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Database: UniProt
Entry: A0A0F4QFV3_9GAMM
LinkDB: A0A0F4QFV3_9GAMM
Original site: A0A0F4QFV3_9GAMM 
ID   A0A0F4QFV3_9GAMM        Unreviewed;       361 AA.
AC   A0A0F4QFV3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=TW77_19240 {ECO:0000313|EMBL:KJZ06461.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ06461.1, ECO:0000313|Proteomes:UP000033452};
RN   [1] {ECO:0000313|EMBL:KJZ06461.1, ECO:0000313|Proteomes:UP000033452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2471 {ECO:0000313|EMBL:KJZ06461.1,
RC   ECO:0000313|Proteomes:UP000033452};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(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:KJZ06461.1}.
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DR   EMBL; JXYA01000049; KJZ06461.1; -; Genomic_DNA.
DR   RefSeq; WP_046006602.1; NZ_JXYA01000049.1.
DR   AlphaFoldDB; A0A0F4QFV3; -.
DR   PATRIC; fig|43658.5.peg.4063; -.
DR   OrthoDB; 154490at2; -.
DR   Proteomes; UP000033452; 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:UP000033452};
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          83..162
FT                   /note="Ribosomal RNA large subunit methyltransferase M
FT                   THUMP-like"
FT                   /evidence="ECO:0000259|Pfam:PF21239"
FT   DOMAIN          184..278
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   ACT_SITE        304
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01551,
FT                   ECO:0000256|PIRSR:PIRSR028774-1"
FT   BINDING         186
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         219..222
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         238
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         258
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         275
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   361 AA;  41061 MW;  EEB678E7322F2343 CRC64;
     MSSVVIYCRS GFESDAAAEI THHAALHNVA GYVKAKPNTG YVTFECFDPA QSELLLKQVD
     FSSLVFARQW FAGVLLSKMP VEDRVSEIKQ VVGGFPLCGD LRVETPDTNE GKELSKFCKK
     FSTPLAKALE KQNKLTRDHK AHKPVLHVLF LANDTAYVGY SFSHNNSPFF MGIPRLKMPA
     DAPSRSTLKL DEAFNVFVGK ENEPERVRSG MRGVDLGACP GGWTYQLVRR GLFVAAIDNG
     PMNDDLMETG QVKHFREDGF KYRPEKRNID WLVCDMVEKP TRVSELMVDW IVNGFVRELI
     FNLKLPMKKR FDTVYECLTL IRDELKKYGV GYELQAKHLY HDREEVTVHI QVLKVPQNLY
     S
//
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