ID F6AIS6_PSEF1 Unreviewed; 351 AA.
AC F6AIS6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=Psefu_2847 {ECO:0000313|EMBL:AEF22811.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22811.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF22811.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002727; AEF22811.1; -; Genomic_DNA.
DR RefSeq; WP_013791938.1; NC_015556.1.
DR AlphaFoldDB; F6AIS6; -.
DR STRING; 743720.Psefu_2847; -.
DR KEGG; pfv:Psefu_2847; -.
DR eggNOG; COG2933; Bacteria.
DR HOGENOM; CLU_043780_0_0_6; -.
DR OrthoDB; 154490at2; -.
DR Proteomes; UP000000686; 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; 3.30.2300.20; -; 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:UP000000686};
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..273
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 351 AA; 39456 MW; D0EA1F183A1546E6 CRC64;
MKTLLLHCRP GFENEVCSEI SEHAARLEVP GYAKAKPDTA CAEFICSDEA GAERLMAGLR
FSQLIFIRQW ARGTFIELPE KDRISVLLEH MAPLPTFGSL WLEVFDTNDG KELSGFCKKF
EGPLRKALTG AGKLAENARA PRLLLTFKSG REVFLGMAAP NNSAIWPMGI PRLKFPREAP
SRSTLKLEEA WHTFIPREQW DERLSDEMTG VDLGAAPGGW TYQLVRRGML VTAIDNGPMA
ESLMDTGLVK HLMVDGFTWK PKQPVDWMVC DIVEKPARSA ALLEAWIGEG HCREAVVNLK
LPMKQRYAEV QRLLERIAEG LAARKVKASI ACKQLYHDRE EVTCHLRRLS K
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