
DR VEuPathDB; VectorBase:FBgn0000559; -.
DR eggNOG; KOG0469; Eukaryota.
DR GeneTree; ENSGT00940000154662; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; P13060; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; P13060; -.
DR Reactome; R-DME-156902; Peptide chain elongation.
DR Reactome; R-DME-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8876725; Protein methylation.
DR SignaLink; P13060; -.
DR BioGRID-ORCS; 35422; 1 hit in 1 CRISPR screen.
DR ChiTaRS; EF2; fly.
DR GenomeRNAi; 35422; -.
DR PRO; PR:P13060; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000559; Expressed in oviduct (Drosophila) and 24 other tissues.
DR Genevisible; P13060; DM.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:FlyBase.
DR GO; GO:0006414; P:translational elongation; ISS:FlyBase.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..844
FT /note="Eukaryotic translation elongation factor 2"
FT /id="PRO_0000091012"
FT DOMAIN 17..348
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 108..112
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 162..165
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 701
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT CONFLICT 607
FT /note="D -> E (in Ref. 1; CAA33804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 844 AA; 94459 MW; 547A6ED0658B6B6F CRC64;
MVNFTVDEIR GLMDKKRNIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGAK AGETRFTDTR
KDEQERCITI KSTAISMYFE VEEKDLVFIT HPDQREKECK GFLINLIDSP GHVDFSSEVT
AALRVTDGAL VVVDCVSGVC VQTETVLRQA IAERIKPILF MNKMDRALLE LQLDAEELYQ
TFQRIVENVN VIIATYNDDG GPMGEVRVDP SKGSVGFGSG LHGWAFTLKQ FSEMYSEKFK
IDVVKLMNRL WGENFFNAKT KKWQKQKEAD NKRSFCMYIL DPIYKVFDAI MNYKKEEIGT
LLEKIGVTLK HEDKDKDGKA LLKTVMRTWL PAGEALLQMI AIHLPSPVVA QKYRMEMLYE
GPHDDEAAIA VKSCDPDGPL MMYISKMVPT SDKGRFYAFG RVFAGKVATG QKCRIMGPNY
TPGKKEDLYE KAIQRTILMM GRYVEAIEDV PSGNICGLVG VDQFLVKTGT ITTFKDAHNM
KVMKFSVSPV VRVAVEPKNP ADLPKLVEGL KRLAKSDPMV QCIIEESGEH IIAGAGELHL
EICLKDLEED HACIPLKKSD PVVSYRETVS EESDQMCLSK SPNKHNRLLM KALPMPDGLP
EDIDNGDVSA KDEFKARARY LSEKYDYDVT EARKIWCFGP DGTGPNFILD CTKSVQYLNE
IKDSVVAGFQ WASKEGILAD ENLRGVRFNI YDVTLHADAI HRGGGQIIPT TRRCLYAAAI
TAKPRLMEPV YLCEIQCPEV AVGGIYGVLN RRRGHVFEEN QVVGTPMFVV KAYLPVNESF
GFTADLRSNT GGQAFPQCVF DHWQVLPGDP SEPSSKPYAI VQDTRKRKGL KEGLPDLSQY
LDKL
