TRMJ_METJA
ID TRMJ_METJA Reviewed; 230 AA.
AC Q58871;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=tRNA (cytidine-2'-O-)-methyltransferase TrmJ {ECO:0000250|UniProtKB:Q4JB16};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q4JB16};
DE AltName: Full=tRNA (cytidine(32)-2'-O)-methyltransferase {ECO:0000250|UniProtKB:Q4JB16};
DE AltName: Full=tRNA Cm32 methyltransferase {ECO:0000250|UniProtKB:Q4JB16};
GN Name=trmJ {ECO:0000250|UniProtKB:Q4JB16}; OrderedLocusNames=MJ1476;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at
CC position 32 in tRNA. {ECO:0000250|UniProtKB:Q4JB16}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q4JB16};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4JB16}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q4JB16}.
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; L77117; AAB99481.1; -; Genomic_DNA.
DR PIR; C64484; C64484.
DR AlphaFoldDB; Q58871; -.
DR SMR; Q58871; -.
DR STRING; 243232.MJ_1476; -.
DR EnsemblBacteria; AAB99481; AAB99481; MJ_1476.
DR KEGG; mja:MJ_1476; -.
DR eggNOG; arCOG01018; Archaea.
DR HOGENOM; CLU_056931_3_0_2; -.
DR InParanoid; Q58871; -.
DR OMA; PIMNLSH; -.
DR PhylomeDB; Q58871; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..230
FT /note="tRNA (cytidine-2'-O-)-methyltransferase TrmJ"
FT /id="PRO_0000159843"
FT BINDING 79..81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4JB16"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4JB16"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4JB16"
FT BINDING 142..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q4JB16"
SQ SEQUENCE 230 AA; 26280 MW; E9B6B9B31B3A146E CRC64;
MIIMISVILV NPKYSGNVGS IARVMMNFGF EELRIVGDKS IINNEAYMMA VHAREILDNA
KFYNTFDEAI GDLDFVIATS GARGGDRNLK RVPITPKELA DKILEVKGNI GIVFGREDDG
LRNEEIDKCD LLVSIPTSEK YPIMNLSHAV AVILYEIYTK KVRNKFLDIN MREASKEDKE
LLIRKFNEFI DKNEKIPEHK KELCKIIFKR LVNRAFISGK EAWTLMSAFK
