ID B2FLW3_STRMK Unreviewed; 192 AA.
AC B2FLW3;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase D {ECO:0000256|ARBA:ARBA00013682, ECO:0000256|PIRNR:PIRNR004553};
DE EC=2.1.1.171 {ECO:0000256|ARBA:ARBA00012141, ECO:0000256|PIRNR:PIRNR004553};
GN OrderedLocusNames=Smlt1810 {ECO:0000313|EMBL:CAQ45331.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45331.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ45331.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ45331.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- FUNCTION: Specifically methylates the guanine in position 966 of 16S
CC rRNA in the assembled 30S particle. {ECO:0000256|ARBA:ARBA00002649,
CC ECO:0000256|PIRNR:PIRNR004553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(966) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(966) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23548, Rhea:RHEA-COMP:10211, Rhea:RHEA-COMP:10212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.171;
CC Evidence={ECO:0000256|ARBA:ARBA00000252,
CC ECO:0000256|PIRNR:PIRNR004553};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmD family.
CC {ECO:0000256|ARBA:ARBA00005269, ECO:0000256|PIRNR:PIRNR004553}.
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DR EMBL; AM743169; CAQ45331.1; -; Genomic_DNA.
DR RefSeq; WP_012479777.1; NC_010943.1.
DR AlphaFoldDB; B2FLW3; -.
DR EnsemblBacteria; CAQ45331; CAQ45331; Smlt1810.
DR KEGG; sml:Smlt1810; -.
DR PATRIC; fig|522373.3.peg.1732; -.
DR eggNOG; COG0742; Bacteria.
DR HOGENOM; CLU_075826_2_1_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0052913; F:16S rRNA (guanine(966)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004398; RNA_MeTrfase_RsmD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00095; 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; 1.
DR PANTHER; PTHR43542; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR43542:SF1; METHYLTRANSFERASE; 1.
DR Pfam; PF03602; Cons_hypoth95; 1.
DR PIRSF; PIRSF004553; CHP00095; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PIRNR:PIRNR004553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW rRNA processing {ECO:0000256|PIRNR:PIRNR004553};
KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR004553};
KW Transferase {ECO:0000256|PIRNR:PIRNR004553}.
SQ SEQUENCE 192 AA; 20877 MW; F53ED7B01A2BC272 CRC64;
MSGRGSNDGQ VRIIGGRWRN TRLPVPTLPG LRPSSDRVRE TLFNWLMPRL GGARVLDLFA
GSGALGLEAV SRGAAHATLV ERDAQLGRNL TAAVAKLQAA DQITVVQADA LRWLQGAPAQ
QADLVFVDPP FADGLWQDVL AQLPRHLAAD AWLYLESPAG HVPVLPPDWL LHREGGTREV
RFALYRRATA TL
//
