ID RLMM_EDWI9 Reviewed; 374 AA.
AC C5BHA4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000255|HAMAP-Rule:MF_01551};
DE EC=2.1.1.186 {ECO:0000255|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000255|HAMAP-Rule:MF_01551};
GN Name=rlmM {ECO:0000255|HAMAP-Rule:MF_01551}; OrderedLocusNames=NT01EI_0823;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(2498) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(2498) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42788, Rhea:RHEA-COMP:10244, Rhea:RHEA-COMP:10245,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.186;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01551};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01551}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. RlmM subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01551}.
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DR EMBL; CP001600; ACR68040.1; -; Genomic_DNA.
DR RefSeq; WP_015870233.1; NC_012779.2.
DR AlphaFoldDB; C5BHA4; -.
DR SMR; C5BHA4; -.
DR STRING; 67780.B6E78_14715; -.
DR GeneID; 69537880; -.
DR KEGG; eic:NT01EI_0823; -.
DR PATRIC; fig|634503.3.peg.743; -.
DR HOGENOM; CLU_043780_0_0_6; -.
DR OrthoDB; 154490at2; -.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.2300.20; -; 1.
DR Gene3D; 3.30.70.2810; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01551; 23SrRNA_methyltr_M; 1.
DR InterPro; IPR040739; RlmM_FDX.
DR InterPro; IPR048646; RlmM_THUMP-like.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR011224; rRNA_MeTrfase_M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR37524; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE M; 1.
DR PANTHER; PTHR37524:SF2; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE M; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF18125; RlmM_FDX; 1.
DR Pfam; PF21239; RLMM_N; 1.
DR PIRSF; PIRSF028774; UCP028774; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..374
FT /note="Ribosomal RNA large subunit methyltransferase M"
FT /id="PRO_1000215469"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 221..224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
SQ SEQUENCE 374 AA; 42674 MW; F07E0BD7507E1FEB CRC64;
MNRLALYCRP GFEKECAAEI TDKAAALEVY GFARVKENSG YVLFECYQPD DADTLARKLP
FRELIFARQM LVVGELLKDL PPEDRIAPIC GMLLGVVEGG GELRVEVPDT NESKELLKFC
RKFTVPLRAA LREQRTLLRQ ENPYRPVVHV LFIAPGCCYV GYSYSDNNSP FYMGIPRLKF
PADAPSRSTL KLEEAFHVFI PADEWDERLG SGMRAVDLGA CPGGWTYQLV QRSMMVQAID
NGPMVPSLME TGQVTHHRAD GFRFTPEGDN DWLVCDMVEK PAKVSALMAR WLVNGWCREA
IFNLKLPMKK RYEEVSQNLA TLAQVLKENG INAQIAAKQL YHDREEVTVH VRRIWGAIPG
RRDEREFRRR EQRD
//
