ID   TRM56_METAC             Reviewed;         177 AA.
AC   Q8TL02;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=MA_3241;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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; AE010299; AAM06612.1; -; Genomic_DNA.
DR   RefSeq; WP_011023175.1; NC_003552.1.
DR   AlphaFoldDB; Q8TL02; -.
DR   SMR; Q8TL02; -.
DR   STRING; 188937.MA_3241; -.
DR   EnsemblBacteria; AAM06612; AAM06612; MA_3241.
DR   GeneID; 1475134; -.
DR   KEGG; mac:MA_3241; -.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   InParanoid; Q8TL02; -.
DR   OMA; VVHLTMY; -.
DR   OrthoDB; 83050at2157; -.
DR   PhylomeDB; Q8TL02; -.
DR   Proteomes; UP000002487; 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..177
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000146928"
FT   BINDING         84
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT   BINDING         109..113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ   SEQUENCE   177 AA;  19801 MW;  E8F4C90D4756420C CRC64;
     MKRIVLLRLG HRPERDKRIT THVGLTARML GAEGMLLASD DQGIVHSLED VVRRWGGDFY
     IKNNVNFKQE IRAWKEEGGK VCHLSMYGVN LPDVTGELKK CKKLMIVVGA EKVPPEIYQL
     ANWNVAVGSQ PHSEVAAVAI TMDRIAEGEP LEKEFPGAEL TIVPAERGKH VIENIRE