TRMJ_SHIF8
ID TRMJ_SHIF8 Reviewed; 246 AA.
AC Q0T1Y7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=SFV_2580;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF04678.1; -; Genomic_DNA.
DR RefSeq; WP_000940019.1; NC_008258.1.
DR AlphaFoldDB; Q0T1Y7; -.
DR SMR; Q0T1Y7; -.
DR EnsemblBacteria; ABF04678; ABF04678; SFV_2580.
DR GeneID; 58390231; -.
DR KEGG; sfv:SFV_2580; -.
DR HOGENOM; CLU_056931_0_1_6; -.
DR OMA; PIMNLSH; -.
DR BioCyc; SFLE373384:SFV_RS14350-MON; -.
DR Proteomes; UP000000659; 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_0000313863"
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
