BMT5_SCHPO
ID BMT5_SCHPO Reviewed; 282 AA.
AC O94480;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=25S rRNA (uridine-N(3))-methyltransferase;
DE EC=2.1.1.-;
GN Name=bmt5; ORFNames=SPCC1919.13c;
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(3) position of a uridine in 25S rRNA.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine in 25S rRNA = H(+) + N(3)-
CC methyluridine in 25S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54588, Rhea:RHEA-COMP:13939, Rhea:RHEA-COMP:13940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74502;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. BMT5 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22644.1; -; Genomic_DNA.
DR PIR; T41238; T41238.
DR RefSeq; NP_588495.1; NM_001023485.2.
DR AlphaFoldDB; O94480; -.
DR BioGRID; 275885; 78.
DR STRING; 4896.SPCC1919.13c.1; -.
DR MaxQB; O94480; -.
DR PaxDb; O94480; -.
DR EnsemblFungi; SPCC1919.13c.1; SPCC1919.13c.1:pep; SPCC1919.13c.
DR GeneID; 2539319; -.
DR KEGG; spo:SPCC1919.13c; -.
DR PomBase; SPCC1919.13c; bmt5.
DR VEuPathDB; FungiDB:SPCC1919.13c; -.
DR eggNOG; KOG4174; Eukaryota.
DR HOGENOM; CLU_035438_0_1_1; -.
DR InParanoid; O94480; -.
DR OMA; DSRHYCF; -.
DR PhylomeDB; O94480; -.
DR PRO; PR:O94480; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; ISO:PomBase.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR InterPro; IPR019446; BMT5-like.
DR Pfam; PF10354; DUF2431; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..282
FT /note="25S rRNA (uridine-N(3))-methyltransferase"
FT /id="PRO_0000343148"
FT REGION 18..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 32345 MW; 4A68370682D80D5D CRC64;
MGKKARFKEA RRLQKRNLNN AIGSSSINSQ NSLTNDKIGK GKNKGPTERY VLPFEKNNRF
LLLGEGNFSF AFSLLLHHVS SEGFVLATSY DSKEDLKQKY PDAAEYISKI EINGGKVMHE
IDATKLHLHK KLKTQKFDTI FWNFPHSGKG IKDQDRNILD NQKMLLAFFK ASKFLLSEKG
VIVITLAETK PYTLWNLKGL AKDAGYTSLM TEKFDSSFYP EYSHRRTIGW IDGISERSPW
KGELRDSRHY CFVVNGSNIK PYNQRKEKRK RSELSDDSSD SS
