RCM1_SCHPO
ID RCM1_SCHPO Reviewed; 460 AA.
AC O14039;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=25S rRNA (cytosine-C(5))-methyltransferase rcm1;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P53972};
DE AltName: Full=rRNA m(5)C methyltransferase 1;
GN Name=rcm1; ORFNames=SPAC2C4.06c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 methyltransferase that
CC specifically methylates the C(5) position of a cytosine in 25S rRNA.
CC {ECO:0000250|UniProtKB:P53972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47780, Rhea:RHEA-COMP:11911, Rhea:RHEA-COMP:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000250|UniProtKB:P53972};
CC -!- SUBUNIT: Interacts with trm112. {ECO:0000250|UniProtKB:P53972}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; CU329670; CAB16366.3; -; Genomic_DNA.
DR PIR; T38517; T38517.
DR RefSeq; NP_594509.3; NM_001019938.3.
DR AlphaFoldDB; O14039; -.
DR SMR; O14039; -.
DR BioGRID; 279084; 6.
DR STRING; 4896.SPAC2C4.06c.1; -.
DR MaxQB; O14039; -.
DR PaxDb; O14039; -.
DR PRIDE; O14039; -.
DR EnsemblFungi; SPAC2C4.06c.1; SPAC2C4.06c.1:pep; SPAC2C4.06c.
DR GeneID; 2542630; -.
DR KEGG; spo:SPAC2C4.06c; -.
DR PomBase; SPAC2C4.06c; rcm1.
DR VEuPathDB; FungiDB:SPAC2C4.06c; -.
DR eggNOG; KOG2360; Eukaryota.
DR HOGENOM; CLU_005316_7_4_1; -.
DR InParanoid; O14039; -.
DR OMA; NRGAVDN; -.
DR PRO; PR:O14039; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; ISO:PomBase.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..460
FT /note="25S rRNA (cytosine-C(5))-methyltransferase rcm1"
FT /id="PRO_0000317150"
FT REGION 430..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 223..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 460 AA; 51877 MW; D3E8D9742041B588 CRC64;
MDFYNHAANI LSDLSKKKGS IKQLAFNSKK HDPKRTYALV CETLKYKPVL DEIIARSELL
VLEKKLKENL ARVLVHDLLM SKRGLSISNG PIKECILRHK TRLNAEFVKL KVKKGVKSHE
ELALKNPVSL PRWLRINTIK STKDEVLQGL GLDKVSSIEE LGPDKFYIDD CVENLIAIDP
SFPIVENSLY KEGKVIIQDK ASCFPAAVLA GLTGHVGDII DGCAAPGNKT THLAACFPKS
HIFAFERDAK RVQTLRKMVG ISGANNVTIE HQDFTLTDPK SDLYRNVTHI LLDPSCSGSG
IVSRQDYLLG NEQDVTEDTE RLENLCSFQS TILKHALQFP NCRHVTYSTC SVHRLENEQV
VCEVLSQEPD WKCNSLTKTL PNWKTRGIPE YCAQPSMAEG MIRCKPGAGG TIGFFVANLY
HPQREQETFK MYKNDDDTKK RKRKKKKKEV KKKARIQGEE
