EFGM_DROMO
ID EFGM_DROMO Reviewed; 747 AA.
AC B4KKD5;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 Flags: Precursor;
GN Name=mEFG1 {ECO:0000250|UniProtKB:Q9VM33};
GN Synonyms=ico {ECO:0000250|UniProtKB:Q9VM33}; ORFNames=GI17797;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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.
CC Essential during development as it acts as a retrograde signal from
CC mitochondria to the nucleus to slow down cell proliferation if
CC mitochondrial energy output is low (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03061}.
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 -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; CH933807; EDW12666.1; -; Genomic_DNA.
DR RefSeq; XP_002003224.1; XM_002003188.2.
DR AlphaFoldDB; B4KKD5; -.
DR SMR; B4KKD5; -.
DR STRING; 7230.FBpp0167014; -.
DR EnsemblMetazoa; FBtr0168522; FBpp0167014; FBgn0140538.
DR GeneID; 6577257; -.
DR KEGG; dmo:Dmoj_GI17797; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B4KKD5; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B4KKD5; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 33..747
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385548"
FT DOMAIN 42..319
FT /note="tr-type G"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 747 AA; 83944 MW; BA6EB66DEB185C04 CRC64;
MTLITRVLNG NLPLRLSTLK AARQLQCGYS SHAKYAEHKP IERIRNIGIS AHIDSGKTTL
TERILFYTGR IAEMHEVRGK DNVGATMDSM ELERQRGITI QSAATYTVWK DVNINIIDTP
GHVDFTVEVE RALRVLDGAV LVLCAVGGVQ SQTLTVNRQM KRYNVPCLAF INKLDRMGSN
PYRVLSQMRS KLNHNAAFIQ LPIGVENNCK GIVDLVQERA IYFEGEHGIN LRLDEIPQDM
RVESQERRQE LIEHLSNADE TLGELFLEEK PFTEADIKAA LRRTCIKRTF TPVLVGTALK
NKGVQPLLDA VVDYLPNPGE VENLAYIEQE GQEKQQIVLN PARDGKDPFM GLAFKLEAGR
FGQLTYLRCY QGALRKGDNI YNARNHKKVR IARLVRLHSN QMEDVNEVFA GDIFALFGVD
CASGDTFTTN PKNNMSMESI FVPEPVVSMA IKPNNTKDRD NFSKAIARFT KEDPTFHFKF
DNDIKETLVS GMGELHLEIY AQRMEREYGC PVTLGKPKVA FRETLVGPCE FDYLHKKQSG
GSGQYARIIG VMEPLPPSQN TLLEFVDETV GTNVPKQFVP GVEKGYREMC ERGMLSGHKL
SGIRFRLQDG GHHIVDSSEL AFMLAAHGAV KEVFQNGAWQ ILEPIMLVEV TAPEEFQGAV
MGHLSKRHGI ITGTEGTEGW FTVYAEVPLN DMFGYASELR SSTQGKGEFT MEYSRYSPCL
PDVQEQIVRQ YQESQGLGQP EKKKKKN
