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TRM56_METS3
ID   TRM56_METS3             Reviewed;         180 AA.
AC   A5ULQ9;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=Msm_0932;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ87137.1; -; Genomic_DNA.
DR   RefSeq; WP_011954183.1; NC_009515.1.
DR   AlphaFoldDB; A5ULQ9; -.
DR   SMR; A5ULQ9; -.
DR   STRING; 420247.Msm_0932; -.
DR   PRIDE; A5ULQ9; -.
DR   EnsemblBacteria; ABQ87137; ABQ87137; Msm_0932.
DR   GeneID; 5217514; -.
DR   KEGG; msi:Msm_0932; -.
DR   PATRIC; fig|420247.28.peg.928; -.
DR   eggNOG; arCOG01857; Archaea.
DR   HOGENOM; CLU_123709_0_0_2; -.
DR   OMA; VVHLTMY; -.
DR   BioCyc; MSMI420247:GHWZ-957-MON; -.
DR   Proteomes; UP000001992; 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; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..180
FT                   /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT                   /id="PRO_0000365304"
FT   BINDING         85
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00077"
SQ   SEQUENCE   180 AA;  20226 MW;  9A226604A901A3D7 CRC64;
     MMNVNVLRLD HRIGRDTRIT THVCLTSRAF GASKIYLSGE EDHKLMENVR DTADRWGGNF
     EIEYAKNYMG VINKWKDNGG KVVHLTMYGS QAHEIVSEVQ KSSADILIVV GGAKVPGKVY
     KSADWNVSVT TQPHSEVSSL AVFQHLLMDG KEFDLEFENP VFEVIPTAHG KNVNIHDENR
 
 
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