ID   EFGM_TALSN              Reviewed;         804 AA.
AC   B8MJJ5;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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; ORFNames=TSTA_046490;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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   -!- 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; EQ962657; EED15195.1; -; Genomic_DNA.
DR   RefSeq; XP_002485148.1; XM_002485103.1.
DR   AlphaFoldDB; B8MJJ5; -.
DR   SMR; B8MJJ5; -.
DR   STRING; 441959.B8MJJ5; -.
DR   PRIDE; B8MJJ5; -.
DR   EnsemblFungi; EED15195; EED15195; TSTA_046490.
DR   GeneID; 8099560; -.
DR   VEuPathDB; FungiDB:TSTA_046490; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   InParanoid; B8MJJ5; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   PhylomeDB; B8MJJ5; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001745; 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; Transit peptide.
FT   TRANSIT         1..9
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           10..804
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385585"
FT   DOMAIN          103..389
FT                   /note="tr-type G"
FT   BINDING         112..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         187..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         241..244
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   804 AA;  89606 MW;  1E87D6145CA5F2D1 CRC64;
     MVRPAQVRAL SGLARSATFV RLLPSQSQNA LRCASLPVSR LGALPLRATT QITSAPLRQW
     HQIRNSSATA TASLAEQAAA DPEGLSQAEI ISNIDAEEWK RISKVRNIGI AAHIDSGKTT
     ATERVLFYTG RINAIHEVRG RDSVGAKMDS MDLEREKGIT IQSAATFCDW VKKENGKEEK
     YHFNLIDTPG HIDFTIEVER ALRVLDGAVM ILCAVSGVQS QTITVDRQMK RYNVPRISFV
     NKMDRMGANP FKAIDQINNK LKLPAAAVQV PIGAEDEFQG VVDLIRMKAI YNEGPRGETI
     VEKDEIPEHI KPLAEERRRI LIETLADVDD EIAEIFLDER EPTIEQIKAA IRRATIALKF
     TPVFMGSALA DKSIQPMLDG VCDYLPNPSE VTNLALDQKR KEAQVKLLPY GSQPFVGLAF
     KLEESNFGQL TYIRVYQGTL RKGANVFNAR NDKKVKVPRI VRMHSNEMEE VQEIGAGEIC
     AVFGVDCASG DTFTDGQLAY TMSSMFVPEP VISLSIKPKN NKDSANFSKA MARFQREDPT
     FRVSYDTESE QTIISGMGEL HLDIYVERMR REYKVDCETG QPQVAYRETI GRRVEFDHLL
     KKQSGGPGDY ARVVGWMEPS ESLEENKFEE QIVGGAISEK FLFACEKGFN LACEKGPLIG
     HKVLGTKMVI NDGATHMTDS SEMSFKNATQ QAFRKAFMES QPHVLEPLMK TVVTAPIEFQ
     GDVIGLLNKR NATINDSEIG VDEFTVYADC SLNGMFGFSS HLRAATQGKG EYTMEFSHYE
     KAPGQLQKEL VQKYLKAQAD RHKK