ID Q31ST5_SHIBS Unreviewed; 228 AA.
AC Q31ST5;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000256|RuleBase:RU362024};
DE EC=2.1.1.200 {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000256|RuleBase:RU362024};
GN Name=lasT {ECO:0000313|EMBL:ABB68873.1};
GN Synonyms=trmJ {ECO:0000256|RuleBase:RU362024};
GN OrderedLocusNames=SBO_4466 {ECO:0000313|EMBL:ABB68873.1};
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB68873.1, ECO:0000313|Proteomes:UP000007067};
RN [1] {ECO:0000313|EMBL:ABB68873.1, ECO:0000313|Proteomes:UP000007067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227 {ECO:0000313|EMBL:ABB68873.1,
RC ECO:0000313|Proteomes:UP000007067};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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|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|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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000036; ABB68873.1; -; Genomic_DNA.
DR RefSeq; WP_001223173.1; NC_007613.1.
DR AlphaFoldDB; Q31ST5; -.
DR KEGG; sbo:SBO_4466; -.
DR HOGENOM; CLU_056931_3_1_6; -.
DR Proteomes; UP000007067; 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; 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:SF1; 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 S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT DOMAIN 3..153
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
SQ SEQUENCE 228 AA; 25375 MW; 5EB3F2C70A37DBBE CRC64;
MRITIILVAP ARAENIGAAA RAMKTMGFSE LRIVDSQAHL EPATRWVAHG SGDIIDNIKV
FPTLVESLHD VDFTVATTAR SRAKYHYYAT PVELVLLLEE KSSWMSHAAL VFGREDSGLT
NEELALADVL TGVPMVADYP SLNLGQAVMV YCYQLATLIQ QPTKSDTTAD QHQLQALRER
VMALLTTLAV ADDIKLVDWL QQRLGLLEQR DTAMLHRLLH DIEKNITK
//
