ID   RLMM_HAES1              Reviewed;         361 AA.
AC   Q0I256;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=HS_0496;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI24773.1; -; Genomic_DNA.
DR   RefSeq; WP_011608653.1; NC_008309.1.
DR   AlphaFoldDB; Q0I256; -.
DR   SMR; Q0I256; -.
DR   STRING; 205914.HS_0496; -.
DR   EnsemblBacteria; ABI24773; ABI24773; HS_0496.
DR   KEGG; hso:HS_0496; -.
DR   eggNOG; COG2933; Bacteria.
DR   HOGENOM; CLU_043780_0_0_6; -.
DR   OMA; PVDWMVC; -.
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; 3.40.50.150; -; 1.
DR   HAMAP; MF_01551; 23SrRNA_methyltr_M; 1.
DR   InterPro; IPR040739; RlmM_FDX.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR011224; rRNA_MeTrfase_M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF18125; RlmM_FDX; 1.
DR   PIRSF; PIRSF028774; UCP028774; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..361
FT                   /note="Ribosomal RNA large subunit methyltransferase M"
FT                   /id="PRO_0000314518"
FT   ACT_SITE        312
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         226..229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         245
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01551"
SQ   SEQUENCE   361 AA;  41837 MW;  D1D583C7A2DF6025 CRC64;
     MNKLALYCRS GFEKELAAEI TEKATALGVF GFARVVENSG YVIFECYQIG EADLLARKIT
     FSQLIFARQL IVVSDLISNL SVQDRISPII EYYRQQEKIL NLKQSSDIWV ETADTNEAKT
     LAAFCRKFTV PLRQALRKQG WLQAKNKKSG ITLHIFFTQS NSCYIGYSYN NNHAEHIMGI
     PRLKFPAEAP SRSTLKLEEA ILYFIPPNQE ATRFNENKYA VDLGACPGGW TYQLVRRGVF
     VYAVDHGKMA TSLHETGRIE HCAEDGFKFR PPKHCKIDWL VCDMVEQPRR IADLISQWLV
     KGWCKETIFN LKLPMKKRYF EVQQCLRQIE DKLNKQNISF QLQAKHLYHD REEITVYIRL
     M