ID   EFGM_MALGO              Reviewed;         777 AA.
AC   A8PXR7;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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};
GN   Name=MEF1 {ECO:0000255|HAMAP-Rule:MF_03061}; ORFNames=MGL_1509;
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966;
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., DeAngelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L. Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(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   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       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; AAYY01000004; EDP44112.1; -; Genomic_DNA.
DR   RefSeq; XP_001731326.1; XM_001731274.1.
DR   AlphaFoldDB; A8PXR7; -.
DR   SMR; A8PXR7; -.
DR   STRING; 425265.A8PXR7; -.
DR   EnsemblFungi; EDP44112; EDP44112; MGL_1509.
DR   GeneID; 5855633; -.
DR   KEGG; mgl:MGL_1509; -.
DR   VEuPathDB; FungiDB:MGL_1509; -.
DR   InParanoid; A8PXR7; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000008837; 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   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; 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.
FT   CHAIN           1..777
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385575"
FT   DOMAIN          34..338
FT                   /note="tr-type G"
FT   BINDING         43..50
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         136..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         190..193
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   777 AA;  85901 MW;  4B2E2A9CE0AACDD1 CRC64;
     MNRIASYLRT YATEAERPMA TDVQPSESDV ERLLRQRNVG ISAHIDSGKT TLTERVLYYT
     GRIKDIHEVR GRDEVGAKMD SMELEREKGI TIQSAATYCN WKATPPTERS NMTGDAADES
     TVTTQKKHDY HINIIDTPGH VDFTIEVERA LRVLDGAVLV LCAVSGVQSQ TMTVDRQMRR
     YSVPRLSFIN KMDRAGANPW RVVEQIRTKL RMPAAAMQVP IGAEDNFQGL VDLVRWKAVY
     NEGTKGNVVR ESDDIPADVL ELAREKRQEL IEQLSDVDDE MAEIFIEERE PTIEELVAAL
     RRATVACRFS PVFLGTAIKN KGVQALLDGM CAYLPNPMEV RAIANDTAVA KKIAAQANEE
     GHDVAAMQSS AQHGSEVQLV PATEAPLVGL AFKLEESRFG QLTYMRVYQG ILRRGGIIFN
     SRTGKKVKVP RLVRMHADDM EDVQEIGPGE ICAMFGVECS SGDTFTDGST TLSMSAMFVP
     EPVISLSLTP EGKDTSVNFS RALNRFQKED PTFRVHVDSE SSETIISGMG ELHLDIYVER
     MRREYNVPCT TGKPRVAFRE TISQPAKFNY THKKQTGGAG QFGRVIGYIE PMTVDEDTGK
     DTAFVNSVMG GNIPPSYIPA CEKGFADGLE KGALAGYPVC GVRMVLEDGA AHSVDSSELA
     FRIAAHAAFR EAFRAANPTI LEPKMSVEVI APVEFQGTVI GALNQRKGTI EDTEVREDDF
     TITAEVSLND MFGFSSQLRG LTQGKGEFSM EYKKHEPVMP NVQADMEAAY KKSLEKK