EFGM_DROGR
ID EFGM_DROGR Reviewed; 747 AA.
AC B4JQM7;
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=GH13155;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916372; EDV99207.1; -; Genomic_DNA.
DR RefSeq; XP_001993282.1; XM_001993246.1.
DR AlphaFoldDB; B4JQM7; -.
DR SMR; B4JQM7; -.
DR STRING; 7222.FBpp0147061; -.
DR EnsemblMetazoa; FBtr0148569; FBpp0147061; FBgn0120632.
DR GeneID; 6567084; -.
DR KEGG; dgr:6567084; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B4JQM7; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B4JQM7; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001070; 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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 17..747
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385547"
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; 83917 MW; EBE182191A6A9B79 CRC64;
MSLIMRVLNG NLSLRLSAMK TVCQLQCGYS SHAKYAEHKS IERIRNIGIS AHIDSGKTTL
TERILFYTGR IAEMHEVRGK DNVGATMDSM ELERQRGITI QSAATYTMWK DTNINIIDTP
GHVDFTVEVE RALRVLDGAV LVLCAVGGVQ SQTLTVNRQM KRYNVPCLAF INKLDRLGSN
PNRVLSQLRS KMNHNAAFIQ LPIGVESHCK GLVDLVQERA VYFEGENGAD LRLDEIPQEM
RVESQERRQE LIEHLSNADE TFGELFLEEK PFTEADIKAA LRRTCIKRTF TPVLVGTALK
NKGVQPLLDA IIDYLPNPGE VENLAYIEHE GKEKQQIVLN PARDGKDPFM GLAFKLEAGR
FGQLTYLRCY QGVLRKGDNI FNARTNKKVR IARLVRLHSN QMEDVNEVFA GDIFALFGVD
CASGDTFTTN PKNNMAMESI FVPEPVVSMA IKPNNTKDRD NFSKAIARFT KEDPTFHFYF
DNDVKETLVS GMGELHLEIY AQRMEREYGC PVTLGKPKVA FRETLVGPCE FDFLHKKQSG
GSGQYARIIG LMEPLPPNQN TLLEFVDETV GTNVPKQFVP GVEKGYREMC ERGMLSGHKL
SGIRFRLQDG GHHIVDSSEL AFMLAAHGAI KEVFQNGSWQ ILEPIMLVEV TAPEEFQGAV
MGHLSKRHGI ITGTEGTEGW FTVYAEVPLN DMFGYASELR SSTQGKGEFT MEYSRYSPCL
PDVQDQIVRQ YQESQGMGQA EKKKKKN
