TRM56_THEVO
ID TRM56_THEVO Reviewed; 338 AA.
AC Q979R3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=tRNA (cytidine(56)-2'-O)-methyltransferase;
DE EC=2.1.1.206;
DE AltName: Full=tRNA ribose 2'-O-methyltransferase aTrm56;
GN OrderedLocusNames=TV1097; ORFNames=TVG1129508;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose
CC methylation of cytidine at position 56 in tRNAs. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000305}.
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DR EMBL; BA000011; BAB60239.1; -; Genomic_DNA.
DR RefSeq; WP_010917329.1; NC_002689.2.
DR AlphaFoldDB; Q979R3; -.
DR SMR; Q979R3; -.
DR STRING; 273116.14325335; -.
DR DNASU; 1441211; -.
DR EnsemblBacteria; BAB60239; BAB60239; BAB60239.
DR GeneID; 1441211; -.
DR KEGG; tvo:TVG1129508; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_817897_0_0_2; -.
DR OMA; LRINHRP; -.
DR OrthoDB; 61735at2157; -.
DR PhylomeDB; Q979R3; -.
DR Proteomes; UP000001017; 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 CDD; cd00077; HDc; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00077; tRNA_methyltr_aTrm56; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR006675; HDIG_dom.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR002845; tRNA_mtfrase_aTrm56.
DR PANTHER; PTHR42197; PTHR42197; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01994; Trm56; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00277; HDIG; 1.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..338
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000365327"
FT DOMAIN 188..295
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 105..109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 38017 MW; 14E4AE364DD97353 CRC64;
MIAVLRINHR PFRDKRITTH VALTARAFGA SSILVDEKDE TLEQTINKVV ENFGGNFFIK
SGVDWKREFR NFKGIRVHLT MYGRPLEDVV KEIRESKKDV MILVGSEKVP FEAYEIADYN
VSVTNQPISE VSALAIFLDR FYDGEELNWR FTGKINVYPS ERGKKVKIIP DEQGCLDLLY
KYGASDYLIN HVKSVKELAV AIAKKTNADI NLVTAGALLH DIGRTQVQGI THAVVGADIL
RREGIDDRVV SIVEKHIGAG IQSEEAVKLG LPPDNYVPET IEEMIVAHAD NLFAGDKRLK
LQQVVDNYRK KGLEDAAERI AKLHKFLSTV IGQDMDEI