ID A0A1Y3P2V4_9PSED Unreviewed; 355 AA.
AC A0A1Y3P2V4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AUC60_10030 {ECO:0000313|EMBL:OUM74148.1};
OS Pseudomonas caspiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1451454 {ECO:0000313|EMBL:OUM74148.1, ECO:0000313|Proteomes:UP000195440};
RN [1] {ECO:0000313|EMBL:OUM74148.1, ECO:0000313|Proteomes:UP000195440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBF102 {ECO:0000313|EMBL:OUM74148.1,
RC ECO:0000313|Proteomes:UP000195440};
RX PubMed=28552245; DOI=10.1016/j.syapm.2017.04.002;
RA Busquets A., Gomila M., Beiki F., Mulet M., Rahimian H., Garcia-Valdes E.,
RA Lalucat J.;
RT "Pseudomonas caspiana sp. nov., a citrus pathogen in the Pseudomonas
RT syringae phylogenetic group.";
RL Syst. Appl. Microbiol. 40:266-273(2017).
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:OUM74148.1}.
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DR EMBL; LOHF01000006; OUM74148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3P2V4; -.
DR OrthoDB; 154490at2; -.
DR Proteomes; UP000195440; 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};
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 82..157
FT /note="Ribosomal RNA large subunit methyltransferase M
FT THUMP-like"
FT /evidence="ECO:0000259|Pfam:PF21239"
FT DOMAIN 181..274
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT ECO:0000256|PIRSR:PIRSR028774-1"
FT BINDING 183
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 216..219
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 235
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 255
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 271
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 355 AA; 40221 MW; 9FE51D2BD525B8F6 CRC64;
MNTLFMHCRP GFEGEVCSEI AEHAARLNVS GYAKAKPNTA FAEFVCTEDD GAERLMNGQR
FSKLIFPRQW ARGVFLELPE TDRISVILAH MATFVTCGSL WLEVVDTNDG KELSTFCRKF
EAPLRKALIQ AGKLVDDPRK PRLLLTFKSG REVFLGLADA DNSAMWPMGI PRLKFPREAP
SRSTLKLEEA WHHFIPRDQW DERLSGDMTG VDLGAAPGGW TYQLVRRGML VTAIDNGPMA
ESLMDTGLVQ HLMADGFTYK PRQPVDWMVC DIVEKPARNA ALLETWLGEG LCREAVVNLK
LPMKQRYAEV SRLLQRIEEG FEVRGIRVEI GCKQLYHDRE EVTCHLRRLD GKRKG
//
