ID B7UGX8_ECO27 Unreviewed; 246 AA.
AC B7UGX8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000256|ARBA:ARBA00013781, ECO:0000256|RuleBase:RU362024};
DE EC=2.1.1.200 {ECO:0000256|ARBA:ARBA00012626, ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000256|ARBA:ARBA00031634, ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000256|ARBA:ARBA00032381, ECO:0000256|RuleBase:RU362024};
GN Name=trmJ {ECO:0000256|RuleBase:RU362024,
GN ECO:0000313|EMBL:CAS10363.1};
GN OrderedLocusNames=E2348C_2815 {ECO:0000313|EMBL:CAS10363.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS10363.1, ECO:0000313|Proteomes:UP000008205};
RN [1] {ECO:0000313|EMBL:CAS10363.1, ECO:0000313|Proteomes:UP000008205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
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:0000256|RuleBase:RU362024}.
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:0000256|ARBA:ARBA00000240,
CC ECO:0000256|RuleBase:RU362024};
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:0000256|ARBA:ARBA00000470,
CC ECO:0000256|RuleBase:RU362024};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362024}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000256|ARBA:ARBA00007228}.
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DR EMBL; FM180568; CAS10363.1; -; Genomic_DNA.
DR RefSeq; WP_000940019.1; NC_011601.1.
DR AlphaFoldDB; B7UGX8; -.
DR SMR; B7UGX8; -.
DR GeneID; 83579917; -.
DR KEGG; ecg:E2348C_2815; -.
DR HOGENOM; CLU_056931_0_1_6; -.
DR Proteomes; UP000008205; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18093; SpoU-like_TrmJ; 1.
DR Gene3D; 1.10.8.590; -; 1.
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 NCBIfam; TIGR00050; rRNA_methyl_1; 1.
DR PANTHER; PTHR42786:SF2; TRNA (CYTIDINE_URIDINE-2'-O-)-METHYLTRANSFERASE TRMJ; 1.
DR PANTHER; PTHR42786; TRNA/RRNA METHYLTRANSFERASE; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF004808; LasT; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362024};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU362024};
KW Reference proteome {ECO:0000313|Proteomes:UP000008205};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAS10363.1};
KW tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT DOMAIN 5..154
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
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
//
