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Database: UniProt
Entry: EFGM_DROWI
LinkDB: EFGM_DROWI
Original site: EFGM_DROWI 
ID   EFGM_DROWI              Reviewed;         745 AA.
AC   B4MZW9;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 91.
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=GK24732;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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; CH963920; EDW77904.1; -; Genomic_DNA.
DR   RefSeq; XP_002066918.1; XM_002066882.1.
DR   AlphaFoldDB; B4MZW9; -.
DR   SMR; B4MZW9; -.
DR   STRING; 7260.B4MZW9; -.
DR   EnsemblMetazoa; FBtr0255383; FBpp0253875; FBgn0226692.
DR   GeneID; 6643963; -.
DR   KEGG; dwi:6643963; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 148165at2759; -.
DR   PhylomeDB; B4MZW9; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000007798; 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; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd04097; mtEFG1_C; 1.
DR   CDD; cd04091; mtEFG1_II_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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..745
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385553"
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;  83667 MW;  FE1E3ECDD5CAE1BB CRC64;
     MSLLTRLCKG NVPLRLNTLK HLSQCGYSSH AKFSEHKPIE KIRNIGISAH IDSGKTTLTE
     RILFYTGRIA EMHEVRGKDN VGATMDSMEL ERQRGITIQS AATYTLWKDT NINIIDTPGH
     VDFTVEVERA LRVLDGAVLV LCAVGGVQSQ TLTVNRQMKR YNVPCLAFIN KLDRLGSNPY
     RVLSQMRSKM NHNAAFIQLP IGVESNCKGI VDLVQEKAIY FEGDHGMDIR LDEIPQDMRA
     ESGERRQELI EHLSNADEKF GELFLEEKPF TEKDIKEALR RTCIQRTFTP VLVGTALKNK
     GVQPLLDAVL DYLPNPGEVE NLAFIEHEGK EPEKVVLNPA RDGKDPFMGL AFKLEAGRFG
     QLTYLRCYQG VLRKGDNIFN ARTNKKVRIA RLVRLHSNQM EDVNEVFAGD IFALFGVDCA
     SGDTFTTNPK NHLAMESIFV PEPVVSMAIK PNNTKDRDNF SKAIARFTKE DPTFHFHFDN
     DVKETLVSGM GELHLEIYAQ RMEREYGCPV TLGKPKVAFR ETLVGPCEFD YLHKKQSGGS
     GQYARIIGIM EPLPPSQNTL LEFVDETVGT NVPKQFIPGV EKGYREMAER GMLSGHKLSG
     IRFRLQDGGH HIVDSSELAF MLAAHGAIKE VFQNGSWQIL EPIMLVEVTA PEEFQGAVMG
     HLSKRHGIIT GTEGTEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFTME YSRYSPCLPE
     VQEQIVRQYQ ESQGVGQAEK KKKKN
//
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