MRM2_YEAST
ID MRM2_YEAST Reviewed; 320 AA.
AC P53123; D6VU13;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000303|PubMed:11867542};
DE EC=2.1.1.168 {ECO:0000269|PubMed:11867542};
DE AltName: Full=21S rRNA (uridine(2791)-2'-O)-methyltransferase {ECO:0000303|PubMed:11867542};
DE AltName: Full=21S rRNA [Um2791] 2'-O-methyltransferase {ECO:0000303|PubMed:11867542};
DE Flags: Precursor;
GN Name=MRM2 {ECO:0000303|PubMed:11867542};
GN OrderedLocusNames=YGL136C {ECO:0000312|SGD:S000003104}; ORFNames=G2830;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840506;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<887::aid-yea971>3.0.co;2-d;
RA Escribano V., Eraso P., Portillo F., Mazon M.J.;
RT "Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces cerevisiae
RT chromosome VII reveals SEC27, SSM1b, a putative S-adenosylmethionine-
RT dependent enzyme and six new open reading frames.";
RL Yeast 12:887-892(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
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-methyluridine at
CC position 2791 (Um2791) in the 21S mitochondrial large subunit ribosomal
CC RNA (mtLSU rRNA), a universally conserved modification in the peptidyl
CC transferase domain of the mtLSU rRNA. {ECO:0000269|PubMed:11867542}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(2791) in 21S rRNA = 2'-O-
CC methyluridine(2791) in 21S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42728, Rhea:RHEA-COMP:10204, Rhea:RHEA-COMP:10205,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.168;
CC Evidence={ECO:0000269|PubMed:11867542};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11867542}.
CC -!- DISRUPTION PHENOTYPE: Loses mitochondrial DNA with high frequency.
CC {ECO:0000269|PubMed:11867542}.
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; X92670; CAA63360.1; -; Genomic_DNA.
DR EMBL; Z72658; CAA96847.1; -; Genomic_DNA.
DR EMBL; AY558500; AAS56826.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07974.1; -; Genomic_DNA.
DR PIR; S64149; S64149.
DR RefSeq; NP_011379.1; NM_001181001.1.
DR AlphaFoldDB; P53123; -.
DR SMR; P53123; -.
DR BioGRID; 33116; 560.
DR STRING; 4932.YGL136C; -.
DR MaxQB; P53123; -.
DR PaxDb; P53123; -.
DR PRIDE; P53123; -.
DR EnsemblFungi; YGL136C_mRNA; YGL136C; YGL136C.
DR GeneID; 852741; -.
DR KEGG; sce:YGL136C; -.
DR SGD; S000003104; MRM2.
DR VEuPathDB; FungiDB:YGL136C; -.
DR eggNOG; KOG4589; Eukaryota.
DR HOGENOM; CLU_009422_2_0_1; -.
DR InParanoid; P53123; -.
DR OMA; WSQVAVN; -.
DR BioCyc; YEAST:G3O-30631-MON; -.
DR BRENDA; 2.1.1.168; 984.
DR PRO; PR:P53123; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53123; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IDA:SGD.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IDA:SGD.
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 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..320
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000155588"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 83..86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 178..179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 320 AA; 37423 MW; 2B76FC4A6628377C CRC64;
MILVYNRIRS IISSSLGRIH VRYNSNSQNR WLNRQLKDPY TKEAKVQNLR SRAAFKLMQI
DDKYRLFSKN RTDQRILDLG YAPGAWSQVA RQRSSPNSMI LGVDILPCEP PHGVNSIQAN
ILAKRTHDLI RLFFSKHFQL NRHDDLHKDH GYFQNMLEEE LTHVKDTELY REIFTSDDIY
ETPNTNSTLI EREKFPVDVI ISDMYEPWPQ TTGFWNNITN QAYFRMANTS GVSIRDHYQS
IDLCDAALVT AIDLLRPLGS FVCKLYTGEE ENLFKKRMQA VFTNVHKFKP DASRDESKET
YYIGLKKKRN VDKLDVFSNS
