ID   EFGM_RAT                Reviewed;         751 AA.
AC   Q07803; Q5U347;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 2.
DT   03-AUG-2022, entry version 150.
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   Name=Gfm1; Synonyms=Efg, Efg1, Gfm;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8332461; DOI=10.1093/nar/21.11.2641;
RA   Barker C.S., Makris A., Patriotis C., Bear S.E., Tsichlis P.N.;
RT   "Identification of the gene encoding the mitochondrial elongation factor G
RT   in mammals.";
RL   Nucleic Acids Res. 21:2641-2647(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [4]
RP   PROTEIN SEQUENCE OF 214-222 AND 292-303, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
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}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000255|HAMAP-Rule:MF_03061}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues with the highest level in
CC       liver, thymus and brain.
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=AAA41107.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L14684; AAA41107.1; ALT_FRAME; mRNA.
DR   EMBL; CH473976; EDM00923.1; -; Genomic_DNA.
DR   EMBL; BC085721; AAH85721.1; -; mRNA.
DR   PIR; S40780; S40780.
DR   RefSeq; NP_446077.1; NM_053625.1.
DR   AlphaFoldDB; Q07803; -.
DR   SMR; Q07803; -.
DR   BioGRID; 250256; 1.
DR   STRING; 10116.ENSRNOP00000040081; -.
DR   iPTMnet; Q07803; -.
DR   PhosphoSitePlus; Q07803; -.
DR   jPOST; Q07803; -.
DR   PaxDb; Q07803; -.
DR   PRIDE; Q07803; -.
DR   GeneID; 114017; -.
DR   KEGG; rno:114017; -.
DR   UCSC; RGD:631396; rat.
DR   CTD; 85476; -.
DR   RGD; 631396; Gfm1.
DR   VEuPathDB; HostDB:ENSRNOG00000012873; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   InParanoid; Q07803; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   PhylomeDB; Q07803; -.
DR   TreeFam; TF105631; -.
DR   Reactome; R-RNO-5389840; Mitochondrial translation elongation.
DR   UniPathway; UPA00345; -.
DR   PRO; PR:Q07803; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Proteomes; UP000234681; Chromosome 2.
DR   Bgee; ENSRNOG00000012873; Expressed in heart and 20 other tissues.
DR   ExpressionAtlas; Q07803; baseline and differential.
DR   Genevisible; Q07803; RN.
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; 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   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Elongation factor; GTP-binding;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..37
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           38..751
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000007443"
FT   DOMAIN          45..322
FT                   /note="tr-type G"
FT   BINDING         54..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         121..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         175..178
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT   CONFLICT        252
FT                   /note="Q -> P (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="G -> R (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="S -> L (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="N -> K (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        564..565
FT                   /note="YT -> LP (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        739
FT                   /note="T -> I (in Ref. 1; AAA41107)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   751 AA;  83457 MW;  A4DD3BD637B295E1 CRC64;
     MRLLRITAGL GRGPLPRVPA ILGWQGKQAN WKTYRWCSSG SIPNEKIRNI GISAHIDSGK
     TTLTERVLYY TGRIATMHEV KGKDGVGAVM DSMELERQRG ITIQSAATYT MWRDVNINII
     DTPGHVDFTI EVERALRVLD GAVLVLCAVG GVQCQTMTVS RQMKRYNVPF LTFINKLDRM
     GSNPARALQQ MRSKLNHNAA FVQIPIGLEG DFKGIIDLIE ERAIYFDGDF GQIVRYDEIP
     ADLRAAAADH RQELIECVAN SDEQLGELFL EEKIPSVSDL KLAIRRATLS RSFTPVFLGS
     ALKNKGVQPL LDAVLEFLPN PSEVQNYALL NQNDSKEKNK ILMNPKRDDS HPFVGLAFKL
     EAGRFGQLTY VRNYQGELKK GSTIYNTRTG KKVRVQRLVR MHADMMEDVE EVYAGDICAL
     FGIDCASGDT FTNKDNSDLS MESIHVPDPV ISVAMKPSNK NDLEKFSKGI ARFTREDPTF
     KVHFDTESKE TIVSGMGELH LEIYAQRMER EYGCPCITGK PKVAFRETVT APVPFDFTHK
     KQSGGAGQYG KVIGVLEPLA PEDYTKLEFS DETFGANVPK QFVPAVEKGF LDACEKGPLS
     GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAS ATLCIIEPIM SVEVIAPNEF
     QGAVFAGINR RHGVITGQDG IEDYFTLYAD VPLNNMFGYS TELRSCTEGK GEYTMEYNRY
     QPCSPSTQEE LVNKYLEATG QLPVKKGKAK N