BMT6_YEAST
ID BMT6_YEAST Reviewed; 365 AA.
AC Q12291; D6VY64;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=25S rRNA (uridine(2843)-N(3))-methyltransferase;
DE EC=2.1.1.312 {ECO:0000269|PubMed:24335083};
DE AltName: Full=Base methyltransferase of 25S RNA 6;
GN Name=BMT6; OrderedLocusNames=YLR063W; ORFNames=L2174;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-294.
RX PubMed=24335083; DOI=10.1093/nar/gkt1281;
RA Sharma S., Yang J., Duttmann S., Watzinger P., Kotter P., Entian K.D.;
RT "Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for
RT the m3U methylations of 25S rRNA in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 42:3246-3260(2014).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC specifically methylates the N(3) position of uridine 2843 (m3U2843) in
CC 25S rRNA. {ECO:0000269|PubMed:24335083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2843) in 25S rRNA = H(+) +
CC N(3)-methyluridine(2843) in 25S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43184, Rhea:RHEA-COMP:10393, Rhea:RHEA-COMP:10394,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; EC=2.1.1.312;
CC Evidence={ECO:0000269|PubMed:24335083};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:24335083}. Nucleus {ECO:0000269|PubMed:24335083}.
CC Note=Localizes predominantly to the cytoplasm, with minor localizations
CC in the nucleus (PubMed:24335083). Associates with pre-60S ribosomal
CC particles (PubMed:24335083). {ECO:0000269|PubMed:24335083}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; X94607; CAA64309.1; -; Genomic_DNA.
DR EMBL; Z73235; CAA97619.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09380.1; -; Genomic_DNA.
DR PIR; S61636; S61636.
DR RefSeq; NP_013164.1; NM_001181950.1.
DR AlphaFoldDB; Q12291; -.
DR BioGRID; 31337; 58.
DR DIP; DIP-4828N; -.
DR IntAct; Q12291; 2.
DR STRING; 4932.YLR063W; -.
DR iPTMnet; Q12291; -.
DR MaxQB; Q12291; -.
DR PaxDb; Q12291; -.
DR PRIDE; Q12291; -.
DR EnsemblFungi; YLR063W_mRNA; YLR063W; YLR063W.
DR GeneID; 850752; -.
DR KEGG; sce:YLR063W; -.
DR SGD; S000004053; BMT6.
DR VEuPathDB; FungiDB:YLR063W; -.
DR eggNOG; ENOG502QR34; Eukaryota.
DR GeneTree; ENSGT00530000068169; -.
DR HOGENOM; CLU_028833_1_0_1; -.
DR InParanoid; Q12291; -.
DR OMA; FFYRLYR; -.
DR BioCyc; MetaCyc:G3O-32216-MON; -.
DR BioCyc; YEAST:G3O-32216-MON; -.
DR BRENDA; 2.1.1.312; 984.
DR PRO; PR:Q12291; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12291; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IMP:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISM:SGD.
DR GO; GO:0070475; P:rRNA base methylation; IMP:SGD.
DR InterPro; IPR021463; Methyltransf_34.
DR Pfam; PF11312; Methyltransf_34; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..365
FT /note="25S rRNA (uridine(2843)-N(3))-methyltransferase"
FT /id="PRO_0000247230"
FT MUTAGEN 294
FT /note="G->R: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24335083"
SQ SEQUENCE 365 AA; 42041 MW; A072FB00FD3A110C CRC64;
MLLMRRFAFL TSSVYFKYIP IYSQYHYSSQ FPINMNPKKV AQLPVHNKST LPPQEIIDLF
KITFLEELYP KDQDNEKSPL TEQIQAVKSD LYNRDYNAAF NNDSKRIAYC CRWSPSRATS
YASVFAHFPE LLKIIRCEID DKDSNVLCIG GGAGGELVAL ASIFTLSRDF SSKFASALKI
DNEVNKKPRN LNIQLVDIAD WSTVVEKLTA TIKSKWLYGD SEAESFNVNF THKDCLQMTE
PQDIKIYQGL DLITLLFTTN ELFTQKKVES IKFLQRLNEN CAPGCHLLIL ESAGSYSHIT
INNKKFPIQF LIDTILVGNR KDKGTTGPWS LVSENDSIWY RMDPKLDYSI PLENMRFFYR
LYVKN
