EFGM_HUMAN
ID EFGM_HUMAN Reviewed; 751 AA.
AC Q96RP9; A6NCI9; B2RCB9; B3KRW1; Q6GTN2; Q96T39;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
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 Short=hEFG1;
DE Flags: Precursor;
GN Name=GFM1 {ECO:0000255|HAMAP-Rule:MF_03061};
GN Synonyms=EFG, EFG1 {ECO:0000255|HAMAP-Rule:MF_03061}, GFM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11374907; DOI=10.1006/geno.2001.6536;
RA Gao J., Yu L., Zhang P., Jiang J., Chen J., Peng J., Wei Y., Zhao S.;
RT "Cloning and characterization of human and mouse mitochondrial elongation
RT factor G, GFM and gfm, and mapping of GFM to human chromosome 3q25.1-
RT q26.2.";
RL Genomics 74:109-114(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11735030; DOI=10.1007/s00439-001-0610-5;
RA Hammarsund M., Wilson W., Corcoran M., Merup M., Einhorn S., Grander D.,
RA Sangfelt O.;
RT "Identification and characterization of two novel human mitochondrial
RT elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved
RT through evolution.";
RL Hum. Genet. 109:542-550(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 116-751 (ISOFORM 2), AND VARIANT ILE-215.
RC TISSUE=Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Duodenum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP POTENTIAL TRANSIT PEPTIDE.
RX PubMed=15358359; DOI=10.1016/j.pep.2004.06.030;
RA Bhargava K., Templeton P., Spremulli L.L.;
RT "Expression and characterization of isoform 1 of human mitochondrial
RT elongation factor G.";
RL Protein Expr. Purif. 37:368-376(2004).
RN [8]
RP FUNCTION, AND PATHWAY.
RX PubMed=19716793; DOI=10.1016/j.molcel.2009.06.028;
RA Tsuboi M., Morita H., Nozaki Y., Akama K., Ueda T., Ito K., Nierhaus K.H.,
RA Takeuchi N.;
RT "EF-G2mt is an exclusive recycling factor in mammalian mitochondrial
RT protein synthesis.";
RL Mol. Cell 35:502-510(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANT COXPD1 SER-174.
RX PubMed=15537906; DOI=10.1056/nejmoa041878;
RA Coenen M.J.H., Antonicka H., Ugalde C., Sasarman F., Rossi R.,
RA Angelien Heister J.G.A.M., Newbold R.F., Trijbels F.J.M.F.,
RA van den Heuvel L.P., Shoubridge E.A., Smeitink J.A.M.;
RT "Mutant mitochondrial elongation factor G1 and combined oxidative
RT phosphorylation deficiency.";
RL N. Engl. J. Med. 351:2080-2086(2004).
RN [15]
RP VARIANT COXPD1 ARG-496.
RX PubMed=17160893; DOI=10.1086/510559;
RA Valente L., Tiranti V., Marsano R.M., Malfatti E., Fernandez-Vizarra E.,
RA Donnini C., Mereghetti P., De Gioia L., Burlina A., Castellan C.,
RA Comi G.P., Savasta S., Ferrero I., Zeviani M.;
RT "Infantile encephalopathy and defective mitochondrial DNA translation in
RT patients with mutations of mitochondrial elongation factors EFG1 and
RT EFTu.";
RL Am. J. Hum. Genet. 80:44-58(2007).
RN [16]
RP VARIANT COXPD1 TRP-250.
RX PubMed=21119709; DOI=10.1038/ejhg.2010.208;
RA Smits P., Antonicka H., van Hasselt P.M., Weraarpachai W., Haller W.,
RA Schreurs M., Venselaar H., Rodenburg R.J., Smeitink J.A.,
RA van den Heuvel L.P.;
RT "Mutation in subdomain G' of mitochondrial elongation factor G1 is
RT associated with combined OXPHOS deficiency in fibroblasts but not in
RT muscle.";
RL Eur. J. Hum. Genet. 19:275-279(2011).
RN [17]
RP VARIANTS COXPD1 TYR-57 AND TRP-250.
