TRM56_THEPD
ID TRM56_THEPD Reviewed; 181 AA.
AC A1RY31;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=tRNA (cytidine(56)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00077};
DE EC=2.1.1.206 {ECO:0000255|HAMAP-Rule:MF_00077};
DE AltName: Full=tRNA ribose 2'-O-methyltransferase aTrm56 {ECO:0000255|HAMAP-Rule:MF_00077};
GN OrderedLocusNames=Tpen_0709;
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5;
RX PubMed=18263724; DOI=10.1128/jb.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
CC -!- FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose
CC methylation of cytidine at position 56 in tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_00077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42968, Rhea:RHEA-COMP:10308, Rhea:RHEA-COMP:10309,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.206;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00077};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00077}.
CC -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000255|HAMAP-
CC Rule:MF_00077}.
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DR EMBL; CP000505; ABL78111.1; -; Genomic_DNA.
DR RefSeq; WP_011752376.1; NC_008698.1.
DR AlphaFoldDB; A1RY31; -.
DR SMR; A1RY31; -.
DR STRING; 368408.Tpen_0709; -.
DR PRIDE; A1RY31; -.
DR EnsemblBacteria; ABL78111; ABL78111; Tpen_0709.
DR GeneID; 4601590; -.
DR KEGG; tpe:Tpen_0709; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_123709_0_0_2; -.
DR OMA; VVHLTMY; -.
DR OrthoDB; 83050at2157; -.
DR Proteomes; UP000000641; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00077; tRNA_methyltr_aTrm56; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR002845; tRNA_mtfrase_aTrm56.
DR PANTHER; PTHR42197; PTHR42197; 1.
DR Pfam; PF01994; Trm56; 1.
DR PIRSF; PIRSF016123; UCP016123; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..181
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000365323"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT BINDING 115..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT BINDING 133..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ SEQUENCE 181 AA; 20308 MW; E8AAE2CA9CF4DEEB CRC64;
MSTGRRVFVL RIGHRPVRDH RVTTHVGLVA RAFGADGIFL EESVEESVIR TLRNVVENWG
GDFKVLTTRD PRETVANWKK NGGIVVHLTM YGENISEELI NLISGQGKDI LVVVGGEKVP
RWLFEEADFN VAIGNQPHSE VAALAVFLDR LFKGEELRRE FPGAKLSIIP SKRGKIVVRR
E