RSMJ_PSEMY
ID RSMJ_PSEMY Reviewed; 260 AA.
AC A4XXN9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=Pmen_3353;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABP86105.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000680; ABP86105.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041772950.1; NC_009439.1.
DR AlphaFoldDB; A4XXN9; -.
DR SMR; A4XXN9; -.
DR STRING; 399739.Pmen_3353; -.
DR EnsemblBacteria; ABP86105; ABP86105; Pmen_3353.
DR KEGG; pmy:Pmen_3353; -.
DR PATRIC; fig|399739.8.peg.3403; -.
DR eggNOG; COG0742; Bacteria.
DR HOGENOM; CLU_076324_0_1_6; -.
DR OMA; SRYDIYP; -.
DR OrthoDB; 1696461at2; -.
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; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..260
FT /note="Ribosomal RNA small subunit methyltransferase J"
FT /id="PRO_0000316260"
FT BINDING 108..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 124..125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01523"
SQ SEQUENCE 260 AA; 28126 MW; 8A7D72EE825C4B24 CRC64;
MTDEPRNASI RMDALQAHHA EAAARWATRL GLPRVGETDF ALQLGDQGLQ LVELGDKAPG
PVRVDFVEGA AAHRRQFGGG SGQMIAKAVG VQSGIRPRIL DATAGLGRDA FVLASLGCEM
TLIERQPLIA ALLEDGLQRA ELDLEVAPIA ARMRLLTGNA IDLMQNWQGE APQVIYLDPM
FPHRDKSALV KKEMRLFRPF VGDDLDAPAL LAAALALASH RVVVKRPRKA PAIEGTKPGY
VLEGKSSRYD VYPKKKLEGA