ID   EFGM_PYRTR              Reviewed;         801 AA.
AC   B2WBM8;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=PTRG_07041;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231621; EDU49960.1; -; Genomic_DNA.
DR   RefSeq; XP_001937373.1; XM_001937338.1.
DR   AlphaFoldDB; B2WBM8; -.
DR   SMR; B2WBM8; -.
DR   STRING; 45151.EDU49960; -.
DR   EnsemblFungi; EDU49960; EDU49960; PTRG_07041.
DR   GeneID; 6345312; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_0_1; -.
DR   InParanoid; B2WBM8; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001471; 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; Reference proteome; Transit peptide.
FT   TRANSIT         1..65
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           66..801
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385582"
FT   DOMAIN          100..387
FT                   /note="tr-type G"
FT   BINDING         109..116
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         185..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         239..242
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   801 AA;  89154 MW;  4C53B541DD01F5E0 CRC64;
     MRVQSLLRAQ SLATSSLRCS ARSVARAPSR CALSTIAASR TPYTNGSKTD TWIEGQKIQN
     QRRWQTTAAK VLEQAKDDPS TLTQEKIVEN LDPVEWERLS RVRNIGIAAH IDSGKTTATE
     RVLFYTGRIN AIHEVRGKDA VGAKMDSMDL EREKGITIQS AATFCDWVKK NDEGKEEKYH
     INLIDTPGHI DFTIEVERAL RVLDGAVMIL CAVSGVQSQT ITVDRQMRRY NIPRISFVNK
     MDRMGANPWK AVEQINQKLR IPAAALQVPI GREDGFLGVV DLVRMKAIYN EGPKGEIIRE
     TDEIPADIVE LCKEKRQELI EKLADVDDEI AEIFLDEKEP TIAQIKAAIR RATISLKFTP
     VMMGSALADK SVQPMLDAVC DYLPNPSEVE NMALDKKRAE APVKLVSYNS LPFVGLAFKL
     EESSFGQLTY IRVYQGTLRK GMNVFNARSD KKIRIPKIVR MHSNDMEEIP EIGAGEICAV
     FGVDCASGDT FTDGNLAYTM TSMFVPEPVI SLSIKPKHTK DTPNFSKAMS RFTREDPTFR
     VHTDAESQET IISGMGELHL DIYVERMRRE YRVECETGQP QVAYRETMTQ RVNFDHTLKK
     QSGGSGDYAR VVGWMEPAES LGENKFEQQI SGGTISEKFL FACEKGFMAS TAKGPLLGHR
     VLGTSMVIND GATHAVDSSE MAFKNATQQA FRKAFKAGAP QVLEPLMKTT ITAPNEFQGS
     VVGLLNKRNA VINDTEIGPE DFTVYADCSL NSMFGFSSQL RASTQGKGEF SMEFSHYSPA
     PPQLQRELVA KYEKEQAAKN A