Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25627

- BUD23_YEAST

UniProt

P25627 - BUD23_YEAST

Protein

18S rRNA (guanine(1575)-N(7))-methyltransferase

Gene

BUD23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N7 position of guanine 1575 (m7G1575) in 18S rRNA. Requires the methyltransferase adapter protein TRM112 for full rRNA methyltransferase activity. Important for biogenesis end export of the 40S ribosomal subunit independent on its methyltransferase activity. Required for efficient cleavage of the primary 35S precursor rRNA at site A2. Involved in positioning the proximal bud pole signal.6 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + guanine(1575) in 18S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(1575) in 18S rRNA.1 Publication

    GO - Molecular functioni

    1. rRNA (guanine) methyltransferase activity Source: SGD
    2. S-adenosylmethionine-dependent methyltransferase activity Source: SGD

    GO - Biological processi

    1. 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) Source: SGD
    2. ribosomal small subunit export from nucleus Source: SGD
    3. rRNA (guanine-N7)-methylation Source: SGD

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29358-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    18S rRNA (guanine(1575)-N(7))-methyltransferase (EC:2.1.1.-)
    Alternative name(s):
    Bud site selection protein 23
    Gene namesi
    Name:BUD23
    Ordered Locus Names:YCR047C
    ORF Names:YCR47C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR047c.
    SGDiS000000643. BUD23.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571G → E: Fails to ctalyze the N-7 methylation of the G1575 residue. 2 Publications
    Mutagenesisi57 – 571G → R: Can only partially restore the slow-growth phenotype and the random budding pattern of a null mutant. 2 Publications
    Mutagenesisi77 – 771D → A: No effect on growth and budding pattern. 2 Publications
    Mutagenesisi77 – 771D → K: Fails to ctalyze the N-7 methylation of the G1575 residue. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27527518S rRNA (guanine(1575)-N(7))-methyltransferasePRO_0000204459Add
    BLAST

    Proteomic databases

    MaxQBiP25627.
    PaxDbiP25627.

    Expressioni

    Gene expression databases

    GenevestigatoriP25627.

    Interactioni

    Subunit structurei

    Interacts with TRM112. Interacts with ECM16.3 Publications

    Protein-protein interaction databases

    BioGridi31029. 12 interactions.
    DIPiDIP-4673N.
    IntActiP25627. 1 interaction.
    MINTiMINT-515776.
    STRINGi4932.YCR047C.

    Structurei

    3D structure databases

    ProteinModelPortaliP25627.
    SMRiP25627. Positions 40-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi257 – 2648Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0500.
    GeneTreeiENSGT00390000014737.
    HOGENOMiHOG000111527.
    OMAiRFFTTLH.
    OrthoDBiEOG71CFZD.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR013216. Methyltransf_11.
    IPR029063. SAM-dependent_MTases-like.
    IPR022238. Unchr_MeTrfase_Williams-Beuren.
    [Graphical view]
    PfamiPF08241. Methyltransf_11. 1 hit.
    PF12589. WBS_methylT. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P25627-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPEELAPP EIFYNDSEAH KYTGSTRVQH IQAKMTLRAL ELLNLQPCSF    50
    ILDIGCGSGL SGEILTQEGD HVWCGLDISP SMLATGLSRE LEGDLMLQDM 100
    GTGIPFRAGS FDAAISISAI QWLCNADTSY NDPKQRLMRF FNTLYAALKK 150
    GGKFVAQFYP KNDDQVDDIL QSAKVAGFSG GLVVDDPESK KNKKYYLVLS 200
    SGAPPQGEEQ VNLDGVTMDE ENVNLKKQLR QRLKGGKDKE SAKSFILRKK 250
    ELMKRRGRKV AKDSKFTGRK RRHRF 275
    Length:275
    Mass (Da):30,742
    Last modified:May 1, 1992 - v1
    Checksum:iA8011A097C461900
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAA42295.1.
    AY692877 Genomic DNA. Translation: AAT92896.1.
    BK006937 Genomic DNA. Translation: DAA07525.1.
    PIRiS19460.
    RefSeqiNP_009976.1. NM_001178761.1.

