GUF1_TRIAD
ID GUF1_TRIAD Reviewed; 660 AA.
AC B3RXR7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Translation factor GUF1 homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03137};
DE EC=3.6.5.-;
DE AltName: Full=Elongation factor 4 homolog {ECO:0000255|HAMAP-Rule:MF_03137};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=GTPase GUF1 homolog {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137};
GN ORFNames=TRIADDRAFT_56304;
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX NCBI_TaxID=10228;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999;
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- FUNCTION: Promotes mitochondrial protein synthesis. May act as a
CC fidelity factor of the translation reaction, by catalyzing a one-codon
CC backward translocation of tRNAs on improperly translocated ribosomes.
CC Binds to mitochondrial ribosomes in a GTP-dependent manner.
CC {ECO:0000255|HAMAP-Rule:MF_03137}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03137};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03137}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03137}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03137}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03137}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. LepA subfamily.
CC {ECO:0000305}.
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DR EMBL; DS985245; EDV24904.1; -; Genomic_DNA.
DR RefSeq; XP_002112794.1; XM_002112758.1.
DR AlphaFoldDB; B3RXR7; -.
DR SMR; B3RXR7; -.
DR STRING; 10228.TriadP56304; -.
DR EnsemblMetazoa; TriadT56304; TriadP56304; TriadG56304.
DR GeneID; 6753580; -.
DR KEGG; tad:TRIADDRAFT_56304; -.
DR CTD; 6753580; -.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_3_1; -.
DR InParanoid; B3RXR7; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 165663at2759; -.
DR PhylomeDB; B3RXR7; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR CDD; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR035654; LepA_IV.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 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 GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..660
FT /note="Translation factor GUF1 homolog, mitochondrial"
FT /id="PRO_0000402911"
FT DOMAIN 62..243
FT /note="tr-type G"
FT BINDING 71..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 136..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 190..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 660 AA; 73855 MW; 8AB9D3508DC4C68E CRC64;
MTLNLRCKVV EPSWKVLQHY ASYVRNTAAV SLVRHHARLS TSTNLTSKAA EPITALSEFP
VEKIRNFSII AHIDHGKSTL ADRLLEIAGV IPKSAENKQV LDKLQVERER GITVKAQTAS
MLYEYHGETY LLNLIDTPGH VDFNYEVSRS LAACQGVLLV VDASQGVQAQ TVANFFLAFE
ADLKIIPVLN KIDMKSANPD RIANQLQRVF DIEPEETMKV SAKDGTGIDQ LLPTIIEKIP
PPTCDQQKPL KALLFDSWYD RYRGVIGLLA IKDGKLTKGE KIQSAFSKKQ YEILDLGILY
PNEKSTKTLG SGQVGFIVAG MKSTKEAQIG DTFCHVNCPV DALPGFKPAK SMVYAGLFPF
NKSEFEVLRS AIHKLTLNDS SVSVHNDNSA ALGPGFRLGF LGLLHMDVFN QRLEQEYDVS
VVITSPNVPF KGKYRYASIL RKEHEEMVIT TPSQFPDIAQ VVEYLEPVVM GTIIFPDKYM
GKMLNLCQSK RGQQVNISYI DETRVMLKYI LPLHEIVIDF YDQLKSLTSG YASFDYEDHG
YRSATLAKME ILLNGTPVDA LTTVVHEEKA RITGKQVCQK LKEAIPRQLY EVAIQATIRG
KVVARETIRA VRKDVTAKCY GGDITRKLKL LKRQKEGKSR LKMIGKIEVP KEAFLAVLKR
