MRM1_YEAST
ID MRM1_YEAST Reviewed; 412 AA.
AC P25270; D6W2Q8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000303|PubMed:11867542};
DE EC=2.1.1.- {ECO:0000269|PubMed:8266080};
DE AltName: Full=21S rRNA (guanosine(2270)-2'-O)-methyltransferase {ECO:0000303|PubMed:8266080};
DE AltName: Full=21S rRNA [Gm2270] 2'-O-methyltransferase {ECO:0000303|PubMed:8266080};
DE AltName: Full=Mitochondrial large ribosomal RNA ribose methylase {ECO:0000303|PubMed:8266080};
DE AltName: Full=Petite colonies protein 56 {ECO:0000303|PubMed:3001645};
DE Flags: Precursor;
GN Name=MRM1 {ECO:0000303|PubMed:11867542};
GN Synonyms=PET56 {ECO:0000303|PubMed:3001645};
GN OrderedLocusNames=YOR201C {ECO:0000312|SGD:S000005727};
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 [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8266080; DOI=10.1126/science.8266080;
RA Sirum-Connolly K., Mason T.L.;
RT "Functional requirement of a site-specific ribose methylation in ribosomal
RT RNA.";
RL Science 262:1886-1889(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RX PubMed=3001645; DOI=10.1093/nar/13.23.8587;
RA Struhl K.;
RT "Nucleotide sequence and transcriptional mapping of the yeast pet56-his3-
RT ded1 gene region.";
RL Nucleic Acids Res. 13:8587-8601(1985).
RN [5]
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 [6]
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 [7]
RP GENE NAME.
RX PubMed=11867542; DOI=10.1093/emboj/21.5.1139;
RA Pintard L., Bujnicki J.M., Lapeyre B., Bonnerot C.;
RT "MRM2 encodes a novel yeast mitochondrial 21S rRNA methyltransferase.";
RL EMBO J. 21:1139-1147(2002).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of 2'-O-methylguanosine
CC at position 2270 (Gm2270) in the 21S mitochondrial large subunit
CC ribosomal RNA (mtLSU rRNA), a universally conserved modification in the
CC peptidyl transferase domain of the mtLSU rRNA. This modification seems
CC to be important for the normal accumulation of the mitochondrial large
CC ribosomal subunit. {ECO:0000269|PubMed:8266080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(2270) in 21S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(2270) in 21S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47768, Rhea:RHEA-COMP:11905, Rhea:RHEA-COMP:11906,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445;
CC Evidence={ECO:0000269|PubMed:8266080};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; L19947; AAA74564.1; -; Genomic_DNA.
DR EMBL; Z75107; CAA99414.1; -; Genomic_DNA.
DR EMBL; X03245; CAA27002.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10974.1; -; Genomic_DNA.
DR PIR; S48881; S48881.
DR RefSeq; NP_014844.3; NM_001183620.3.
DR AlphaFoldDB; P25270; -.
DR SMR; P25270; -.
DR BioGRID; 34597; 160.
DR DIP; DIP-2603N; -.
DR IntAct; P25270; 12.
DR MINT; P25270; -.
DR STRING; 4932.YOR201C; -.
DR iPTMnet; P25270; -.
DR MaxQB; P25270; -.
DR PaxDb; P25270; -.
DR PRIDE; P25270; -.
DR TopDownProteomics; P25270; -.
DR EnsemblFungi; YOR201C_mRNA; YOR201C; YOR201C.
DR GeneID; 854376; -.
DR KEGG; sce:YOR201C; -.
DR SGD; S000005727; MRM1.
DR VEuPathDB; FungiDB:YOR201C; -.
DR eggNOG; KOG0838; Eukaryota.
DR GeneTree; ENSGT00390000018761; -.
DR HOGENOM; CLU_021322_5_1_1; -.
DR InParanoid; P25270; -.
DR OMA; VMSRRNC; -.
DR BioCyc; YEAST:G3O-33707-MON; -.
DR PRO; PR:P25270; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P25270; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008989; F:rRNA (guanine-N1-)-methyltransferase activity; IDA:SGD.
DR GO; GO:0000154; P:rRNA modification; IDA:SGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..412
FT /note="rRNA methyltransferase 1, mitochondrial"
FT /id="PRO_0000058321"
SQ SEQUENCE 412 AA; 46387 MW; C01B10254C0EDEA8 CRC64;
MTSLTNAVFK RYLAVTPSAH QALKTRIKKK SSSFDKFFPQ QSNSRKKQWE TLNEDKASWF
KRKYAHVHAR EQDRAADPYG KKKAHVEKLK EIKNQAKLNQ KSHKSKFQNK DIALKLMNDN
PIFEYVYGTN SVYAALLNPS RNCHSRLLYH GTIPSKFLQI VDELKVTTEL VDKHRLNLLT
NYGVHNNIAL ETKPLQPVEI AYLGDMDTSS AALSIHELGF NNENIPHELP YGTKTDAKKF
PLGLYLDEIT DPHNIGAIIR SAYFLGVDFI VMSRRNCSPL TPVVSKTSSG ALELLPIFYV
DKPLEFFTKS QEMGGWTFIT SHLANATSEK YTVGKTISMH DLNGLCNELP VVLVVGNESQ
GVRTNLKMRS DFFVEIPFGG IEKGNRAPEP IVDSLNVSVA TALLIDNILT CK
