ID   EFGM_PENRW              Reviewed;         799 AA.
AC   B6H460;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Pc13g07720;
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS   54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA   van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA   Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920428; CAP91841.1; -; Genomic_DNA.
DR   RefSeq; XP_002559201.1; XM_002559155.1.
DR   AlphaFoldDB; B6H460; -.
DR   SMR; B6H460; -.
DR   STRING; 1108849.XP_002559201.1; -.
DR   PRIDE; B6H460; -.
DR   EnsemblFungi; CAP91841; CAP91841; PCH_Pc13g07720.
DR   GeneID; 8309933; -.
DR   KEGG; pcs:Pc13g07720; -.
DR   VEuPathDB; FungiDB:PCH_Pc13g07720; -.
DR   eggNOG; KOG0465; Eukaryota.
DR   HOGENOM; CLU_002794_4_1_1; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 637899at2759; -.
DR   BioCyc; PCHR:PC13G07720-MON; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000000724; Contig Pc00c13.
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..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   CHAIN           34..799
FT                   /note="Elongation factor G, mitochondrial"
FT                   /id="PRO_0000385578"
FT   DOMAIN          97..384
FT                   /note="tr-type G"
FT   BINDING         106..113
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         182..186
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT   BINDING         236..239
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ   SEQUENCE   799 AA;  88561 MW;  DAA0587701097CBB CRC64;
     MRSPSLARLQ TRAVFGLTRS ARFQPQTLLR QRCASTAAFR SAAVAPAYQS KLGQWDQRRN
     ASAAASAVLE AAKVNPDGLS QTAIIDNLDP VEAARLDKCR NIGIAAHIDS GKTTCTERVL
     FYTGRIKAIH EVRGRDSVGA KMDSMDLERE KGITIQSAAT FCDWVKKDKE GVEQKYHLNL
     IDTPGHIDFT IEVERALRVL DGAVMILCAV SGVQSQTITV DRQMRRYNVP RISFVNKMDR
     MGANPFKAVD QINNKLKMPA AAVQVPIGAE DEFEGVVDLI RMKALYNVGG SGEEIMEKDE
     IPEKVKAIAE ERRTMLIETL ADVDDEIAEI FLEELTPSED QIRAAIRRAT IGLKFTPVFM
     GSALANKSVQ PMLDGVIDYL PNPAEVENLA LDQKREEASV KLVPYNSLPF VGLAFKLEES
     NFGQLTYIRV YQGTLRKGAN VFNARNSKKV KVPRIVRMHS NDMEEVSEIG AGEICAVFGI
     ECASGDTFTD GTLGYSMSSM FVPEPVVSLS IKPKQSKDGA NFSKAMARFQ REDPTFRVSY
     DSESDQTIIS GMGELHLDIY VERMRREYRV DCETGQPQVA YRETIGNRVE FDHLLKKQSG
     GPGEFARVMG YMEPTGALEE NKFEQQVIGG SISEKFLYAC EKGFNLSCEK GPLIGHKVLG
     TRMVINDGAT HMTDSSEMSF KNATQQAFRK AFAESQPSVL EPLMKTVVTA PTEFQGDVIG
     LLNKRNATIN DTETGVDEFT VHADCSLNGM FGFSSNLRAA TQGKGEYTME FSHYEKAPPH
     MQKELIAKYV KAQADRHKK