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EFGM_AEDAE
ID   EFGM_AEDAE              Reviewed;         748 AA.
AC   Q16S14;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 116.
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   ORFNames=AAEL010742;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(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       {ECO:0000255|HAMAP-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; CH477689; EAT37254.1; -; Genomic_DNA.
DR   RefSeq; XP_001661064.1; XM_001661014.1.
DR   AlphaFoldDB; Q16S14; -.
DR   SMR; Q16S14; -.
DR   STRING; 7159.AAEL010742-PA; -.
DR   GeneID; 5573819; -.
DR   KEGG; aag:5573819; -.
DR   VEuPathDB; VectorBase:AAEL010742; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   InParanoid; Q16S14; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   PhylomeDB; Q16S14; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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..14
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           15..748
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385542"
FT   DOMAIN          40..318
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   748 AA;  83633 MW;  761C777A92C888BC CRC64;
     MTISSFLRVR HSLAAAKCVL ENAKQSFSSH AAFAEHAKLE RIRNIGISAH IDSGKTTLTE
     RILFYTGRIK QMHEVKGKDN VGATMDSMEL ERQRGITIQS AATYTMWKDH NINIIDTPGH
     VDFTVEVERA LRVLDGAILV LCSVGGVQSQ TLTVNRQMKR YNVPCLAFIN KLDRTGANPY
     RVLGQMRSKL NHNAAFIQLP IGVESNCKGI VDLVKQRALY FEDHLGLTVR EDEIPQEMRA
     ESDERRHELI EHLSNVDESI GELFLEEKTP TEQDIMAAIR RSALKRTFTP VLVGTALKNK
     GVQPLLDAVL NYLPHPGEVE NIALIEKKGK EPQQIMLDPA RDGKSPFVGL AFKLEAGRFG
     QLTYLRCYQG VLRKGDSIFN VRSGKKVRLA RLVRLHSNNM EDVNEVYAGD IFALFGVDCA
     SGDTFVTNPD LELSMESIFV PDPVVSMAIK PANNKDRDNF SKAVARFTKE DPTFRFAYDT
     DIKETLVSGM GELHLEIYAQ RMEREYNCPV ILGKPKVAFR ETLVAPCEFD FLHKKQSGGQ
     GQYARVTGVL EPLPPHQNTT IEFTDETVGT NVPKQFVPGI EKGFRQMAEK GLLSGHKLSG
     IKFRLQDGAH HIVDSSELAF MLAAQGAIKS VFENGSWQIL EPIMMVEVTA PEEFQGTVIG
     QLNKRHGIIT GTEGSEGWFT VYAEVPLNDM FGYAGELRSS TQGKGEFSME YSRYSPCKPD
     VQEKLMQDYQ IAQGNVVVDA KKQQKKKN
 
 
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