EFGM_XENLA
ID EFGM_XENLA Reviewed; 748 AA.
AC A5PKR8;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=gfm1; Synonyms=efg1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fat body;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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. Does
CC not mediate the disassembly of ribosomes from messenger RNA at the
CC termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-
CC 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; BC142588; AAI42589.1; -; mRNA.
DR RefSeq; NP_001093367.1; NM_001099897.1.
DR AlphaFoldDB; A5PKR8; -.
DR SMR; A5PKR8; -.
DR GeneID; 100101315; -.
DR KEGG; xla:100101315; -.
DR CTD; 100101315; -.
DR Xenbase; XB-GENE-983075; gfm1.L.
DR OrthoDB; 637899at2759; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 100101315; Expressed in testis and 19 other tissues.
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; 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 2: Evidence at transcript level;
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..748
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385539"
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 748 AA; 83523 MW; F8808C50F3B94776 CRC64;
MRLLREASKL GPRLLQYNGV TRNKPLSLAF CRHCSSGIVP NERIRNIGIS AHIDSGKTTL
TERVLYYTGR IAHMHEVKGK DGVGAVMDSM ELERQRGITI QSAATYTMWK DTNINIIDTP
GHVDFTIEVE RALRVLDGAV LVLCAVGGVQ CQTMTVNRQM KRYNVPFLTF INKLDRMGSN
PSRAVLQLRS KLNHNAAFIQ IPIGVESKFK GIIDLVEERA MYFDGEFGQS VRYDDIPAEF
RAEATDRRQE LIESVANSDE ILGEMFLEEK IPTVADLKPA IRRATLKRLF TPVLVGSALK
NKGVQPLLDA VLEYLPNPSE VQNFAILNHE NSEETSRILM KSDRDSSQPF VGLAFKLEAG
RFGQLTYVRV YQGMLRKSDY IYNTRTGKKV RVQRLVCLHA DIMEDIEEAY AGDICALFGI
DCASGDTFTS KSNDNLSMES IHVPDPVISV SMKPTNKNDL DKFSKGISRF TREDPTFRVH
YEVESKETIV SGMGELHLEI YAQRMEREYA CPCVMGKPKV AFRETISNTA PFDFTHKKQS
GGAGQYGKVI GFLEPLEPES YTKVEFEDKT VGTNVPKQFV PAVERGFREA CEKGPLTGHK
ISGLRFVLED GAHHMVDSNE ISFIRAGEGA LKQAMEKSTV CILEPIMSVE IVAPSEFQGP
VIAGINRRHG VIVGQDGSDG YFTLYADVPL NDMFGYASEL RSCTEGKGEY TMDYSRYQPC
LPSTQEELIN KYLEATGQLP AKKGKVKG
