ID   TRM56_METTP             Reviewed;         174 AA.
AC   A0B9Q9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Mthe_1667;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK15433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B9Q9; -.
DR   SMR; A0B9Q9; -.
DR   STRING; 349307.Mthe_1667; -.
DR   EnsemblBacteria; ABK15433; ABK15433; Mthe_1667.
DR   KEGG; mtp:Mthe_1667; -.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   OMA; VVHLTMY; -.
DR   BioCyc; MTHE349307:G12X8-1676-MON; -.
DR   Proteomes; UP000000674; 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..174
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000365314"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT   BINDING         108..112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT   BINDING         126..133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ   SEQUENCE   174 AA;  19504 MW;  AC51BED4FC8E8167 CRC64;
     MRITVLRLGH RPERDKRITT HVGLVARAFG ADEILIEGRD ESVVESLRDV VNRWGGSFSV
     TDGIAWRDEL RRFRDSGGKI VHLTMYGRRI DEVIGEIRSC ERIMVVVGAE KVPPDVYDIA
     DWNVAVGNQP HSEVAALAVF LDRLFMGEEL EKDFGGRLKV IPAARGKVVL DRGL