EFGM_KLULA
ID EFGM_KLULA Reviewed; 755 AA.
AC Q6CRY5;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
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};
GN OrderedLocusNames=KLLA0D05467g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382124; CAH00400.1; -; Genomic_DNA.
DR RefSeq; XP_453304.1; XM_453304.1.
DR AlphaFoldDB; Q6CRY5; -.
DR SMR; Q6CRY5; -.
DR STRING; 28985.XP_453304.1; -.
DR EnsemblFungi; CAH00400; CAH00400; KLLA0_D05467g.
DR GeneID; 2893410; -.
DR KEGG; kla:KLLA0_D05467g; -.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q6CRY5; -.
DR OMA; AATTCHW; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000598; Chromosome D.
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..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 39..755
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385573"
FT DOMAIN 63..344
FT /note="tr-type G"
FT BINDING 72..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 143..147
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 197..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 755 AA; 83436 MW; B6DF4CC79CFB72A8 CRC64;
MFKRVGLIAG IAGPVAGSSR FSAVSFSKRA FSASSKRCTY EEERAVLDEI QPLLSEKDID
ASKKLRNIGI SAHIDSGKTT FTERVLYYTG RIKAIHEVRG RDNVGAKMDS MDLEREKGIT
IQSAATYCSW DKDNESYHFN LIDTPGHIDF TIEVERALRI LDGAVLVVCA VSGVQSQTVT
VDRQMRRYNV PRVTFINKMD RMGANPFRSI EQINNKLRIP AAAIQVPIGA ESELKGVVNI
IDRVAIYNEG SNGEKLVTGP VPEDLKDLVE EKRALLIETL ADVDDEIAEI FLEEKEPSVD
EIKAAIRRAT IARKFSPVLM GSALANTGIQ NVLDAIVEYL PNPSEVLNTG LDIAKDETKV
NLIPSSTQPF VGLAFKLEEG KYGQLTYIRV YQGKMRKGGY ITNVKTGKKV KISRLVRMHS
NDMEDVDEVG AGEICATFGI DCSSGDTFTD GTLKYSMSSM FVPDAVISLS ITPKSKDSTN
FSKALNRFQK EDPTFRVRFD PESKETVISG MGELHLEIYV ERMRREYNVE CVTGKPQVSY
RESIQSSAEF DYTHKKQSGG AGQYGRVMGN LSHIENSNTN NFETAIVGGR IPDKYLAACA
KGFEEACEKG PLIGHRVLGV NMLINDGAIH AVDSNELAFK TATMAAFRQA FLESQPVILE
PIMNVSVTSP NEFQGNVIGL MNKLQAVIQD TENGQDEFTI TAECPLNTMF GFATSLRAST
QGKGEFSLEF KHYAPASPQL QKQLIADYQK KQQQK