    Genome annotation databases

    EnsemblFungiiYCR047C; YCR047C; YCR047C.
    GeneIDi850414.
    KEGGisce:YCR047C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59720 Genomic DNA. Translation: CAA42295.1 .
    AY692877 Genomic DNA. Translation: AAT92896.1 .
    BK006937 Genomic DNA. Translation: DAA07525.1 .
    PIRi S19460.
    RefSeqi NP_009976.1. NM_001178761.1.

    3D structure databases

    ProteinModelPortali P25627.
    SMRi P25627. Positions 40-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31029. 12 interactions.
    DIPi DIP-4673N.
    IntActi P25627. 1 interaction.
    MINTi MINT-515776.
    STRINGi 4932.YCR047C.

    Proteomic databases

    MaxQBi P25627.
    PaxDbi P25627.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR047C ; YCR047C ; YCR047C .
    GeneIDi 850414.
    KEGGi sce:YCR047C.

    Organism-specific databases

    CYGDi YCR047c.
    SGDi S000000643. BUD23.

    Phylogenomic databases

    eggNOGi COG0500.
    GeneTreei ENSGT00390000014737.
    HOGENOMi HOG000111527.
    OMAi RFFTTLH.
    OrthoDBi EOG71CFZD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29358-MONOMER.

    Miscellaneous databases

    NextBioi 965971.
    PROi P25627.

    Gene expression databases

    Genevestigatori P25627.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    InterProi IPR013216. Methyltransf_11.
    IPR029063. SAM-dependent_MTases-like.
    IPR022238. Unchr_MeTrfase_Williams-Beuren.
    [Graphical view ]
    Pfami PF08241. Methyltransf_11. 1 hit.
    PF12589. WBS_methylT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53335. SSF53335. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Comprehensive sequence analysis of the 182 predicted open reading frames of yeast chromosome III."
      Bork P., Ouzounis C., Sander C., Scharf M., Schneider R., Sonnhammer E.
      Protein Sci. 1:1677-1690(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO METHYLTRANSFERASES.
    5. "S-adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase."
      Niewmierzycka A., Clarke S.
      J. Biol. Chem. 274:814-824(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO METHYLTRANSFERASES.
    6. "A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae."
      Ni L., Snyder M.
      Mol. Biol. Cell 12:2147-2170(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Automated identification of putative methyltransferases from genomic open reading frames."
      Katz J.E., Dlakic M., Clarke S.
      Mol. Cell. Proteomics 2:525-540(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO METHYLTRANSFERASES.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Bud23 methylates G1575 of 18S rRNA and is required for efficient nuclear export of pre-40S subunits."
      White J., Li Z., Sardana R., Bujnicki J.M., Marcotte E.M., Johnson A.W.
      Mol. Cell. Biol. 28:3151-3161(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-57 AND ASP-77.
    11. "The methyltransferase adaptor protein Trm112 is involved in biogenesis of both ribosomal subunits."
      Sardana R., Johnson A.W.
      Mol. Biol. Cell 23:4313-4322(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRM112.
    12. "Trm112 is required for Bud23-mediated methylation of the 18S rRNA at position G1575."
      Figaro S., Wacheul L., Schillewaert S., Graille M., Huvelle E., Mongeard R., Zorbas C., Lafontaine D.L., Heurgue-Hamard V.
      Mol. Cell. Biol. 32:2254-2267(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TRM112.
    13. "New phenotypes generated by the G57R mutation of BUD23 in Saccharomyces cerevisiae."
      Lin J.L., Yu H.C., Chao J.L., Wang C., Cheng M.Y.
      Yeast 29:537-546(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-57 AND ASP-77.
    14. "The rRNA methyltransferase Bud23 shows functional interaction with components of the SSU processome and RNase MRP."
      Sardana R., White J.P., Johnson A.W.
      RNA 19:828-840(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Physical and functional interaction between the methyltransferase Bud23 and the essential DEAH-box RNA helicase Ecm16."
      Sardana R., Zhu J., Gill M., Johnson A.W.
      Mol. Cell. Biol. 34:2208-2220(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ECM16.

    Entry informationi

    Entry nameiBUD23_YEAST
    AccessioniPrimary (citable) accession number: P25627
    Secondary accession number(s): D6VR56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1620 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3