ID A0A0L7SWL7_9GAMM Unreviewed; 367 AA.
AC A0A0L7SWL7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase M {ECO:0000256|HAMAP-Rule:MF_01551};
DE EC=2.1.1.186 {ECO:0000256|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA (cytidine2498-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01551};
DE AltName: Full=23S rRNA 2'-O-ribose methyltransferase RlmM {ECO:0000256|HAMAP-Rule:MF_01551};
GN Name=rlmM {ECO:0000256|HAMAP-Rule:MF_01551};
GN ORFNames=NG42_11680 {ECO:0000313|EMBL:KOC89785.1}, NG43_21375
GN {ECO:0000313|EMBL:KOC87537.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC87537.1, ECO:0000313|Proteomes:UP000036851};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC89785.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC87537.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S
CC rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01551};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01551}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01551}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOC87537.1}.
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DR EMBL; JRXF01000065; KOC87537.1; -; Genomic_DNA.
DR EMBL; JRXE01000014; KOC89785.1; -; Genomic_DNA.
DR RefSeq; WP_052899523.1; NZ_JRXF01000065.1.
DR AlphaFoldDB; A0A0L7SWL7; -.
DR STRING; 1560201.NG42_11680; -.
DR PATRIC; fig|1560201.3.peg.2482; -.
DR OrthoDB; 154490at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01551};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01551}; Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01551};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01551};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01551}.
FT DOMAIN 1..70
FT /note="RlmM ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18125"
FT DOMAIN 84..164
FT /note="Ribosomal RNA large subunit methyltransferase M
FT THUMP-like"
FT /evidence="ECO:0000259|Pfam:PF21239"
FT DOMAIN 186..279
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 306
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-1"
FT BINDING 188
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-2"
FT BINDING 221..224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-2"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-2"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-2"
FT BINDING 277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-2"
SQ SEQUENCE 367 AA; 42143 MW; 8D0C6519BF72E0D8 CRC64;
MNKVLLYCRQ GFEKECAAEI TDKATQREVF GFARVKEDSG YVLFECYQHE DADKLVRELP
FSELIFARQM VVVGELLRDL PPEDRVSPVV GMLTGVVEKG GELRVEVPDT NASKELLKFC
RKFTVPLRAS LRSSNILLNY ESAKRPVVHV FFIAPGCCYV GYSYPDNNST FFMGIPRLKF
PSDAPSRSTL KLEEAFHVFI PADEWDERLA SGMYAVDLGA CPGGWTYQLV QRSMMVDAID
NGPMAPSLMD TGQVTHHRED GFKYRPTRTN IYWLVCDMVE KPVRVANLMT EWLVNGWCRE
AIFNLKLPMK KRYEEVSQNL AMMQEKLKAN GINAQINARQ LYHDREEVTV HVRRIWSATP
GRRDERY
//
