TRM56_METM6
ID TRM56_METM6 Reviewed; 179 AA.
AC A9A9N8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=MmarC6_1248;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
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., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-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; CP000867; ABX02061.1; -; Genomic_DNA.
DR RefSeq; WP_012193997.1; NC_009975.1.
DR AlphaFoldDB; A9A9N8; -.
DR SMR; A9A9N8; -.
DR STRING; 444158.MmarC6_1248; -.
DR EnsemblBacteria; ABX02061; ABX02061; MmarC6_1248.
DR GeneID; 5737785; -.
DR KEGG; mmx:MmarC6_1248; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_123709_0_0_2; -.
DR OMA; VVHLTMY; -.
DR OrthoDB; 83050at2157; -.
DR PhylomeDB; A9A9N8; -.
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_0000365308"
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; 20504 MW; FE529210F7C562D2 CRC64;
MTIEILRLGH RGERDKRIST HVALTSRALG AKKIIFTEED KHVKESVERI VDSWGGDFKF
EVVKSWRTYT KRFKDNGIVV HLTMYGENIN KIMTEIREDI SKTNKNLLLI IGAEKVPREA
YDLADYNLSV GNQPHSEVAA LAIFLDRLTE GKTLYSEYND AKIKVTPSKS EKCVFVEKD
