EFGM_DROYA
ID EFGM_DROYA Reviewed; 745 AA.
AC B4NZM7;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=GE18370;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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 -!- 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; CM000157; EDW87776.1; -; Genomic_DNA.
DR RefSeq; XP_002088064.1; XM_002088028.2.
DR AlphaFoldDB; B4NZM7; -.
DR SMR; B4NZM7; -.
DR STRING; 7245.FBpp0263380; -.
DR EnsemblMetazoa; FBtr0264888; FBpp0263380; FBgn0235790.
DR GeneID; 6526968; -.
DR KEGG; dya:Dyak_GE18370; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; B4NZM7; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002282; Chromosome 2L.
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.
FT CHAIN 1..745
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385554"
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; 83573 MW; 625F55D89609AE0F CRC64;
MSLITRLLTG NITLRRRAME 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 EPLPPTQNTL LEFVDETVGT NVPKQFVPGV EKGYREMAEK GMLSGHKLSG
IRFRLQDGGH HIVDSSELAF MLASHGAIKE VFQNGSWQIL EPIMLVEVTA PEEFQGAVMG
HLSKRHGIIT GTEGTEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFTME YSRYSPCLPD
VQDQIVRQYQ ESQGLAQPDK KKKKN
