MRM2_SCHPO
ID MRM2_SCHPO Reviewed; 218 AA.
AC P78860;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000250|UniProtKB:P53123};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P53123};
DE AltName: Full=21S rRNA (uridine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:P53123};
DE Flags: Precursor;
GN Name=mrm2 {ECO:0000250|UniProtKB:P53123};
GN ORFNames=SPBC2G2.15c {ECO:0000312|PomBase:SPBC2G2.15c};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-218.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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 2'-O-ribose
CC methyltransferase that catalyzes the formation of the 2'-O-
CC methyluridine corresponding to position 2791 in S.cerevisiae 21S
CC mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally
CC conserved modification in the peptidyl transferase domain of the mtLSU
CC rRNA. {ECO:0000250|UniProtKB:P53123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in 21S rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methyluridine in 21S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47760, Rhea:RHEA-COMP:11901, Rhea:RHEA-COMP:11902,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC Evidence={ECO:0000250|UniProtKB:P53123};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17895.1; -; Genomic_DNA.
DR EMBL; D89210; BAA13871.1; -; mRNA.
DR PIR; T40154; T40154.
DR PIR; T43014; T43014.
DR RefSeq; NP_596444.1; NM_001022363.2.
DR AlphaFoldDB; P78860; -.
DR SMR; P78860; -.
DR STRING; 4896.SPBC2G2.15c.1; -.
DR PaxDb; P78860; -.
DR EnsemblFungi; SPBC2G2.15c.1; SPBC2G2.15c.1:pep; SPBC2G2.15c.
DR GeneID; 2540444; -.
DR KEGG; spo:SPBC2G2.15c; -.
DR PomBase; SPBC2G2.15c; mrm2.
DR VEuPathDB; FungiDB:SPBC2G2.15c; -.
DR eggNOG; KOG4589; Eukaryota.
DR HOGENOM; CLU_009422_4_0_1; -.
DR InParanoid; P78860; -.
DR OMA; HRQTDHL; -.
DR PhylomeDB; P78860; -.
DR PRO; PR:P78860; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; ISO:PomBase.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..218
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000155590"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 59..62
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 96..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 218 AA; 24743 MW; 02936061A0EA0CAA CRC64;
MFGSKTLFSW AAKRSKDFYR KKSKIDNFRS RAAYKLIELN SKYRFINKED VVIDVGFAPG
SWSQVAKKLV GNKGKVIGID IQHIAPPEGV LPIYGDIRDP NTLTKLFEAL RLLHEPNTND
SIDCRVVDAV ISDMLHKATG IRIRDHALSM ELCASALHVA LTFLKSNGSF ICKFYMGDED
ADLQNLLKSH FRFVQVMKPK ASLKESREAY FVCLERKP
