ID   TRMJ_YERPA              Reviewed;         257 AA.
AC   Q1C5G8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-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=YPA_2339;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG14304.1; -; Genomic_DNA.
DR   RefSeq; WP_002217034.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C5G8; -.
DR   SMR; Q1C5G8; -.
DR   EnsemblBacteria; ABG14304; ABG14304; YPA_2339.
DR   GeneID; 66844717; -.
DR   KEGG; ypa:YPA_2339; -.
DR   OMA; PIMNLSH; -.
DR   Proteomes; UP000001971; 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..257
FT                   /note="tRNA (cytidine/uridine-2'-O-)-methyltransferase
FT                   TrmJ"
FT                   /id="PRO_0000313868"
FT   REGION          238..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   257 AA;  28385 MW;  0488FFF12B7AA9F4 CRC64;
     MLHNIRIVLV ETSHTGNMGS TARAMKTMGL TNLYLVNPLV KPDSQAIALS AGASDVIGKA
     TIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LEPRECGVRS AREAEHAPVA LVFGRERVGL
     TNDELQKCHY HVAIPANPEY SSLNLAMAVQ ILAYEVRVAY LDRQQANAPV EEEEEAPYPL
     VDDLERFYQH LEQVLSHSGF IRQAHPGQIM SKLRRLFTRA RPEAQELNIL RGMLTSIEKQ
     DKYPQRGTGD TAGKSKD