ID   BUD23_SCHPO             Reviewed;         268 AA.
AC   Q10162;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=18S rRNA (guanine-N(7))-methyltransferase bud23;
DE            EC=2.1.1.-;
DE   AltName: Full=Bud site selection protein 23 homolog;
GN   Name=bud23; ORFNames=SPAC26A3.06;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(7) position of a guanine in 18S rRNA.
CC       Important for biogenesis end export of the 40S ribosomal subunit
CC       independent on its methyltransferase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a guanosine in 18S rRNA + S-adenosyl-L-methionine = an N(7)-
CC         methylguanosine in 18S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:54584, Rhea:RHEA-COMP:13937, Rhea:RHEA-COMP:13938,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74480;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. BUD23/WBSCR22 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93229.1; -; Genomic_DNA.
DR   PIR; T38394; T38394.
DR   RefSeq; NP_594149.1; NM_001019573.2.
DR   AlphaFoldDB; Q10162; -.
DR   SMR; Q10162; -.
DR   BioGRID; 279138; 10.
DR   STRING; 4896.SPAC26A3.06.1; -.
DR   MaxQB; Q10162; -.
DR   PaxDb; Q10162; -.
DR   EnsemblFungi; SPAC26A3.06.1; SPAC26A3.06.1:pep; SPAC26A3.06.
DR   GeneID; 2542685; -.
DR   KEGG; spo:SPAC26A3.06; -.
DR   PomBase; SPAC26A3.06; bud23.
DR   VEuPathDB; FungiDB:SPAC26A3.06; -.
DR   eggNOG; KOG1541; Eukaryota.
DR   HOGENOM; CLU_055194_0_2_1; -.
DR   InParanoid; Q10162; -.
DR   OMA; PHVWVGM; -.
DR   PhylomeDB; Q10162; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q10162; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; ISO:PomBase.
DR   GO; GO:0070476; P:rRNA (guanine-N7)-methylation; ISO:PomBase.
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   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..268
FT                   /note="18S rRNA (guanine-N(7))-methyltransferase bud23"
FT                   /id="PRO_0000116474"
FT   REGION          246..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..268
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   268 AA;  30083 MW;  0EEC30BED8608FE3 CRC64;
     MSRPEHIAPP EIFYNDVEAG KYSTNTRIQS IQTEMSERAL ELLDAEGPSF ILDIGCGSGI
     STQIGESQGH VVVGMDISPS MLSVALESQE IEGDLLLCDM GTGVPFRPGT FDGVISISAI
     QWLLNADKTC NVPQRRLNRF FQTLYISMKR GGRAVMQYYP ETEKSQQMIM DTARKAGFAG
     GIVVDHPESK RQKKYYLVLQ AGGTRTLDIS SMTLDQEGTN AKQRKLKKKQ DMSTREYIIH
     KKELNRKRGR LHVPKDSKYS GRRRKAAF