EFGM_CAEEL
ID EFGM_CAEEL Reviewed; 750 AA.
AC Q9XV52;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=gfm-1; ORFNames=F29C12.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z81519; CAB04216.1; -; Genomic_DNA.
DR PIR; T21534; T21534.
DR RefSeq; NP_496787.1; NM_064386.4.
DR AlphaFoldDB; Q9XV52; -.
DR SMR; Q9XV52; -.
DR BioGRID; 40252; 5.
DR DIP; DIP-26845N; -.
DR STRING; 6239.F29C12.4; -.
DR EPD; Q9XV52; -.
DR PaxDb; Q9XV52; -.
DR PeptideAtlas; Q9XV52; -.
DR PRIDE; Q9XV52; -.
DR EnsemblMetazoa; F29C12.4.1; F29C12.4.1; WBGene00009246.
DR GeneID; 174956; -.
DR KEGG; cel:CELE_F29C12.4; -.
DR UCSC; F29C12.4; c. elegans.
DR CTD; 174956; -.
DR WormBase; F29C12.4; CE19822; WBGene00009246; gfm-1.
DR eggNOG; KOG0465; Eukaryota.
DR GeneTree; ENSGT00550000074911; -.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q9XV52; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q9XV52; -.
DR Reactome; R-CEL-5389840; Mitochondrial translation elongation.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q9XV52; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00009246; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
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..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 25..750
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007444"
FT DOMAIN 42..319
FT /note="tr-type G"
FT BINDING 51..58
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 118..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 172..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 750 AA; 83654 MW; D054528698A18ABD CRC64;
MSPLGRFSAV AQSRRQLNNV LRRFASNEAP SSVVVPGVRP IERIRNIGIS AHIDSGKTTV
TERILYYAGR IDSMHEVRGK DDVGATMDFM DLERQRGITI QSAATYVDWH GTNINIIDTP
GHVDFTVEVE RALRVLDGAV LVLCGVGGVQ SQTFTVNRQL ARYNVPFICF VNKMDRNGAT
PLKALDGLRN KLNHNAALIH LPIGKDSNFN GIVDLVEGHA LYYEGEGGLI VRKDEIPKDL
RVEAEDRRQE LIEHIANVDE TLGEMFLNDQ TPNVQQIHEA IRRTVVKRAF VPVLSGSALK
NKGVQTMINS VVKYLPDPSE VVNRATVKTE TTGDEKGIIL SPKRNNDKPF VGLAFKLEAG
KYGQLTYFRV YQGQLSKGDT VYASRDGRKV RVQRLVRMHA ADMEEITTAY AGDICATFGL
DCHSGETFST DQNLAPHCES MHIPEPVISM AIKPVNRKDA DNFIKALTRF TKEDPTFRRE
YNQEAKETIV SGMGELHLEI YAQRMKSEYN CPVELGKPTV AYRECLGSPY KFHFRHKKQT
GGQGQFGEIE GVIDPLPSDR NTVVEFSDET FGNNIPKNLF PALKKGLDAI VAEGPLIKSR
IAGIHVRIQD GSTHAVDSTE IAMINTMQNM MRESFEKANW LLLEPIMKVE ATVPTEFQGN
VVTSLTQRNA LITTTDSTEG YATVICEAPL SDMFGYTSEL RSLTEGKGEF SMEYSRYAPT
TLEAQDRVQA EWRQLHGIAD PNEKGKKKKK
