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Database: UniProt
Entry: EFGM_CAEEL
LinkDB: EFGM_CAEEL
Original site: 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   27-MAR-2024, entry version 164.
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; 6.
DR   DIP; DIP-26845N; -.
DR   STRING; 6239.F29C12.4.2; -.
DR   EPD; Q9XV52; -.
DR   PaxDb; 6239-F29C12-4; -.
DR   PeptideAtlas; 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   AGR; WB:WBGene00009246; -.
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; 148165at2759; -.
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 cell types or 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; cd01886; EF-G; 1.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd04097; mtEFG1_C; 1.
DR   CDD; cd04091; mtEFG1_II_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR047872; EFG_IV.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_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   NCBIfam; TIGR00484; EF-G; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43636; ELONGATION FACTOR G, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43636:SF2; ELONGATION FACTOR G, MITOCHONDRIAL; 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; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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
//
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