EFGM_DROAN
ID EFGM_DROAN Reviewed; 745 AA.
AC B3MK91;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-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 AltName: Full=Protein iconoclast;
DE Flags: Precursor;
GN Name=ico; ORFNames=GF14034;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
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; CH902620; EDV32475.1; -; Genomic_DNA.
DR RefSeq; XP_001963254.1; XM_001963218.2.
DR AlphaFoldDB; B3MK91; -.
DR SMR; B3MK91; -.
DR STRING; 7217.FBpp0117226; -.
DR EnsemblMetazoa; FBtr0118734; FBpp0117226; FBgn0091061.
DR GeneID; 6496862; -.
DR KEGG; dan:6496862; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; B3MK91; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B3MK91; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000007801; 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..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 16..745
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385545"
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"
SQ SEQUENCE 745 AA; 83698 MW; 8EBE99297D0C3E29 CRC64;
MSLITRLLTA SSPLRLRAME TMSRAGYSSH AKYAEHRPID KIRNIGISAH IDSGKTTLTE
RILFYTGRIV EMHEVRGKDN VGATMDSMEL ERQRGITIQS AATYTLWKDT NINIIDTPGH
VDFTVEVERA LRVLDGAVLV LCAVGGVQSQ TLTVNRQMKR YNVPCLAFIN KLDRMGSNPY
RVLSQMRSKM NHNAAFIQLP IGVESNCKGI VDLVRERAIY FEGEHGMNLR LDEIPQDMRV
ESQERRQELI EHLSNADDTF GELFLEEKPF TEDDIKAALR RTCIKRTFTP VLVGTALKNK
GVQPLLDAVL EYLPNPGEVE NLAFVEKEGQ DPEKIVLNPA RDGKDAFVGL AFKLEAGRFG
QLTYLRCYQG VLRKGDNIFN ARTNKKVRIA RLVRLHSNQM EDVNEVYAGD IFALFGVDCA
SGDTFTTNPK NNLAMESIFV PEPVVSMAIK PNNTKDRDNF SKAIARFTKE DPTFHFFFDN
DVKETLVSGM GELHLEIYAQ RMEREYGCPV TLGKPKVAFR ETLVGPCEFD YLHKKQSGGS
GQYARIIGIM EPLPPNQNTL LEFVDETVGT NVPKQFVPGV EKGYREMAEK GMLSGHKLSG
IRFRLQDGGH HIVDSSELAF MLAAHGAIKE VFQNGNWQIL EPIMLVEVTA PEEFQGAVMG
HLSKRHGIIT GTEGTEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFTME YSRYSPCLPD
VQDQIVRQYQ ESQGLGQADK KKRKN
