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 27-MAR-2024, entry version 175. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7WTN; EM; 3.40 A; CB=1-275. DR PDB; 7WTP; EM; 3.80 A; CB=1-275. DR PDB; 7WTQ; EM; 3.70 A; CB=1-275. DR PDB; 7WTR; EM; 3.50 A; CB=1-275. DR PDBsum; 4QTT; -. DR PDBsum; 4QTU; -. DR PDBsum; 7WTN; -. DR PDBsum; 7WTP; -. DR PDBsum; 7WTQ; -. DR PDBsum; 7WTR; -. DR AlphaFoldDB; P25627; -. DR EMDB; EMD-32792; -. DR EMDB; EMD-32794; -. DR EMDB; EMD-32795; -. DR EMDB; EMD-32796; -. DR SMR; P25627; -. DR BioGRID; 31029; 105. 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; 4932-YCR047C; -. DR PeptideAtlas; P25627; -. DR EnsemblFungi; YCR047C_mRNA; YCR047C; YCR047C. DR GeneID; 850414; -. DR KEGG; sce:YCR047C; -. DR AGR; SGD:S000000643; -. 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; FYPKNDE; -. DR OrthoDB; 5486608at2759; -. DR BioCyc; MetaCyc:G3O-29358-MONOMER; -. DR BioCyc; YEAST:G3O-29358-MONOMER; -. DR BRENDA; 2.1.1.309; 984. DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR BioGRID-ORCS; 850414; 6 hits in 10 CRISPR screens. 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 CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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:SF0; 18S RRNA (GUANINE-N(7))-METHYLTRANSFERASE-RELATED; 1. DR PANTHER; PTHR12734; METHYLTRANSFERASE-RELATED; 1. DR Pfam; PF08241; Methyltransf_11; 1. DR Pfam; PF12589; WBS_methylT; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //