EFGM_DROPS
ID EFGM_DROPS Reviewed; 744 AA.
AC Q29N77;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 109.
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};
GN Name=mEFG1 {ECO:0000250|UniProtKB:Q9VM33};
GN Synonyms=ico {ECO:0000250|UniProtKB:Q9VM33}; ORFNames=GA18263;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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 -!- 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}.
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DR EMBL; CH379060; EAL33465.1; -; Genomic_DNA.
DR RefSeq; XP_001356402.1; XM_001356366.3.
DR AlphaFoldDB; Q29N77; -.
DR SMR; Q29N77; -.
DR STRING; 7237.FBpp0280351; -.
DR EnsemblMetazoa; FBtr0281913; FBpp0280351; FBgn0078269.
DR GeneID; 4817299; -.
DR KEGG; dpo:Dpse_GA18263; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q29N77; -.
DR OMA; AATTCHW; -.
DR PhylomeDB; Q29N77; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0078269; Expressed in female reproductive system and 2 other tissues.
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.
FT CHAIN 1..744
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385549"
FT DOMAIN 39..316
FT /note="tr-type G"
FT REGION 725..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 115..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 169..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 744 AA; 83536 MW; 14DDA25CFFF13BE4 CRC64;
MSLITRVLQG NLTRKNALQT LTRCGYSSHA KFAEHRPIEK IRNIGISAHI DSGKTTLTER
ILFYTGRIAE MHEVRGKDNV GATMDSMELE RQRGITIQSA ATYTMWKDTN VNIIDTPGHV
DFTVEVERAL RVLDGAVLVL CAVGGVQSQT LTVNRQMKRY NVPCLAFINK LDRLGSNPYR
VLSQMRSKMN HNAAFIQLPI GVESNCKGLV DLVREQAIYF EGENGMDVRL DEIPQDMRVE
SQERRQELIE HLSNADETFG EFFLEEKPFS EADLRAALRR TCINRTFTPV LVGTALKNKG
VQPLLDAVID YLPNPGEVEN LGFIEREGKD PEKIVLNPAR DGKDPFVGLA FKLEAGRFGQ
LTYLRCYQGV LRKGDNIFNA RTNKKVRIAR LVRLHSSQME DVNEVYAGDI FALFGVDCAS
GDTFTTNPKN NLAMESIFVP EPVVSMAIKP NNTKDRDNFS KAIARFTKED PTFHFFFDND
VKETLVSGMG ELHLEIYAQR MEREYGCPVT LGKPKVAFRE TLVGPCEFDY LHKKQSGGSG
QYARIIGVME PLPPNQNTLL EFVDETVGTN VPKQFVPGVE KGYREMAERG MLSGHRLSGI
KFRLQDGGHH IVDSSELAFM LAAHGAIKEV FQNGSWQILE PIMMVEVTAP EEFQGAVMGH
LSKRHGIITG TEGTEGWFTV YAEVPLNDMF GYAGELRSST QGKGEFTMEY SRYSPCLPDV
QDQIVRQYQE TQGASQPDKK KKKN
