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BMT2_SCHPO
ID   BMT2_SCHPO              Reviewed;         270 AA.
AC   Q9UUH2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=25S rRNA adenine-N(1) methyltransferase {ECO:0000255|HAMAP-Rule:MF_03044};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03044};
GN   ORFNames=SPAC630.10;
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(1) position of an adenine present in
CC       helix 65 in 25S rRNA. {ECO:0000255|HAMAP-Rule:MF_03044}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03044, ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
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DR   EMBL; CU329670; CAB52732.1; -; Genomic_DNA.
DR   PIR; T38988; T38988.
DR   RefSeq; NP_592906.1; NM_001018306.2.
DR   AlphaFoldDB; Q9UUH2; -.
DR   BioGRID; 279836; 28.
DR   STRING; 4896.SPAC630.10.1; -.
DR   MaxQB; Q9UUH2; -.
DR   PaxDb; Q9UUH2; -.
DR   EnsemblFungi; SPAC630.10.1; SPAC630.10.1:pep; SPAC630.10.
DR   GeneID; 2543414; -.
DR   KEGG; spo:SPAC630.10; -.
DR   PomBase; SPAC630.10; -.
DR   VEuPathDB; FungiDB:SPAC630.10; -.
DR   eggNOG; ENOG502R82D; Eukaryota.
DR   HOGENOM; CLU_041583_1_0_1; -.
DR   InParanoid; Q9UUH2; -.
DR   OMA; KLVYYLW; -.
DR   PhylomeDB; Q9UUH2; -.
DR   PRO; PR:Q9UUH2; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; ISO:PomBase.
DR   GO; GO:0031167; P:rRNA methylation; IC:PomBase.
DR   HAMAP; MF_03044; BMT2; 1.
DR   InterPro; IPR021867; Bmt2/SAMTOR.
DR   PANTHER; PTHR21008; PTHR21008; 1.
DR   Pfam; PF11968; Bmt2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..270
FT                   /note="25S rRNA adenine-N(1) methyltransferase"
FT                   /id="PRO_0000351423"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
SQ   SEQUENCE   270 AA;  30760 MW;  BA9C840142105A9B CRC64;
     MRPIPVKNRI GKNNIDNAKG LKGNKLIRHY HNLLKEKSRL IASSAPIEKI KNVESELENI
     GIDAYQRASR SGQAEGKGGD SSKILIKWIR TTPCFSYCAR LKEPKDLLEI GSVSVDNKCS
     TCGLFRVSRI DLHSVHPLIK QQDFLERTPE EGLFTGISCS LVLNFAPPEL RAKMLLHCTG
     LLMPPNKEQP PWLFLVLPSP CITNSRYMDE KTLHSIMIQF GFICRQKSIS KKIAYYLYSY
     ECFPMKEIDW KKKIVNDGAT RNNFFIPCIL
 
 
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