EFGM_DROME
ID EFGM_DROME Reviewed; 745 AA.
AC Q9VM33; Q494L3;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=dEF-G1;
DE AltName: Full=Protein iconoclast;
GN Name=mEFG1 {ECO:0000312|FlyBase:FBgn0263133};
GN Synonyms=ico {ECO:0000303|PubMed:21364917};
GN ORFNames=CG4567 {ECO:0000312|FlyBase:FBgn0263133};
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], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=21364917; DOI=10.1371/journal.pone.0016799;
RA Trivigno C., Haerry T.E.;
RT "The Drosophila mitochondrial translation elongation factor G1 contains a
RT nuclear localization signal and inhibits growth and DPP signaling.";
RL PLoS ONE 6:E16799-E16799(2011).
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., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome (By
CC similarity). Essential during development as it acts as a retrograde
CC signal from mitochondria to the nucleus to slow down cell proliferation
CC if mitochondrial energy output is low. {ECO:0000255|HAMAP-
CC Rule:MF_03061, ECO:0000269|PubMed:21364917}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061,
CC ECO:0000269|PubMed:21364917}.
CC -!- DISRUPTION PHENOTYPE: Larvae are able to survive on maternal
CC contribution until the third larval stage but they fail to initiate the
CC rapid growth phase and die. {ECO:0000269|PubMed:21364917}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03061}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ41771.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014134; AAF52495.2; -; Genomic_DNA.
DR EMBL; BT023763; AAZ41771.1; ALT_FRAME; mRNA.
DR RefSeq; NP_609105.1; NM_135261.2.
DR AlphaFoldDB; Q9VM33; -.
DR SMR; Q9VM33; -.
DR STRING; 7227.FBpp0079041; -.
DR PaxDb; Q9VM33; -.
DR PRIDE; Q9VM33; -.
DR EnsemblMetazoa; FBtr0079413; FBpp0079041; FBgn0263133.
DR GeneID; 34004; -.
DR KEGG; dme:Dmel_CG4567; -.
DR UCSC; CG4567-RA; d. melanogaster.
DR CTD; 34004; -.
DR FlyBase; FBgn0263133; mEFG1.
DR VEuPathDB; VectorBase:FBgn0263133; -.
DR eggNOG; KOG0465; Eukaryota.
DR GeneTree; ENSGT00550000074911; -.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q9VM33; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q9VM33; -.
DR Reactome; R-DME-5389840; Mitochondrial translation elongation.
DR UniPathway; UPA00345; -.
DR BioGRID-ORCS; 34004; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34004; -.
DR PRO; PR:Q9VM33; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0263133; Expressed in ovary and 42 other tissues.
DR Genevisible; Q9VM33; DM.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_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; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
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; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..745
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007445"
FT DOMAIN 40..317
FT /note="tr-type G"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 116..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 170..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CONFLICT 150
FT /note="Q -> E (in Ref. 4; AAZ41771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 83509 MW; D27DF21DB4682A83 CRC64;
MSLITRLLTG NNTLRLRALK SLGKAGYSSH AKFSEHKPIE RIRNIGISAH IDSGKTTLTE
RILFYTGRIA EMHEVRGKDN VGATMDSMEL ERQRGITIQS AATYTLWKDT NINIIDTPGH
VDFTVEVERA LRVLDGAVLV LCAVGGVQSQ TLTVNRQMKR YNVPCLAFIN KLDRLGSNPY
RVLSQMRSKM NHNAAFIQLP IGVESNCKGI VDLVREKAIY FEGEHGMDIR LDEIPQDMRV
ESLERRQELI EHLSNADETL GELFLEEKPF TEDDIKAALR RTCINRTFTP VLVGTALKNK
GVQPLLDAVL DYLPNPGEVE NLGFIEKEGQ DPEKVVLNPA RDGKDPFVGL AFKLEAGRFG
QLTYLRCYQG VLRKGDNIFN ARTNKKVRIA RLVRLHSNQM EDVNEVYAGD IFALFGVDCA
SGDTFTTNPK NNLSMESIFV PEPVVSMAIK PNNTKDRDNF SKAIARFTKE DPTFHFFFDN
DVKETLVSGM GELHLEIYAQ RMEREYGCPV TLGKPKVAFR ETLVGPCEFD YLHKKQSGGS
GQYARIIGVM EPLPPNQNTL LEFVDETVGT NVPKQFVPGV EKGYREMAEK GMLSGHKLSG
IRFRLQDGGH HIVDSSELAF MLAAHGAIKE VFQNGSWQIL EPIMLVEVTA PEEFQGAVMG
HLSKRHGIIT GTEGTEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFTME YSRYSPCLPD
VQDQIVRQYQ ESQGLAQPDK KKKKN
