GUF1_YEAST
ID GUF1_YEAST Reviewed; 645 AA.
AC P46943; D6VYT5; Q05891;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
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}; OrderedLocusNames=YLR289W;
GN ORFNames=L8003.7;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=8553703; DOI=10.1002/yea.320111312;
RA Kiser G.L., Weinert T.L.;
RT "GUF1, a gene encoding a novel evolutionarily conserved GTPase in budding
RT yeast.";
RL Yeast 11:1311-1316(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=16415861; DOI=10.1038/nchembio762;
RA Butcher R.A., Bhullar B.S., Perlstein E.O., Marsischky G., LaBaer J.,
RA Schreiber S.L.;
RT "Microarray-based method for monitoring yeast overexpression strains
RT reveals small-molecule targets in TOR pathway.";
RL Nat. Chem. Biol. 2:103-109(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18442968; DOI=10.1074/jbc.m710037200;
RA Bauerschmitt H., Funes S., Herrmann J.M.;
RT "The membrane-bound GTPase Guf1 promotes mitochondrial protein synthesis
RT under suboptimal conditions.";
RL J. Biol. Chem. 283:17139-17146(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, ECO:0000269|PubMed:18442968}.
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, ECO:0000269|PubMed:16415861};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03137, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18442968}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03137, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18442968}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03137, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:18442968}.
CC -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96351.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U22360; AAA96351.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U17243; AAB67335.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09601.1; -; Genomic_DNA.
DR PIR; S50374; S50374.
DR RefSeq; NP_013392.1; NM_001182177.1.
DR AlphaFoldDB; P46943; -.
DR SMR; P46943; -.
DR BioGRID; 31555; 60.
DR DIP; DIP-2842N; -.
DR IntAct; P46943; 5.
DR MINT; P46943; -.
DR STRING; 4932.YLR289W; -.
DR BindingDB; P46943; -.
DR ChEMBL; CHEMBL1250406; -.
DR MaxQB; P46943; -.
DR PaxDb; P46943; -.
DR PRIDE; P46943; -.
DR EnsemblFungi; YLR289W_mRNA; YLR289W; YLR289W.
DR GeneID; 850996; -.
DR KEGG; sce:YLR289W; -.
DR SGD; S000004280; GUF1.
DR VEuPathDB; FungiDB:YLR289W; -.
DR eggNOG; KOG0462; Eukaryota.
DR GeneTree; ENSGT00550000074940; -.
DR HOGENOM; CLU_009995_3_1_1; -.
DR InParanoid; P46943; -.
DR OMA; MVQIAIQ; -.
DR BioCyc; YEAST:G3O-32384-MON; -.
DR PRO; PR:P46943; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P46943; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
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; IPR004161; EFTu-like_2.
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 PANTHER; PTHR43512; PTHR43512; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..645
FT /note="Translation factor GUF1, mitochondrial"
FT /id="PRO_0000091560"
FT DOMAIN 44..228
FT /note="tr-type G"
FT BINDING 53..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 120..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT BINDING 174..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03137"
FT CONFLICT 260
FT /note="S -> F (in Ref. 1; AAA96351)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="A -> P (in Ref. 1; AAA96351)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="E -> Q (in Ref. 1; AAA96351)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="G -> R (in Ref. 1; AAA96351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 73188 MW; BA1C371CCFECDC9B CRC64;
MLKFRIRPVR HIRCYKRHAY FLRYNHTTTP AQKLQAQIEQ IPLENYRNFS IVAHVDHGKS
TLSDRLLEIT HVIDPNARNK QVLDKLEVER ERGITIKAQT CSMFYKDKRT GKNYLLHLID
TPGHVDFRGE VSRSYASCGG AILLVDASQG IQAQTVANFY LAFSLGLKLI PVINKIDLNF
TDVKQVKDQI VNNFELPEED IIGVSAKTGL NVEELLLPAI IDRIPPPTGR PDKPFRALLV
DSWYDAYLGA VLLVNIVDGS VRKNDKVICA QTKEKYEVKD IGIMYPDRTS TGTLKTGQVG
YLVLGMKDSK EAKIGDTIMH LSKVNETEVL PGFEEQKPMV FVGAFPADGI EFKAMDDDMS
RLVLNDRSVT LERETSNALG QGWRLGFLGS LHASVFRERL EKEYGSKLII TQPTVPYLVE
FTDGKKKLIT NPDEFPDGAT KRVNVAAFHE PFIEAVMTLP QEYLGSVIRL CDSNRGEQID
ITYLNTNGQV MLKYYLPLSH LVDDFFGKLK SVSRGFASLD YEDAGYRISD VVKLQLLVNG
NAIDALSRVL HKSEVERVGR EWVKKFKEYV KSQLYEVVIQ ARANNKIIAR ETIKARRKDV
LQKLHASDVS RRKKLLAKQK EGKKHMKTVG NIQINQEAYQ AFLRR
