ID   TRMJ_ECOUT              Reviewed;         246 AA.
AC   Q1R8K0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=UTI89_C2854;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08314.1; -; Genomic_DNA.
DR   RefSeq; WP_000940019.1; NC_007946.1.
DR   AlphaFoldDB; Q1R8K0; -.
DR   SMR; Q1R8K0; -.
DR   EnsemblBacteria; ABE08314; ABE08314; UTI89_C2854.
DR   GeneID; 58390231; -.
DR   KEGG; eci:UTI89_C2854; -.
DR   HOGENOM; CLU_056931_0_1_6; -.
DR   OMA; PIMNLSH; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..246
FT                   /note="tRNA (cytidine/uridine-2'-O-)-methyltransferase
FT                   TrmJ"
FT                   /id="PRO_0000313854"
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   246 AA;  27048 MW;  83C1AE4507E097D2 CRC64;
     MLQNIRIVLV ETSHTGNMGS VARAMKTMGL TNLWLVNPLV KPDSQAIALA AGASDVIGNA
     HIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LDPRECGLKS VAEAANTPVA LVFGRERVGL
     TNEELQKCHY HVAIAANPEY SSLNLAMAVQ VIAYEVRMAW LATQENGEQV EHEETPYPLV
     DDLERFYGHL EQTLLATGFI RENHPGQVMN KLRRLFTRAR PESQELNILR GILASIEQQN
     KGNKAE