Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

BUD23

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 11-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00390000014737.
HOGENOMiHOG000111527.
InParanoidiP25627.
OMAiRFFTTLH.
OrthoDBiEOG71CFZD.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR013216. Methyltransf_11.
IPR029063. SAM-dependent_MTases.
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

        10         20         30         40         50
MSRPEELAPP EIFYNDSEAH KYTGSTRVQH IQAKMTLRAL ELLNLQPCSF
60 70 80 90 100
ILDIGCGSGL SGEILTQEGD HVWCGLDISP SMLATGLSRE LEGDLMLQDM
110 120 130 140 150
GTGIPFRAGS FDAAISISAI QWLCNADTSY NDPKQRLMRF FNTLYAALKK
160 170 180 190 200
GGKFVAQFYP KNDDQVDDIL QSAKVAGFSG GLVVDDPESK KNKKYYLVLS
210 220 230 240 250
SGAPPQGEEQ VNLDGVTMDE ENVNLKKQLR QRLKGGKDKE SAKSFILRKK
260 270
ELMKRRGRKV AKDSKFTGRK RRHRF
Length:275
Mass (Da):30,742
Last modified:May 1, 1992 - v1
Checksum:iA8011A097C461900
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP25627.
SMRiP25627. Positions 11-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP25627.
PaxDbiP25627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYCR047c.
SGDiS000000643. BUD23.

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00390000014737.
HOGENOMiHOG000111527.
InParanoidiP25627.
OMAiRFFTTLH.
OrthoDBiEOG71CFZD.

Enzyme and pathway databases

BioCyciYEAST:G3O-29358-MONOMER.

Miscellaneous databases

NextBioi965971.
PROiP25627.

Gene expression databases

GenevestigatoriP25627.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.