ID A0A1Q6CIT4_9GAMM Unreviewed; 358 AA.
AC A0A1Q6CIT4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BI291_12055 {ECO:0000313|EMBL:OKY26313.1};
OS Thalassotalea sp. PP2-459.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1742724 {ECO:0000313|EMBL:OKY26313.1, ECO:0000313|Proteomes:UP000186791};
RN [1] {ECO:0000313|EMBL:OKY26313.1, ECO:0000313|Proteomes:UP000186791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PP2-459 {ECO:0000313|EMBL:OKY26313.1,
RC ECO:0000313|Proteomes:UP000186791};
RA Barja J.L., Dubert J.;
RT "Draft genome of the tyrosinase inhibitors producing Thalassotalea sp. PP2-
RT 459.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKY26313.1}.
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DR EMBL; MKQD01000038; OKY26313.1; -; Genomic_DNA.
DR RefSeq; WP_074498360.1; NZ_MKQD01000038.1.
DR AlphaFoldDB; A0A1Q6CIT4; -.
DR STRING; 1742724.BI291_12055; -.
DR OrthoDB; 154490at2; -.
DR Proteomes; UP000186791; 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:UP000186791};
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..71
FT /note="RlmM ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF18125"
FT DOMAIN 85..162
FT /note="Ribosomal RNA large subunit methyltransferase M
FT THUMP-like"
FT /evidence="ECO:0000259|Pfam:PF21239"
FT DOMAIN 185..278
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-1"
FT BINDING 187
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 220..223
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 239
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 259
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 276
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 358 AA; 41059 MW; 8D23DF3648E12B0F CRC64;
MTAIVLYCRP GFEKECGAEI QEKAAWNEIY GYLQLKKNQG IVFFHLNNAD EGERLIAKLP
LKRLIFARQW FVSLTDTIEL PEYNRVEAII EHLGHEWQYA DLRMETPDTN DGKALSKFCR
KLGVPLRQGL RAKKMLAPKG QHDGAVLHAL FFSGSEVILG YSLGTNTSPH LMGIPRLKFP
SQAPSRSTLK LDEAFLYFIP KDEWPTRLTS GMNAVDLGAA PGGWTYQLVR RGMMVTSIDN
GPMAESLMDT GQVKHRMIDG FKFTPAKQNV YWLVCDMIEK PQRVAKLMAE WLLRGDCKEA
MFNLKLPMKG RYQQVQDDLQ LIKDMFSEHQ VKYELYAKHL YYDREEITVH ARLLSPPL
//
