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TRM56_METM7
ID   TRM56_METM7             Reviewed;         179 AA.
AC   A6VH11;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=MmarC7_0670;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) 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; CP000745; ABR65737.1; -; Genomic_DNA.
DR   RefSeq; WP_011977059.1; NC_009637.1.
DR   AlphaFoldDB; A6VH11; -.
DR   SMR; A6VH11; -.
DR   STRING; 426368.MmarC7_0670; -.
DR   EnsemblBacteria; ABR65737; ABR65737; MmarC7_0670.
DR   GeneID; 5329580; -.
DR   KEGG; mmz:MmarC7_0670; -.
DR   eggNOG; arCOG01857; Archaea.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   OMA; VVHLTMY; -.
DR   OrthoDB; 83050at2157; -.
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; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..179
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000365309"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT   BINDING         112..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
FT   BINDING         130..137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ   SEQUENCE   179 AA;  20517 MW;  D9390DA63A072A52 CRC64;
     MAIEILRLGH RGERDKRIST HVALTSRALG AEKIIFTEDD KHVKESVERI VESWGGEFKF
     EVVKSWRTYT RRFKDNGIVV HLTMYGENIN KIMTEIREDI SKTNKNLLLI IGAEKVPREA
     YDLADYNLSV GNQPHSEVAA LAIFLDRLTE GKTLYSEYDD AKIKVTPSKS EKCVFVEKD
 
 
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