ID   TRM56_HALWD             Reviewed;         193 AA.
AC   Q18HD7;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=HQ_2492A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ52605.1; -; Genomic_DNA.
DR   RefSeq; WP_011571724.1; NC_008212.1.
DR   AlphaFoldDB; Q18HD7; -.
DR   SMR; Q18HD7; -.
DR   STRING; 362976.HQ_2492A; -.
DR   EnsemblBacteria; CAJ52605; CAJ52605; HQ_2492A.
DR   GeneID; 4192971; -.
DR   KEGG; hwa:HQ_2492A; -.
DR   eggNOG; arCOG01857; Archaea.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   OMA; VVHLTMY; -.
DR   Proteomes; UP000001975; 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..193
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000365300"
FT   BINDING         86
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"
SQ   SEQUENCE   193 AA;  21458 MW;  5153F2BACDEA180F CRC64;
     MKRSCENDVS VLRYGHRPGR DDRMTTHVGL TARALGADQV IFPDNATQSA ETVSDIVSRF
     GGPFDVERTD GLNATIREWS GTVIHLTMYG ERVQDVTEVI RETCLHHQPL LIIIGGEKVP
     SDVYEWADWN IAVTNQPHSE VAGLAVFLDR LFMGQELEQE WAGAEHVVVP QACGKRVVDA
     ELTTEADEMN AEK