ID   EFGM_YEAS1              Reviewed;         761 AA.
AC   B3LT39;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=MEF1 {ECO:0000255|HAMAP-Rule:MF_03061}; ORFNames=SCRG_05054;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- PTM: The precursor is processed in two steps involving mitochondrial
CC       intermediate peptidase (MIP) and mitochondrial processing peptidase
CC       (MPP). {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; CH408054; EDV09374.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LT39; -.
DR   SMR; B3LT39; -.
DR   EnsemblFungi; EDV09374; EDV09374; SCRG_05054.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000008335; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IEA:UniProtKB-UniRule.
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; Transit peptide.
FT   TRANSIT         1..42
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           43..761
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385589"
FT   DOMAIN          68..349
FT                   /note="tr-type G"
FT   BINDING         77..84
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         148..152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         202..205
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   761 AA;  84616 MW;  F2515A758676152F CRC64;
     MSVQKMMRVP RKMVGGRIPF FTCSKVFSGF SRRSFHESPL ARSTYEEEKV LVDEIKQKLT
     PDDIERCNKL RNIGISAHID SGKTTFTERV LYYTKRIKAI HEVRGRDNVG AKMDSMDLER
     EKGITIQSAA TYCSWDKEGK NYHFNLIDTP GHIDFTIEVE RALRVLDGAV LVVCAVSGVQ
     SQTVTVDRQM RRYNVPRVTF INKMDRMGSD PFRAIEQLNS KLKIPAAAVQ IPIGSESSLS
     GVVDLINRVA IYNKGDNGEI IEKGPVPENL KPLMEEKRQL LIETLADVDD EMAEMFLEEK
     EPTTQQIKDA IRRSTIARSF TPVLMGSALA NTGIQPVLDA IVDYLPNPSE VLNTALDVSN
     NEAKVNLVPA VQQPFVGLAF KLEEGKYGQL TYVRVYQGRL RKGNYITNVK TGKKVKVARL
     VRMHSSEMED VDEVGSGEIC ATFGIDCASG DTFTDGSVQY SMSSMYVPDA VVSLSITPNS
     KDASNFSKAL NRFQKEDPTF RVKFDPESKE TIISGMGELH LEIYVERMRR EYNVDCVTGK
     PQVSYRESIT IPADFDYTHK KQSGGAGQYG RVIGTLSPVD DITKGNIFET AIVGGRIPDK
     YLAACGKGFE EVCEKGPLIG HRVLDVKMLI NDGAIHAVDS NELSFKTATM SAFRDAFLRA
     QPVIMEPIMN VSVTSPNEFQ GNVIGLLNKL QAVIQDTENG HDEFTLKAEC ALSTMFGFAT
     SLRASTQGKG EFSLEFSHYA PTAPHVQKEL ISEFQKKQAK K