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Database: UniProt
Entry: Q66FW5_YERPS
LinkDB: Q66FW5_YERPS
Original site: Q66FW5_YERPS 
ID   Q66FW5_YERPS            Unreviewed;       220 AA.
AC   Q66FW5;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
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=YPTB0220 {ECO:0000313|EMBL:CAH19460.1};
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH19460.1, ECO:0000313|Proteomes:UP000001011};
RN   [1] {ECO:0000313|EMBL:CAH19460.1, ECO:0000313|Proteomes:UP000001011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19460.1; -; Genomic_DNA.
DR   RefSeq; WP_011191520.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66FW5; -.
DR   GeneID; 66843375; -.
DR   KEGG; ypo:BZ17_2363; -.
DR   KEGG; yps:YPTB0220; -.
DR   PATRIC; fig|273123.14.peg.2485; -.
DR   Proteomes; UP000001011; 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   rRNA processing {ECO:0000256|PIRNR:PIRNR004553};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR004553};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004553}.
SQ   SEQUENCE   220 AA;  24381 MW;  0F114596A4720A0C CRC64;
     MAKQPIAKRS IVKKASPQSA GQIRIIGGKW RGRKLPVPDS PGLRPTTDRV RETLFNWLAP
     MIQGARCLDC FAGSGALGLE ALSRYASETT LLEADRQVAK QLSDNLTLLK AENGQVVNTN
     SLQWLAQPGQ PFNLVFLDPP FRKGLLAETI NLLEQFNWLA ADAWIYVEAE AESAVADVPA
     NWLLHREKIA GQVAYRLFIR QQTDLPACTS VAEQEQHHVD
//
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