BUD23_YEAST
ID BUD23_YEAST Reviewed; 275 AA.
AC P25627; D6VR56;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=18S rRNA (guanine(1575)-N(7))-methyltransferase;
DE EC=2.1.1.309 {ECO:0000269|PubMed:18332120};
DE AltName: Full=Bud site selection protein 23;
GN Name=BUD23; OrderedLocusNames=YCR047C; ORFNames=YCR47C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SIMILARITY TO METHYLTRANSFERASES.
RX PubMed=1304897; DOI=10.1002/pro.5560011216;
RA Bork P., Ouzounis C., Sander C., Scharf M., Schneider R., Sonnhammer E.;
RT "Comprehensive sequence analysis of the 182 predicted open reading frames
RT of yeast chromosome III.";
RL Protein Sci. 1:1677-1690(1992).
RN [5]
RP SIMILARITY TO METHYLTRANSFERASES.
RX PubMed=9873020; DOI=10.1074/jbc.274.2.814;
RA Niewmierzycka A., Clarke S.;
RT "S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae.
RT Identification of a novel protein arginine methyltransferase.";
RL J. Biol. Chem. 274:814-824(1999).
RN [6]
RP FUNCTION.
RX PubMed=11452010; DOI=10.1091/mbc.12.7.2147;
RA Ni L., Snyder M.;
RT "A genomic study of the bipolar bud site selection pattern in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 12:2147-2170(2001).
RN [7]
RP SIMILARITY TO METHYLTRANSFERASES.
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 [8]
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 [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-57 AND ASP-77.
RX PubMed=18332120; DOI=10.1128/mcb.01674-07;
RA White J., Li Z., Sardana R., Bujnicki J.M., Marcotte E.M., Johnson A.W.;
RT "Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear
RT export of pre-40S subunits.";
RL Mol. Cell. Biol. 28:3151-3161(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH TRM112.
RX PubMed=22956767; DOI=10.1091/mbc.e12-05-0370;
RA Sardana R., Johnson A.W.;
RT "The methyltransferase adaptor protein Trm112 is involved in biogenesis of
RT both ribosomal subunits.";
RL Mol. Biol. Cell 23:4313-4322(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH TRM112.
RX PubMed=22493060; DOI=10.1128/mcb.06623-11;
RA Figaro S., Wacheul L., Schillewaert S., Graille M., Huvelle E.,
RA Mongeard R., Zorbas C., Lafontaine D.L., Heurgue-Hamard V.;
RT "Trm112 is required for Bud23-mediated methylation of the 18S rRNA at
RT position G1575.";
RL Mol. Cell. Biol. 32:2254-2267(2012).
RN [13]
RP MUTAGENESIS OF GLY-57 AND ASP-77.
RX PubMed=23233232; DOI=10.1002/yea.2934;
RA Lin J.L., Yu H.C., Chao J.L., Wang C., Cheng M.Y.;
RT "New phenotypes generated by the G57R mutation of BUD23 in Saccharomyces
RT cerevisiae.";
RL Yeast 29:537-546(2012).
RN [14]
RP FUNCTION.
RX PubMed=23604635; DOI=10.1261/rna.037671.112;
RA Sardana R., White J.P., Johnson A.W.;
RT "The rRNA methyltransferase Bud23 shows functional interaction with
RT components of the SSU processome and RNase MRP.";
RL RNA 19:828-840(2013).
RN [15]
RP FUNCTION, AND INTERACTION WITH ECM16.
RX PubMed=24710271; DOI=10.1128/mcb.01656-13;
RA Sardana R., Zhu J., Gill M., Johnson A.W.;
RT "Physical and functional interaction between the methyltransferase Bud23
RT and the essential DEAH-box RNA helicase Ecm16.";
RL Mol. Cell. Biol. 34:2208-2220(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(7) position of guanine 1575 (m7G1575) in
CC 18S rRNA. Requires the methyltransferase adapter protein TRM112 for
CC full rRNA methyltransferase activity. Important for biogenesis end
CC export of the 40S ribosomal subunit independent on its
CC methyltransferase activity. Required for efficient cleavage of the
CC primary 35S precursor rRNA at site A2. Involved in positioning the
CC proximal bud pole signal. {ECO:0000269|PubMed:11452010,
CC ECO:0000269|PubMed:18332120, ECO:0000269|PubMed:22493060,
CC ECO:0000269|PubMed:22956767, ECO:0000269|PubMed:23604635,
CC ECO:0000269|PubMed:24710271}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1575) in yeast 18S rRNA + S-adenosyl-L-methionine =
CC N(7)-methylguanosine(1575) in yeast 18S rRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:43172, Rhea:RHEA-COMP:10387, Rhea:RHEA-
CC COMP:10388, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.309;
CC Evidence={ECO:0000269|PubMed:18332120};
CC -!- SUBUNIT: Interacts with TRM112. Interacts with ECM16.
