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RSMJ_PASMU
ID   RSMJ_PASMU              Reviewed;         252 AA.
AC   Q9CK31;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase J {ECO:0000255|HAMAP-Rule:MF_01523};
DE            EC=2.1.1.242 {ECO:0000255|HAMAP-Rule:MF_01523};
DE   AltName: Full=16S rRNA m2G1516 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01523};
GN   Name=rsmJ {ECO:0000255|HAMAP-Rule:MF_01523}; OrderedLocusNames=PM1804;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Specifically methylates the guanosine in position 1516 of 16S
CC       rRNA. {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43220, Rhea:RHEA-COMP:10412, Rhea:RHEA-COMP:10413,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.242;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01523};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01523}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmJ family.
CC       {ECO:0000255|HAMAP-Rule:MF_01523}.
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DR   EMBL; AE004439; AAK03888.1; -; Genomic_DNA.
DR   RefSeq; WP_010907347.1; NC_002663.1.
DR   AlphaFoldDB; Q9CK31; -.
DR   SMR; Q9CK31; -.
DR   STRING; 747.DR93_132; -.
DR   PRIDE; Q9CK31; -.
DR   EnsemblBacteria; AAK03888; AAK03888; PM1804.
DR   KEGG; pmu:PM1804; -.
DR   HOGENOM; CLU_076324_0_0_6; -.
DR   OMA; SRYDIYP; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01523; 16SrRNA_methyltr_J; 1.
DR   InterPro; IPR007536; 16SrRNA_methylTrfase_J.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR36112; PTHR36112; 1.
DR   Pfam; PF04445; SAM_MT; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..252
FT                   /note="Ribosomal RNA small subunit methyltransferase J"
FT                   /id="PRO_0000212080"
FT   BINDING         105..106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         121..122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         175
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ   SEQUENCE   252 AA;  28006 MW;  08098F96B59C4B50 CRC64;
     MNIQLICETE NPEKFTALCT QYGLVHDPES YLALVQTYDE QGQVRLELRK LDEAKLGAVF
     VDFVAGAMAH RRKFGGGRGE AVAKAVGIKS GYLPTVIDAT AGLGRDAFVL ASIGCRVRLV
     ERHPVVRLLL QDGLQRAYAD SEIGEMLQQN MQLLPVSHIA QLNPALDCVD VVYLDPMYPH
     KPKSALVKKE MRVFQHLVGA DLDADNLLEP ALALANKRVV VKRPDYAPFL AQQSPHFSRE
     TKNHRFDIYL TG
 
 
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