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RSMJ_HAHCH
ID   RSMJ_HAHCH              Reviewed;         263 AA.
AC   Q2SL17;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=HCH_01818;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC28657.1; -; Genomic_DNA.
DR   RefSeq; WP_011395729.1; NC_007645.1.
DR   AlphaFoldDB; Q2SL17; -.
DR   SMR; Q2SL17; -.
DR   STRING; 349521.HCH_01818; -.
DR   PRIDE; Q2SL17; -.
DR   EnsemblBacteria; ABC28657; ABC28657; HCH_01818.
DR   KEGG; hch:HCH_01818; -.
DR   eggNOG; COG0500; Bacteria.
DR   HOGENOM; CLU_076324_0_1_6; -.
DR   OMA; SRYDIYP; -.
DR   OrthoDB; 1696461at2; -.
DR   Proteomes; UP000000238; 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..263
FT                   /note="Ribosomal RNA small subunit methyltransferase J"
FT                   /id="PRO_0000244273"
FT   BINDING         115..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         131..132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ   SEQUENCE   263 AA;  28820 MW;  F75C5ACC28E99826 CRC64;
     MISYDDQVLV SYSNQRWEEA EAFSSQFGLR LVALEALPAK SDRAVYLLNF SDTRVELVNW
     REQAPGPVFV DFVEGALAYR REHGGGRGEM VAKSVGLKGE VKCLNVLDAT AGLGRDAYVL
     AALGCHVVMY ERNPLVHALL ADGLRRALEC ADAASVVSRM TLHLGEAFNT FPDGIDVVYL
     DPMFPERRKS SAVKKEMQAF KDIVGADPDA DELLAAALRQ EVKRIVVKRP KGAPCLLGRE
     PSFTVTGKSG RFDVYALRKL TGG
 
 
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