BMT5_YEAST
ID BMT5_YEAST Reviewed; 336 AA.
AC P40493; D6VVJ1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=25S rRNA (uridine(2634)-N(3))-methyltransferase;
DE EC=2.1.1.313 {ECO:0000269|PubMed:24335083};
DE AltName: Full=Base methyltransferase of 25S RNA 5;
GN Name=BMT5; OrderedLocusNames=YIL096C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 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 [4]
RP IDENTIFICATION AS METHYLTRANSFERASE, AND SAM-BINDING.
RX PubMed=21858014; DOI=10.1371/journal.pone.0023168;
RA Wlodarski T., Kutner J., Towpik J., Knizewski L., Rychlewski L.,
RA Kudlicki A., Rowicka M., Dziembowski A., Ginalski K.;
RT "Comprehensive structural and substrate specificity classification of the
RT Saccharomyces cerevisiae methyltransferome.";
RL PLoS ONE 6:E23168-E23168(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SAM-BINDING, AND
RP MUTAGENESIS OF GLY-182.
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 2634 (m3U2634) in
CC 25S rRNA. {ECO:0000269|PubMed:24335083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2634) in 25S rRNA = H(+) +
CC N(3)-methyluridine(2634) in 25S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43188, Rhea:RHEA-COMP:10395, Rhea:RHEA-COMP:10396,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; EC=2.1.1.313;
CC Evidence={ECO:0000269|PubMed:24335083};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24335083}.
CC -!- MISCELLANEOUS: Present with 2960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. BMT5 family. {ECO:0000305}.
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DR EMBL; Z38125; CAA86285.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08457.1; -; Genomic_DNA.
DR PIR; S48477; S48477.
DR RefSeq; NP_012170.1; NM_001179444.1.
DR AlphaFoldDB; P40493; -.
DR BioGRID; 34895; 48.
DR DIP; DIP-5098N; -.
DR IntAct; P40493; 1.
DR MINT; P40493; -.
DR STRING; 4932.YIL096C; -.
DR MaxQB; P40493; -.
DR PaxDb; P40493; -.
DR PRIDE; P40493; -.
DR EnsemblFungi; YIL096C_mRNA; YIL096C; YIL096C.
DR GeneID; 854711; -.
DR KEGG; sce:YIL096C; -.
DR SGD; S000001358; BMT5.
DR VEuPathDB; FungiDB:YIL096C; -.
DR eggNOG; KOG4174; Eukaryota.
DR GeneTree; ENSGT00940000160701; -.
DR HOGENOM; CLU_035438_1_0_1; -.
DR InParanoid; P40493; -.
DR OMA; NIMFNFP; -.
DR BioCyc; MetaCyc:G3O-31355-MON; -.
DR BioCyc; YEAST:G3O-31355-MON; -.
DR BRENDA; 2.1.1.313; 984.
DR PRO; PR:P40493; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40493; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IMP:SGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR GO; GO:0070475; P:rRNA base methylation; IMP:SGD.
DR InterPro; IPR019446; BMT5-like.
DR Pfam; PF10354; DUF2431; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Nucleus; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..336
FT /note="25S rRNA (uridine(2634)-N(3))-methyltransferase"
FT /id="PRO_0000202971"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 182
FT /note="G->R: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:24335083"
SQ SEQUENCE 336 AA; 39402 MW; C36EC3034A746A11 CRC64;
MARKLKGKIG SKGLKGALLR HKAKVKLVRN IESKQKHELR KKNSSANNKT VKRNQEFQKL
NQGKVMPFEK DETLMLCGEG DFSFARSIVE QNYIESDNLI ITSYDNSVNE LKLKYPHTFE
ENYQYLKDLN IPIFFQIDVT KLVKSFKISK NNTWFKIINR LSDHRWGNKP LQNIVFNFPH
NGKGIKDQER NIREHQDLIF NFFQNSLQLF NLINTKIQND TLRYTQGYDL NEDTPQAKKL
TAEGYGNIIL SLFDGEPYDS WQIKLLAKKN GLTLSRSSKF QWENFPGYHH RRTNSEQDTT
KPAKERDARF YIFSKYVSNS SKHNRKSKKD TDSDSD
