ID EFGM_DANRE Reviewed; 745 AA.
AC Q08BB1;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 119.
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; ORFNames=zgc:154041;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC124798; AAI24799.1; -; mRNA.
DR RefSeq; NP_001073463.1; NM_001079994.1.
DR AlphaFoldDB; Q08BB1; -.
DR SMR; Q08BB1; -.
DR STRING; 7955.ENSDARP00000087584; -.
DR PaxDb; 7955-ENSDARP00000087584; -.
DR GeneID; 561840; -.
DR KEGG; dre:561840; -.
DR AGR; ZFIN:ZDB-GENE-061013-79; -.
DR CTD; 85476; -.
DR ZFIN; ZDB-GENE-061013-79; gfm1.
DR eggNOG; KOG0465; Eukaryota.
DR HOGENOM; CLU_002794_4_0_1; -.
DR InParanoid; Q08BB1; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 148165at2759; -.
DR PhylomeDB; Q08BB1; -.
DR TreeFam; TF105631; -.
DR Reactome; R-DRE-5389840; Mitochondrial translation elongation.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q08BB1; -.
DR Proteomes; UP000000437; Chromosome 15.
DR Bgee; ENSDARG00000063624; Expressed in muscle tissue and 29 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 2: Evidence at transcript level;
KW Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 31..745
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000385538"
FT DOMAIN 39..316
FT /note="tr-type G"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 115..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 169..172
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
SQ SEQUENCE 745 AA; 82749 MW; 76D4E023B7DA1B18 CRC64;
MRLLRAASSL ARLHRPGHST LQQVLISCRS CSNGITPNER IRNIGISAHI DSGKTTLTER
VLYYTGRIAE MHEVRGKDGV GAIMDSMELE RQRGITIQSA ATYTMWKNHN INIIDTPGHV
DFTIEVERSL RVLDGAVLVL CAVGGVQCQT VTVNRQMKRY SVPFLTFINK LDRLGANPNR
ALQQLRTKLN QNAAFVNIPI GLEGNLRGII DLIEERSIVF DGPFGESVRY EDIPPEMRSE
AADRRQELVE CVANADETLG EMFLEERVPT VLDLKAAVRR ATVKRSFSPV LVGSALKNKG
VQPLLDAVLE YLPNPTEVQN YAILNEEGES EGSKILMDST RDDTQPFVGL AFKLEAGRFG
QLTYVRVYQG CLRKTDYIHN SRTGRRVRVQ RLVRLHADQM EDVEVAYAGD ICALFGIDCA
SGDTFTARNN ANLSMESIHV PEPVISMAIR PSNKNDTDKL SKGISRFTRE DPTFRVHFDT
ESKETIISGM GELHLEIYSQ RMEREYSCPC VMGKPKVAFR ETLTSAVPFE YTHKKQSGGS
GQYGKVIGVL EPLDSENYTK VEFSDETVGT NIPKQFVPAV EKGFRDACEK GPLIGHKISG
VRFVLEDGAH HMVDSNEISF IRAGEGAVKQ ALEKATVVIL EPVMSVEIVA PNEFQGAVIA
GVNRRHGVIS GQDGADGYFT LYADIPLNDM FGYATELRSC TEGKGEYTME YSRYQPCAAS
VQEDLVNKHL EATGQLPAKK SKWKN
//