RX PubMed=26741492; DOI=10.1371/journal.pgen.1005679;
RA Kohda M., Tokuzawa Y., Kishita Y., Nyuzuki H., Moriyama Y., Mizuno Y.,
RA Hirata T., Yatsuka Y., Yamashita-Sugahara Y., Nakachi Y., Kato H.,
RA Okuda A., Tamaru S., Borna N.N., Banshoya K., Aigaki T., Sato-Miyata Y.,
RA Ohnuma K., Suzuki T., Nagao A., Maehata H., Matsuda F., Higasa K.,
RA Nagasaki M., Yasuda J., Yamamoto M., Fushimi T., Shimura M.,
RA Kaiho-Ichimoto K., Harashima H., Yamazaki T., Mori M., Murayama K.,
RA Ohtake A., Okazaki Y.;
RT "A comprehensive genomic analysis reveals the genetic landscape of
RT mitochondrial respiratory chain complex deficiencies.";
RL PLoS Genet. 12:E1005679-E1005679(2016).
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. Does
CC not mediate the disassembly of ribosomes from messenger RNA at the
CC termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03061, ECO:0000269|PubMed:19716793}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061, ECO:0000269|PubMed:19716793}.
CC -!- INTERACTION:
CC Q96RP9; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-2255048, EBI-5661333;
CC Q96RP9; P03508: NS; Xeno; NbExp=2; IntAct=EBI-2255048, EBI-2547979;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96RP9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RP9-2; Sequence=VSP_038189;
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 1 (COXPD1)
CC [MIM:609060]: A mitochondrial disease resulting in early rapidly
CC progressive hepatoencephalopathy. {ECO:0000269|PubMed:15537906,
CC ECO:0000269|PubMed:17160893, ECO:0000269|PubMed:21119709,
CC ECO:0000269|PubMed:26741492}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW78682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF309777; AAK58877.1; -; mRNA.
DR EMBL; AF367998; AAK53402.1; -; mRNA.
DR EMBL; AK092293; BAG52523.1; -; mRNA.
DR EMBL; AK315031; BAG37516.1; -; mRNA.
DR EMBL; AC080013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78677.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC049210; AAH49210.1; -; mRNA.
DR CCDS; CCDS33885.1; -. [Q96RP9-1]
DR CCDS; CCDS77851.1; -. [Q96RP9-2]
DR RefSeq; NP_001295093.1; NM_001308164.1. [Q96RP9-2]
DR RefSeq; NP_001295095.1; NM_001308166.1.
DR RefSeq; NP_079272.4; NM_024996.5. [Q96RP9-1]
DR PDB; 6VLZ; EM; 2.97 A; v=1-751.
DR PDB; 6VMI; EM; 2.96 A; v=1-751.
DR PDB; 6YDP; EM; 3.00 A; BC=37-751.
DR PDB; 6YDW; EM; 4.20 A; BC=37-751.
DR PDB; 7A5K; EM; 3.70 A; r1=1-751.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6YDP; -.
DR PDBsum; 6YDW; -.
DR PDBsum; 7A5K; -.
DR AlphaFoldDB; Q96RP9; -.
DR SMR; Q96RP9; -.
DR BioGRID; 124551; 315.
DR IntAct; Q96RP9; 28.
DR MINT; Q96RP9; -.
DR STRING; 9606.ENSP00000419038; -.
DR GlyGen; Q96RP9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96RP9; -.
DR MetOSite; Q96RP9; -.
DR PhosphoSitePlus; Q96RP9; -.
DR BioMuta; GFM1; -.
DR DMDM; 116241346; -.
DR EPD; Q96RP9; -.
DR jPOST; Q96RP9; -.
DR MassIVE; Q96RP9; -.
DR MaxQB; Q96RP9; -.
DR PaxDb; Q96RP9; -.
DR PeptideAtlas; Q96RP9; -.
DR PRIDE; Q96RP9; -.
DR ProteomicsDB; 78000; -. [Q96RP9-1]
DR ProteomicsDB; 78001; -. [Q96RP9-2]
DR Antibodypedia; 46773; 191 antibodies from 28 providers.
DR DNASU; 85476; -.
DR Ensembl; ENST00000264263.9; ENSP00000264263.5; ENSG00000168827.15. [Q96RP9-2]
DR Ensembl; ENST00000486715.6; ENSP00000419038.1; ENSG00000168827.15. [Q96RP9-1]
DR GeneID; 85476; -.
DR KEGG; hsa:85476; -.
DR MANE-Select; ENST00000486715.6; ENSP00000419038.1; NM_024996.7; NP_079272.4.
DR UCSC; uc003fce.4; human. [Q96RP9-1]
DR CTD; 85476; -.
DR DisGeNET; 85476; -.
DR GeneCards; GFM1; -.
DR HGNC; HGNC:13780; GFM1.
DR HPA; ENSG00000168827; Low tissue specificity.
