Entry euk:BMT2_YEAST

ID   BMT2_YEAST              Reviewed;         337 AA.
AC   P38278; D6VQD7;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   10-MAY-2017, entry version 109.
DE   RecName: Full=25S rRNA (adenine(2142)-N(1))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03044};
DE            EC=2.1.1.286 {ECO:0000255|HAMAP-Rule:MF_03044};
DE   AltName: Full=Base MethylTransferase of 25S RNA {ECO:0000255|HAMAP-Rule:MF_03044};
GN   Name=BMT2 {ECO:0000255|HAMAP-Rule:MF_03044};
GN   OrderedLocusNames=YBR141C; ORFNames=YBR1118;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7754712; DOI=10.1002/yea.320100911;
RA   Zagulski M., Becam A.-M., Grzybowska E., Lacroute F., Migdalski A.,
RA   Slonimski P.P., Sokolowska B., Herbert C.J.;
RT   "The sequence of 12.5 kb from the right arm of chromosome II predicts
RT   a new N-terminal sequence for the IRA1 protein and reveals two new
RT   genes, one of which is a DEAD-box helicase.";
RL   Yeast 10:1227-1234(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 312.
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
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   [5]
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.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   GLY-180, AND DISRUPTION PHENOTYPE.
RX   PubMed=23558746; DOI=10.1093/nar/gkt195;
RA   Sharma S., Watzinger P., Kotter P., Entian K.D.;
RT   "Identification of a novel methyltransferase, Bmt2, responsible for
RT   the N-1-methyl-adenosine base modification of 25S rRNA in
RT   Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 41:5428-5443(2013).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the N(1) position of adenine 2142 in 25S
CC       rRNA. N(1)-methyladenine(2142) in 25S rRNA is present in helix 65,
CC       a region that accounts for most of the intersubunit surface of the
CC       large subunit. {ECO:0000255|HAMAP-Rule:MF_03044,
CC       ECO:0000269|PubMed:23558746}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + adenine(2142) in 25S
CC       rRNA = S-adenosyl-L-homocysteine + N(1)-methyladenine(2142) in 25S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_03044,
CC       ECO:0000269|PubMed:23558746}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03044, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:23558746}.
CC   -!- DISRUPTION PHENOTYPE: Loss of N(1)-methyladenine(2142) in 25S
CC       rRNA. Confers anisomycin and peroxide sensitivity to the cells as
CC       well as slight defects in ribosome subunit joining.
CC       {ECO:0000269|PubMed:23558746}.
CC   -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the BMT2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03044}.
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DR   EMBL; Z36010; CAA85099.1; -; Genomic_DNA.
DR   EMBL; X78937; CAA55538.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07257.2; -; Genomic_DNA.
DR   PIR; S46010; S46010.
DR   RefSeq; NP_009699.2; NM_001178489.2.
DR   ProteinModelPortal; P38278; -.
DR   SMR; P38278; -.
DR   BioGrid; 32841; 183.
DR   DIP; DIP-1766N; -.
DR   IntAct; P38278; 2.
DR   MINT; MINT-407203; -.
DR   MaxQB; P38278; -.
DR   EnsemblFungi; YBR141C; YBR141C; YBR141C.
DR   GeneID; 852438; -.
DR   KEGG; sce:YBR141C; -.
DR   EuPathDB; FungiDB:YBR141C; -.
DR   SGD; S000000345; BMT2.
DR   HOGENOM; HOG000171862; -.
DR   InParanoid; P38278; -.
DR   KO; K18849; -.
DR   OMA; IIRRFHL; -.
DR   OrthoDB; EOG092C3SND; -.
DR   BioCyc; YEAST:G3O-29095-MONOMER; -.
DR   PRO; PR:P38278; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0016433; F:rRNA (adenine) methyltransferase activity; IMP:SGD.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISM:SGD.
DR   HAMAP; MF_03044; BMT2; 1.
DR   InterPro; IPR021867; Bmt2.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR21008; PTHR21008; 1.
DR   Pfam; PF11968; Bmt2; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    337       25S rRNA (adenine(2142)-N(1))-
FT                                methyltransferase.
FT                                /FTId=PRO_0000202494.
FT   MUTAGEN     180    180       G->R: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:23558746}.
FT   CONFLICT    312    312       P -> S (in Ref. 1; CAA85099 and 2;
FT                                CAA55538). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       126    335       ipfam:Bmt2 [T]
FT   MYHIT        22    336       ihamap:BMT2 [T]
SQ   SEQUENCE   337 AA;  38550 MW;  CB0309828FABF3BE CRC64;
     MHSRKSKSIT GKRKQVGSNV TRVIKPQKTR RIIRRFHHLI NKRQSICKFL CLKENLDDSN
     EEKNDKIIRL SIKGNVRLGK YYEDGKSQSF NDAMESQLLR LHSLIKNESK SKDTSDLAVM
     YTLLGYIMNQ INKLGGLETY QIASQNGQLK ERGGDTSKLL EKWIRSSFEN CPGAVALEIG
     SLSSGNRISR CALFRNVVRI DLEEHEGVIK QDFMERPLPR NENDKFDLIS CSLVLNFVKN
     HRDRGAMCHR MVKFLKPQGY IFIVLPQACV THSRYCDKTL LQNLLGSIGL IMLNSHQSNK
     LYYCLYQLQV VPPQPSSFSK RIKVNDGPGL NNFGITL
//