ID RLMM_HAEIN Reviewed; 363 AA. AC P45100; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 110. 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}; GN OrderedLocusNames=HI_1195; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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 + S-adenosyl-L-homocysteine + H(+); 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC22849.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC22849.1; ALT_INIT; Genomic_DNA. DR PIR; H64168; H64168. DR AlphaFoldDB; P45100; -. DR SMR; P45100; -. DR STRING; 71421.HI_1195; -. DR EnsemblBacteria; AAC22849; AAC22849; HI_1195. DR KEGG; hin:HI_1195; -. DR PATRIC; fig|71421.8.peg.1247; -. DR eggNOG; COG2933; Bacteria. DR HOGENOM; CLU_043780_0_0_6; -. DR OrthoDB; 154490at2; -. DR PhylomeDB; P45100; -. DR BioCyc; HINF71421:G1GJ1-1226-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0070677; F:rRNA (cytosine-2'-O-ribose)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. 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 NCBIfam; NF008734; PRK11760.1; 1. DR PANTHER; PTHR37524; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE M; 1. DR PANTHER; PTHR37524:SF2; RIBOSOMAL RNA METHYLTRANSFERASE FTSJ DOMAIN-CONTAINING PROTEIN; 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; Reference proteome; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..363 FT /note="Ribosomal RNA large subunit methyltransferase M" FT /id="PRO_0000070406" FT ACT_SITE 313 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" FT BINDING 194 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" FT BINDING 227..230 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" FT BINDING 246 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" FT BINDING 266 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" FT BINDING 284 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01551" SQ SEQUENCE 363 AA; 41563 MW; DC7B76D1B192D524 CRC64; MNKLALYCRP GFEKEVAAEI TDQASHLGVF GFARVQDNSG YVIFECYQPD EADRLARDIP FNRLIFARQM MVISDLLEDL DPADRISPIV VAFEELSQQV NFAQSSELFV ETADTNEAKE LSTFCRKFTV PLRQALKKQG WLSAKASQKC GQFLHCFFVK PNCCYVGYSY VDNHSSHFMG IPRLKFPADA PSRSTLKLEE AILTFIPRKE ENKRLNENMI GVDLGACPGG WTYQLVKRGL FVYAVDHGKM AASLHDTGRI EHCAEDGFKF QPPKRKKVDW LVCDMVEQPS RISLLIGKWL LNGWCRETIF NLKLPMKKRY QEVILCLENL AVMLAEQNLN FDIQAKHLYH DREEITVHIA LKP //