TRMJ_YERPN
ID TRMJ_YERPN Reviewed; 257 AA.
AC Q1CKB1; C4GRI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=YPN_1239; ORFNames=YP516_1359;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG17569.1; -; Genomic_DNA.
DR EMBL; ACNQ01000008; EEO77679.1; -; Genomic_DNA.
DR RefSeq; WP_002217034.1; NZ_ACNQ01000008.1.
DR AlphaFoldDB; Q1CKB1; -.
DR SMR; Q1CKB1; -.
DR EnsemblBacteria; ABG17569; ABG17569; YPN_1239.
DR GeneID; 66844717; -.
DR KEGG; ypn:YPN_1239; -.
DR HOGENOM; CLU_056931_0_1_6; -.
DR OMA; PIMNLSH; -.
DR Proteomes; UP000008936; 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_0000313869"
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
