EFGM_CANDC
ID EFGM_CANDC Reviewed; 761 AA.
AC B9W9T4;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=CD36_12130;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992688; CAX45568.1; -; Genomic_DNA.
DR RefSeq; XP_002417853.1; XM_002417808.1.
DR AlphaFoldDB; B9W9T4; -.
DR SMR; B9W9T4; -.
DR STRING; 42374.XP_002417853.1; -.
DR PRIDE; B9W9T4; -.
DR EnsemblFungi; CAX45568; CAX45568; CD36_12130.
DR GeneID; 8045403; -.
DR KEGG; cdu:CD36_12130; -.
DR CGD; CAL0000166175; Cd36_12130.
DR VEuPathDB; FungiDB:CD36_12130; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002605; Chromosome 1.
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; 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; 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..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 34..761
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385565"
FT DOMAIN 66..347
FT /note="tr-type G"
FT BINDING 75..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 146..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 200..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 761 AA; 84344 MW; ADB38F3B11DFFFEE CRC64;
MTSVLRGVLK THLPRTLTLP RCARNFQTTT FLRNEQVKLP QTYDEEKVII DEINENLKPD
DLQASTRLRN IGISAHIDSG KTTFTERVLF YTGRIKAIHE VRGKDSVGAK MDHMDLEREK
GITIQSAATY CSWDKDDKSY HFNLIDTPGH IDFTIEVERA LRVLDGAVLV VCAVAGVQSQ
TVTVDRQMRR YNVPRVTFIN KMDRMGANPW RAIEQINAKL KIPAAAIQVP IGAEENLQGV
VNIIDRVALY NEGSQGETIR KAEIPEDLKE LVEEKRALLI ETLADVDEEM ADIYLEGEEP
TVEQIKSAIR RATIGRKFTP VLMGSALANR GIQSVLDSVV DYLPQPNEVL NTGLELQKDG
SEKPVHLTPS SSEPFVGLAF KLEEGPYGQL TYIRVYQGKL KKGAYMTHVK TGKKVKVSRL
VRMHSNDMED VAEVGAGEIC ATFGIDCASG DTFIGQGTQQ QITMSSMFVP EAVISLSISP
KTKDNGAFSK AMNRFQKEDP TFRVHYDSES KETIISGMGE LHLEIYVERI KREYGVDCIT
GKPQVSYREA ITVPSAFDYT HKKQSGGAGQ YGRVIGEMNP IESENKFETQ IIGGKIPEKF
LFACSKGFED CLEKGPLIGH RVLGVHMLIN DGQTHVVDSS ELAFRTATHG AFKQAFLNAQ
PVILEPIMSV EVTAPNEFQG SVVGLINKLG GMINDTVNGP DDFTVTAECS LNSMFGFSTS
LRASTQGKGE FSLEFLKYSP TAPQVQKQLI QEYQKAQAAK K