CC {ECO:0000269|PubMed:22493060, ECO:0000269|PubMed:22956767,
CC ECO:0000269|PubMed:24710271}.
CC -!- INTERACTION:
CC P25627; P53738: TRM112; NbExp=5; IntAct=EBI-21924, EBI-28520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. BUD23/WBSCR22 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42295.1; -; Genomic_DNA.
DR EMBL; AY692877; AAT92896.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07525.1; -; Genomic_DNA.
DR PIR; S19460; S19460.
DR RefSeq; NP_009976.1; NM_001178761.1.
DR PDB; 4QTT; X-ray; 2.00 A; B/D=1-202.
DR PDB; 4QTU; X-ray; 2.12 A; B/D=1-202.
DR PDBsum; 4QTT; -.
DR PDBsum; 4QTU; -.
DR AlphaFoldDB; P25627; -.
DR SMR; P25627; -.
DR BioGRID; 31029; 72.
DR ComplexPortal; CPX-1047; BUD23-TRM112 methyltransferase complex.
DR DIP; DIP-4673N; -.
DR IntAct; P25627; 4.
DR MINT; P25627; -.
DR STRING; 4932.YCR047C; -.
DR MaxQB; P25627; -.
DR PaxDb; P25627; -.
DR PRIDE; P25627; -.
DR EnsemblFungi; YCR047C_mRNA; YCR047C; YCR047C.
DR GeneID; 850414; -.
DR KEGG; sce:YCR047C; -.
DR SGD; S000000643; BUD23.
DR VEuPathDB; FungiDB:YCR047C; -.
DR eggNOG; KOG1541; Eukaryota.
DR GeneTree; ENSGT00390000014737; -.
DR HOGENOM; CLU_055194_0_2_1; -.
DR InParanoid; P25627; -.
DR OMA; PHVWVGM; -.
DR BioCyc; MetaCyc:G3O-29358-MON; -.
DR BioCyc; YEAST:G3O-29358-MON; -.
DR BRENDA; 2.1.1.309; 984.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P25627; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25627; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IMP:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR039769; Bud23-like.
DR InterPro; IPR022238; Bud23_C.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12734; PTHR12734; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF12589; WBS_methylT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..275
FT /note="18S rRNA (guanine(1575)-N(7))-methyltransferase"
FT /id="PRO_0000204459"
FT REGION 256..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..264
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MUTAGEN 57
FT /note="G->E: Fails to ctalyze the N-7 methylation of the
FT G1575 residue."
FT /evidence="ECO:0000269|PubMed:18332120,
FT ECO:0000269|PubMed:23233232"
FT MUTAGEN 57
FT /note="G->R: Can only partially restore the slow-growth
FT phenotype and the random budding pattern of a null mutant."
FT /evidence="ECO:0000269|PubMed:18332120,
FT ECO:0000269|PubMed:23233232"
FT MUTAGEN 77
FT /note="D->A: No effect on growth and budding pattern."
FT /evidence="ECO:0000269|PubMed:18332120,
FT ECO:0000269|PubMed:23233232"
FT MUTAGEN 77
FT /note="D->K: Fails to ctalyze the N-7 methylation of the
FT G1575 residue."
FT /evidence="ECO:0000269|PubMed:18332120,
FT ECO:0000269|PubMed:23233232"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:4QTU"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:4QTT"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:4QTT"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:4QTT"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:4QTT"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4QTT"
SQ SEQUENCE 275 AA; 30742 MW; A8011A097C461900 CRC64;
MSRPEELAPP EIFYNDSEAH KYTGSTRVQH IQAKMTLRAL ELLNLQPCSF ILDIGCGSGL
SGEILTQEGD HVWCGLDISP SMLATGLSRE LEGDLMLQDM GTGIPFRAGS FDAAISISAI
QWLCNADTSY NDPKQRLMRF FNTLYAALKK GGKFVAQFYP KNDDQVDDIL QSAKVAGFSG
GLVVDDPESK KNKKYYLVLS SGAPPQGEEQ VNLDGVTMDE ENVNLKKQLR QRLKGGKDKE
SAKSFILRKK ELMKRRGRKV AKDSKFTGRK RRHRF
