ID   TRMJ_SALTY              Reviewed;         243 AA.
AC   P66974; Q8XEM9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000250|UniProtKB:P0AE01};
DE            EC=2.1.1.200 {ECO:0000250|UniProtKB:P0AE01};
DE   AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:P0AE01};
DE   AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000250|UniProtKB:P0AE01};
GN   Name=trmJ; OrderedLocusNames=STM2545;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or
CC       2'O-methylated uridine (Um32) at position 32 in tRNA.
CC       {ECO:0000250|UniProtKB:P0AE01}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.200;
CC         Evidence={ECO:0000250|UniProtKB:P0AE01};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-
CC         methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42936, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10290,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.200;
CC         Evidence={ECO:0000250|UniProtKB:P0AE01};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AE01}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE01}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR   EMBL; AE006468; AAL21439.1; -; Genomic_DNA.
DR   RefSeq; NP_461480.1; NC_003197.2.
DR   RefSeq; WP_000940032.1; NC_003197.2.
DR   AlphaFoldDB; P66974; -.
DR   SMR; P66974; -.
DR   STRING; 99287.STM2545; -.
DR   PaxDb; P66974; -.
DR   EnsemblBacteria; AAL21439; AAL21439; STM2545.
DR   GeneID; 1254067; -.
DR   KEGG; stm:STM2545; -.
DR   PATRIC; fig|99287.12.peg.2685; -.
DR   HOGENOM; CLU_056931_0_1_6; -.
DR   OMA; PIMNLSH; -.
DR   PhylomeDB; P66974; -.
DR   BioCyc; SENT99287:STM2545-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0002128; P:tRNA nucleoside ribose methylation; IBA:GO_Central.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR42786; PTHR42786; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   PIRSF; PIRSF004808; LasT; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00050; rRNA_methyl_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..243
FT                   /note="tRNA (cytidine/uridine-2'-O-)-methyltransferase
FT                   TrmJ"
FT                   /id="PRO_0000159828"
FT   BINDING         79..81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         141..143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
SQ   SEQUENCE   243 AA;  26613 MW;  F6C608919030D096 CRC64;
     MLQNIRIVLV ETSHTGNMGS VARAMKTMGL TNLWLVNPLV KPDSQAIALA AGASDVIGNA
     QIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LDPRECGLKS VAEAANTPVA LVFGRERVGL
     TNDELQKCHY HVAIAANPEY SSLNLAMAVQ VIAYEVRMAW LATQENGDAA DHEETPYPLV
     DDLERFYGHL EQTLLSTGFI RENHPGQVMN KLRRLFTRAR PESQELNILR GILASIEQQN
     KGK