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 03-AUG-2022, entry version 139.
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}; OrderedLocusNames=YBR141C;
GN ORFNames=YBR1118;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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 a new
RT N-terminal sequence for the IRA1 protein and reveals two new genes, one of
RT 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; DOI=10.1002/j.1460-2075.1994.tb06923.x;
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., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA 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 GLY-180,
RP 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 the N-
RT 1-methyl-adenosine base modification of 25S rRNA in Saccharomyces
RT 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 rRNA.
CC N(1)-methyladenine(2142) in 25S rRNA is present in helix 65, a region
CC that accounts for most of the intersubunit surface of the large
CC subunit. {ECO:0000255|HAMAP-Rule:MF_03044,
CC ECO:0000269|PubMed:23558746}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(2142) in 25S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(1)-methyladenosine(2142) in 25S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43784, Rhea:RHEA-COMP:10691, Rhea:RHEA-COMP:10692,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.286;
CC Evidence={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 rRNA.
CC Confers anisomycin and peroxide sensitivity to the cells as well as
CC slight defects in ribosome subunit joining.
CC {ECO:0000269|PubMed:23558746}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {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 AlphaFoldDB; P38278; -.
DR BioGRID; 32841; 189.
DR DIP; DIP-1766N; -.
DR IntAct; P38278; 2.
DR MINT; P38278; -.
DR STRING; 4932.YBR141C; -.
DR MaxQB; P38278; -.
DR PaxDb; P38278; -.
DR PRIDE; P38278; -.
DR EnsemblFungi; YBR141C_mRNA; YBR141C; YBR141C.
DR GeneID; 852438; -.
DR KEGG; sce:YBR141C; -.
DR SGD; S000000345; BMT2.
DR VEuPathDB; FungiDB:YBR141C; -.
DR eggNOG; ENOG502R82D; Eukaryota.
DR HOGENOM; CLU_041583_1_0_1; -.
DR InParanoid; P38278; -.
DR OMA; KLVYYLW; -.
DR BioCyc; YEAST:G3O-29095-MON; -.
DR PRO; PR:P38278; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38278; protein.
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 Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03044; BMT2; 1.
DR InterPro; IPR021867; Bmt2/SAMTOR.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR21008; PTHR21008; 1.
DR Pfam; PF11968; Bmt2; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..337
FT /note="25S rRNA (adenine(2142)-N(1))-methyltransferase"
FT /id="PRO_0000202494"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT BINDING 201
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03044"
FT MUTAGEN 180
FT /note="G->R: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:23558746"
FT CONFLICT 312
FT /note="P -> S (in Ref. 1; CAA85099 and 2; CAA55538)"
FT /evidence="ECO:0000305"
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
