RLMM_HAEIG
ID RLMM_HAEIG Reviewed; 363 AA.
AC A5UIV9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, 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};
GN OrderedLocusNames=CGSHiGG_09685;
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG;
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(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; CP000672; ABR00715.1; -; Genomic_DNA.
DR RefSeq; WP_012055449.1; NC_009567.1.
DR AlphaFoldDB; A5UIV9; -.
DR SMR; A5UIV9; -.
DR EnsemblBacteria; ABR00715; ABR00715; CGSHiGG_09685.
DR KEGG; hiq:CGSHiGG_09685; -.
DR HOGENOM; CLU_043780_0_0_6; -.
DR OMA; PVDWMVC; -.
DR Proteomes; UP000001990; 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; 3.40.50.150; -; 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..363
FT /note="Ribosomal RNA large subunit methyltransferase M"
FT /id="PRO_0000314517"
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; 41532 MW; 997FC949DCB99724 CRC64;
MNKLALYCRP GFEKEVAAEI TDQASHLGVF GFARVQDNSG YVIFECYQPD EADRLARDIP
FNRLIFARQM IVISDLLEDL DPADRISPIV AAFEELSQQV NFAQSSELFV ETADTNEAKE
LSTFCRKFTV PLRQALKKQG WLSAKASQKC GQFLHCFFVK PNCCYVGYSY VDNHSSHFMG
IPRLKFPADA PSRSTLKLEE AILTFIPRKE ENKRLNENMI GVDLGACPGG WTYQLVKRGL
FVYAVDHGKM AANLHDTGRI EHCAEDGFKF QPPKRKKVDW LVCDMVEQPS RISSLIGKWL
LNGWCRETIF NLKLPMKKRY QEVILCLENL AVMLAEQNLN FEIQAKHLYH DREEITVHIA
LKP