OMS1_YEAST
ID OMS1_YEAST Reviewed; 471 AA.
AC Q06668; D6VSU5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Methyltransferase OMS1, mitochondrial;
DE EC=2.1.1.-;
DE AltName: Full=OXA1 multicopy suppressor 1;
DE Flags: Precursor;
GN Name=OMS1; OrderedLocusNames=YDR316W;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION.
RX PubMed=12872006; DOI=10.1074/mcp.m300037-mcp200;
RA Katz J.E., Dlakic M., Clarke S.;
RT "Automated identification of putative methyltransferases from genomic open
RT reading frames.";
RL Mol. Cell. Proteomics 2:525-540(2003).
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 FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15355998; DOI=10.1074/jbc.m404861200;
RA Lemaire C., Guibet-Grandmougin F., Angles D., Dujardin G., Bonnefoy N.;
RT "A yeast mitochondrial membrane methyltransferase-like protein can
RT compensate for oxa1 mutations.";
RL J. Biol. Chem. 279:47464-47472(2004).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Mitochondrial methyltransferase which suppresses respiratory
CC defects caused by OXA1 mutations when overexpressed.
CC {ECO:0000269|PubMed:12872006, ECO:0000269|PubMed:15355998}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15355998,
CC ECO:0000269|PubMed:16823961}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15355998,
CC ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
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DR EMBL; U28374; AAB64752.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12155.1; -; Genomic_DNA.
DR PIR; S61202; S61202.
DR RefSeq; NP_010602.3; NM_001180624.3.
DR AlphaFoldDB; Q06668; -.
DR SMR; Q06668; -.
DR BioGRID; 32369; 356.
DR DIP; DIP-6431N; -.
DR IntAct; Q06668; 12.
DR STRING; 4932.YDR316W; -.
DR iPTMnet; Q06668; -.
DR MaxQB; Q06668; -.
DR PaxDb; Q06668; -.
DR PRIDE; Q06668; -.
DR EnsemblFungi; YDR316W_mRNA; YDR316W; YDR316W.
DR GeneID; 851911; -.
DR KEGG; sce:YDR316W; -.
DR SGD; S000002724; OMS1.
DR VEuPathDB; FungiDB:YDR316W; -.
DR eggNOG; KOG4300; Eukaryota.
DR GeneTree; ENSGT00940000175010; -.
DR HOGENOM; CLU_665906_0_0_1; -.
DR InParanoid; Q06668; -.
DR OMA; TWGCRWN; -.
DR BioCyc; YEAST:G3O-29874-MON; -.
DR PRO; PR:Q06668; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06668; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:SGD.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR027034; OMS1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42912:SF60; PTHR42912:SF60; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Membrane; Methyltransferase; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..471
FT /note="Methyltransferase OMS1, mitochondrial"
FT /id="PRO_0000268693"
FT TOPO_DOM 40..103
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:15355998"
FT TRANSMEM 104..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..471
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:15355998"
FT REGION 450..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 55589 MW; 4F6403DCD14E69A6 CRC64;
MIVFRRFPTC LLHHIRQPAS RSLLLESQRR SLSFTSYKYN SSHIDDDKSK KKLKNVFQMN
SNRVIRKQKT KEELAKERFE EQLRSPNRFV RWGAIARSEK FSKGMTKYMI GAYVIFLIYG
LFFTKKLFAK DKELERLLKK QEEGNANEYE ALRIKELKGK LRRRDELKLE EYKKMQEEGI
ENFDDIRVQN FDQNKLNEQI LPARDTTNFY QEKANEYDKA INMEERVIFL GKRRKWLMKH
CQGDVLEVSC GTGRNIKYLD MSRINSITFL DSSENMMEIT HKKFREKFPK YKKVAFVVGK
AENLVDLAEK GKPSLENEKE NQVKYDTIVE AFGLCSHEDP VKALNNFGKL LKPDGRIILL
EHGRGQYDFI NKILDNRAER RLNTWGCRWN LDLGEVLDDS DLELVEEKRT HLGTTWCIVA
KRKGDVKKKD ELGFVEKYLQ SSIRKRMESF EKKDDMASKK ELEPVPPVSK S
