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 27-NOV-2024, entry version 189. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-10778; -. DR EMDB; EMD-10779; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR SMR; Q96RP9; -. DR BioGRID; 124551; 338. DR IntAct; Q96RP9; 42. DR MINT; Q96RP9; -. DR STRING; 9606.ENSP00000264263; -. DR GlyGen; Q96RP9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96RP9; -. DR MetOSite; Q96RP9; -. DR PhosphoSitePlus; Q96RP9; -. DR SwissPalm; Q96RP9; -. DR BioMuta; GFM1; -. DR DMDM; 116241346; -. DR jPOST; Q96RP9; -. DR MassIVE; Q96RP9; -. DR PaxDb; 9606-ENSP00000419038; -. DR PeptideAtlas; Q96RP9; -. DR ProteomicsDB; 78000; -. [Q96RP9-1] DR ProteomicsDB; 78001; -. [Q96RP9-2] DR Pumba; Q96RP9; -. DR Antibodypedia; 46773; 186 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 AGR; HGNC:13780; -. 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; 148165at2759; -. 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; 448 hits in 1172 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 182 other cell types or tissues. DR ExpressionAtlas; Q96RP9; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. 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; 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 FunFam; 3.30.230.10:FF:000003; Elongation factor G; 1. DR FunFam; 3.30.70.240:FF:000001; Elongation factor G; 1. DR FunFam; 2.40.30.10:FF:000022; Elongation factor G, mitochondrial; 1. DR FunFam; 3.30.70.870:FF:000008; Elongation factor G, mitochondrial; 1. DR FunFam; 3.40.50.300:FF:000539; Elongation factor G, mitochondrial; 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. 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 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; KW Proteomics identification; Reference proteome; 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 //