GUF1_SORMK
ID GUF1_SORMK Reviewed; 690 AA.
AC D1ZET3; F7W4V2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Translation factor GUF1, 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 {ECO:0000255|HAMAP-Rule:MF_03137};
DE AltName: Full=Ribosomal back-translocase {ECO:0000255|HAMAP-Rule:MF_03137};
GN Name=GUF1 {ECO:0000255|HAMAP-Rule:MF_03137}; ORFNames=SMAC_06946;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000029; CCC12539.1; -; Genomic_DNA.
DR RefSeq; XP_003349110.1; XM_003349062.1.
DR AlphaFoldDB; D1ZET3; -.
DR SMR; D1ZET3; -.
DR STRING; 771870.D1ZET3; -.
DR EnsemblFungi; CCC12539; CCC12539; SMAC_06946.
DR GeneID; 10806625; -.
DR KEGG; smp:SMAC_06946; -.
DR VEuPathDB; FungiDB:SMAC_06946; -.
DR eggNOG; KOG0462; Eukaryota.
DR HOGENOM; CLU_009995_3_1_1; -.
DR InParanoid; D1ZET3; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 165663at2759; -.
DR Proteomes; UP000001881; 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:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
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..690
FT /note="Translation factor GUF1, mitochondrial"
FT /id="PRO_0000402905"
FT DOMAIN 89..272
FT /note="tr-type G"
FT REGION 40..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 165..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 219..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
SQ SEQUENCE 690 AA; 76096 MW; 87C956B1566989F6 CRC64;
MSAPTTTKAS ASSSPPALRP LSSSLLLTIP TTNAQLVLPS VTVPAARRHN STKSTNSTTS
TNSTTATSKM PIERRAAEIE KRIAAIPLER YRNFCIVAHI DHGKSTLSDR LLEHTGTIVA
GDGNKQVLDK LDVERERGIT VKAQTCTMIY KHKEDGLDYL LHLVDTPGHV DFRAEVTRSY
SSCSGALLLV DASQGVQAQT VANFYLAFAQ GLSLVPVVNK IDMASADVPR VLEQLETVFE
LDTSTAVKVS AKTGQGVGEI LPAVIKKMPA PVGDAKKPLR MLLVDSWYDT FKGVVLLVRL
FDGTLKQGDK VYSYATGNEY IVGEVGIQYP DAVPQKVLRA GQVGYVFFNP GMKRIQDAKL
GDTFTNVGYE DIVEPCPGFE EPKPMVFVAA FPTNQDDYGR LADSISHLVL NDRSVTLQKD
YSEALGAGWR LGFLGSLHCS VFQDRLRQEH GASIIITEPA VPTKIVWSTG QEEIVTNPAE
FPDPDDHRIR SATLYEPFVN ATVTLPEEYV GRCIEICENA RGVQKSLEFF TATQVILKYE
LPAASLVDDL FGKLKGATKG YATLDYEDAG WRQAQLVKLN LLVNKKAVDA VARIVHTSQV
ERLGRQWVTK FKEHVDRQMF EVIIQAAAGR RIVARETIKP FRKDVLAKLH ASDITRRRKL
LEKQKAGRKR LRAVGNVIID QSAFQKFLSK
