ID   RLMM_AGGAN              Reviewed;         362 AA.
AC   C6ANQ9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=NT05HA_1104;
OS   Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=634176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJ8700;
RX   PubMed=19447908; DOI=10.1128/jb.00447-09;
RA   Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H.,
RA   Fine D.H., Kaplan J.B., Planet P.J.;
RT   "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus
RT   NJ8700.";
RL   J. Bacteriol. 191:4693-4694(2009).
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; CP001607; ACS97470.1; -; Genomic_DNA.
DR   RefSeq; WP_005700839.1; NZ_CP009230.1.
DR   AlphaFoldDB; C6ANQ9; -.
DR   SMR; C6ANQ9; -.
DR   PRIDE; C6ANQ9; -.
DR   KEGG; aap:NT05HA_1104; -.
DR   PATRIC; fig|634176.19.peg.1058; -.
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..362
FT                   /note="Ribosomal RNA large subunit methyltransferase M"
FT                   /id="PRO_0000388978"
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   362 AA;  42044 MW;  E34EC8A4656EB5C1 CRC64;
     MNKLALYCRM GFEREMAAEI TDKAAEKGVF GFVRVIENSG YVIFECYQAD EADYLARELD
     FQQLIFARQM LVVSDLLTDL PQQDRITPIV QQYQQIADKI DLKQSTELLV ETADTNEAKE
     LLGFCRKFTV PLRQTLKKQG WLRASNHAKC GLFLHLFFLR NNACYVGYSY NHNHSAHLMG
     IQRLKFPADA PSRSTLKLEE AILTFIPRQK ETEWLNENQY AVDLGACPGG WTYQLVKRGL
     FVYAVDHGKM AASLHETGRI EHCAEDGFKF QPPKRQKIDW LVCDMVEKPS RIAELMTKWL
     LNGWCHSMIF NLKLPMKKRY AEVQQCLQYI ADKLTQRGLA FQLKAKHLYH DREEITVYLR
     LL