DR MalaCards; GFM1; -.
DR MIM; 606639; gene.
DR MIM; 609060; phenotype.
DR neXtProt; NX_Q96RP9; -.
DR OpenTargets; ENSG00000168827; -.
DR Orphanet; 137681; Hepatoencephalopathy due to combined oxidative phosphorylation defect type 1.
DR PharmGKB; PA134971637; -.
DR VEuPathDB; HostDB:ENSG00000168827; -.
DR eggNOG; KOG0465; Eukaryota.
DR GeneTree; ENSGT00550000074911; -.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q96RP9; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q96RP9; -.
DR TreeFam; TF105631; -.
DR PathwayCommons; Q96RP9; -.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR SignaLink; Q96RP9; -.
DR UniPathway; UPA00345; -.
DR BioGRID-ORCS; 85476; 421 hits in 1088 CRISPR screens.
DR ChiTaRS; GFM1; human.
DR GeneWiki; GFM1; -.
DR GenomeRNAi; 85476; -.
DR Pharos; Q96RP9; Tbio.
DR PRO; PR:Q96RP9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96RP9; protein.
DR Bgee; ENSG00000168827; Expressed in endothelial cell and 180 other tissues.
DR ExpressionAtlas; Q96RP9; baseline and differential.
DR Genevisible; Q96RP9; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; IDA: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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Elongation factor;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW Primary mitochondrial disease; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 37..751
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007440"
FT DOMAIN 44..321
FT /note="tr-type G"
FT BINDING 53..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 120..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 174..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 230
FT /note="G -> GHFLRDFLPLLWNWDRRSGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038189"
FT VARIANT 57
FT /note="S -> Y (in COXPD1; dbSNP:rs1254972325)"
FT /evidence="ECO:0000269|PubMed:26741492"
FT /id="VAR_076197"
FT VARIANT 174
FT /note="N -> S (in COXPD1; dbSNP:rs119470018)"
FT /evidence="ECO:0000269|PubMed:15537906"
FT /id="VAR_021512"
FT VARIANT 215
FT /note="V -> I (in dbSNP:rs2303909)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_028303"
FT VARIANT 250
FT /note="R -> W (in COXPD1; dbSNP:rs139430866)"
FT /evidence="ECO:0000269|PubMed:21119709,
FT ECO:0000269|PubMed:26741492"
FT /id="VAR_076198"
FT VARIANT 496
FT /note="M -> R (in COXPD1; dbSNP:rs119470020)"
FT /evidence="ECO:0000269|PubMed:17160893"
FT /id="VAR_031901"
FT CONFLICT 373
FT /note="S -> C (in Ref. 1; AAK58877)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="I -> M (in Ref. 1; AAK58877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 83471 MW; 5937FFB24A089E2E CRC64;
MRLLGAAAVA ALGRGRAPAS LGWQRKQVNW KACRWSSSGV IPNEKIRNIG ISAHIDSGKT
TLTERVLYYT GRIAKMHEVK GKDGVGAVMD SMELERQRGI TIQSAATYTM WKDVNINIID
TPGHVDFTIE VERALRVLDG AVLVLCAVGG VQCQTMTVNR QMKRYNVPFL TFINKLDRMG
SNPARALQQM RSKLNHNAAF MQIPMGLEGN FKGIVDLIEE RAIYFDGDFG QIVRYGEIPA
ELRAAATDHR QELIECVANS DEQLGEMFLE EKIPSISDLK LAIRRATLKR SFTPVFLGSA
LKNKGVQPLL DAVLEYLPNP SEVQNYAILN KEDDSKEKTK ILMNSSRDNS HPFVGLAFKL
EVGRFGQLTY VRSYQGELKK GDTIYNTRTR KKVRLQRLAR MHADMMEDVE EVYAGDICAL
FGIDCASGDT FTDKANSGLS MESIHVPDPV ISIAMKPSNK NDLEKFSKGI GRFTREDPTF
KVYFDTENKE TVISGMGELH LEIYAQRLER EYGCPCITGK PKVAFRETIT APVPFDFTHK
KQSGGAGQYG KVIGVLEPLD PEDYTKLEFS DETFGSNIPK QFVPAVEKGF LDACEKGPLS
GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN ATLCILEPIM AVEVVAPNEF
QGQVIAGINR RHGVITGQDG VEDYFTLYAD VPLNDMFGYS TELRSCTEGK GEYTMEYSRY
QPCLPSTQED VINKYLEATG QLPVKKGKAK N
