ID   MTO1_YEAST              Reviewed;         669 AA.
AC   P53070; D6VV98;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Mitochondrial translation optimization protein 1;
DE   Flags: Precursor;
GN   Name=MTO1; Synonyms=IPS1; OrderedLocusNames=YGL236C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
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   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MSS1.
RX   PubMed=9774408; DOI=10.1074/jbc.273.43.27945;
RA   Colby G., Wu M., Tzagoloff A.;
RT   "MTO1 codes for a mitochondrial protein required for respiration in
RT   paromomycin-resistant mutants of Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:27945-27952(1998).
RN   [4]
RP   IDENTIFICATION OF FRAMESHIFT.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [5]
RP   MUTAGENESIS OF ALA-431.
RX   PubMed=22608499; DOI=10.1016/j.ajhg.2012.04.011;
RA   Ghezzi D., Baruffini E., Haack T.B., Invernizzi F., Melchionda L.,
RA   Dallabona C., Strom T.M., Parini R., Burlina A.B., Meitinger T.,
RA   Prokisch H., Ferrero I., Zeviani M.;
RT   "Mutations of the mitochondrial-tRNA modifier MTO1 cause hypertrophic
RT   cardiomyopathy and lactic acidosis.";
RL   Am. J. Hum. Genet. 90:1079-1087(2012).
CC   -!- FUNCTION: Involved in the 5-carboxymethylaminomethyl modification
CC       (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Forms a heterodimer with MSS1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9774408}.
CC   -!- SIMILARITY: Belongs to the MnmG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA96953.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z72758; CAA96953.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006941; DAA07882.1; -; Genomic_DNA.
DR   PIR; S64258; S64258.
DR   RefSeq; NP_011278.2; NM_001181102.1.
DR   AlphaFoldDB; P53070; -.
DR   SMR; P53070; -.
DR   BioGRID; 33004; 201.
DR   DIP; DIP-4488N; -.
DR   IntAct; P53070; 3.
DR   STRING; 4932.YGL236C; -.
DR   MaxQB; P53070; -.
DR   PaxDb; P53070; -.
DR   PRIDE; P53070; -.
DR   EnsemblFungi; YGL236C_mRNA; YGL236C; YGL236C.
DR   GeneID; 852616; -.
DR   KEGG; sce:YGL236C; -.
DR   SGD; S000003205; MTO1.
DR   VEuPathDB; FungiDB:YGL236C; -.
DR   eggNOG; KOG2311; Eukaryota.
DR   GeneTree; ENSGT00390000011297; -.
DR   HOGENOM; CLU_007831_2_2_1; -.
DR   InParanoid; P53070; -.
DR   OMA; FRPGYAI; -.
DR   BioCyc; MetaCyc:G3O-30709-MON; -.
DR   BioCyc; YEAST:G3O-30709-MON; -.
DR   PRO; PR:P53070; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53070; protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0070899; P:mitochondrial tRNA wobble uridine modification; IMP:SGD.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR   Gene3D; 1.10.150.570; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_00129; MnmG_GidA; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR004416; MnmG.
DR   InterPro; IPR002218; MnmG-rel.
DR   InterPro; IPR020595; MnmG-rel_CS.
DR   InterPro; IPR026904; MnmG_C.
DR   InterPro; IPR044920; MnmG_C_subdom.
DR   InterPro; IPR040131; MnmG_N.
DR   PANTHER; PTHR11806; PTHR11806; 1.
DR   PANTHER; PTHR11806:SF0; PTHR11806:SF0; 1.
DR   Pfam; PF01134; GIDA; 1.
DR   Pfam; PF13932; GIDA_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00136; gidA; 1.
DR   PROSITE; PS01280; GIDA_1; 1.
DR   PROSITE; PS01281; GIDA_2; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Mitochondrion; Reference proteome; Transit peptide;
KW   tRNA processing.
FT   TRANSIT         1..59
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..669
FT                   /note="Mitochondrial translation optimization protein 1"
FT                   /id="PRO_0000042687"
FT   MUTAGEN         431
FT                   /note="A->T: Does not completely restore mitochondrial DNA-
FT                   dependent respiratory chain activities in respiration-
FT                   defective mutant cells."
FT                   /evidence="ECO:0000269|PubMed:22608499"
SQ   SEQUENCE   669 AA;  74215 MW;  917F22AE324F1B87 CRC64;
     MLRVTTLASS CTSFPLQVLR RRLTISSLTS FQPTTKTQVV VIGAGHAGCE AAAASSRTGA
     HTTLITPSLT DIGKCSCNPS IGGVGKGILV KEIDALDGLM GKVTDLAGVQ FKMLNRSKGP
     AVWGPRAQID RELYKKYMQR ELSDKKAHPN LSLLQNKVAD LILYDPGCGH KVIKGVVLDD
     GTQVGADQVI ITTGTFLSAE IHIGDKRIAA GRIGEQPTYG ISNTLQNEVG FQLGRLKTGT
     PARLAKESID FSALEVQKGD ALPVPMSFLN ETVSVEPTKQ LDCFGTHTTP QMHDFLRNNL
     HQSIHIQDTT IKGPRYCPSI EAKILRFPDR SSHKIWLEPE GFNSDVIYPN GISNSMPEDV
     QLQMMRLIPG MANVEILQPA YGVEYDYVDP RQLKPSLETK LVDGLFLAGQ INGTTGYEEA
     AAQGIIAGIN AGLLSRQERE QLVLKRSEAY IGVLIDDLIN NGVIEPYRMF TSRSEFRISV
     RADNADFRLT PIGAQLGIIS PVRLSQYSRD KHLYDETIRA LQNFKLSSQK WSSLLQANIA
     PQAENRSAWE IFRFKDMDLH KLYECIPDLP INLLDIPMHV VTKINIQGKY EPYIVKQNQF
     VKAFQADENM LLPQDYDYRQ LPTLSTECKL LLNRVQPLTI GQARRIQGIT AAALFELYRV
     ARKPSQPVM