TRM56_THEAC
ID TRM56_THEAC Reviewed; 339 AA.
AC Q9HJN6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Ta0931;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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; AL445066; CAC12060.1; -; Genomic_DNA.
DR RefSeq; WP_010901340.1; NC_002578.1.
DR AlphaFoldDB; Q9HJN6; -.
DR SMR; Q9HJN6; -.
DR STRING; 273075.Ta0931; -.
DR EnsemblBacteria; CAC12060; CAC12060; CAC12060.
DR GeneID; 1456466; -.
DR KEGG; tac:Ta0931; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_817897_0_0_2; -.
DR OMA; LRINHRP; -.
DR OrthoDB; 61735at2157; -.
DR BRENDA; 2.1.1.206; 6324.
DR Proteomes; UP000001024; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..339
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000365326"
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 339 AA; 38120 MW; 74A0FB868268138A CRC64;
MITVLRINHR PYRDKRITTH VALTARAFGA SAILVDERDE TLENTIRGVI SNFGGSFSIK
TGCNWIQEFK HFQGIRVHLT MYGRRINDVI DEIRNSGKDV MVLVGSEKVP IEAYEIADYN
VSVTNQPISE VSALAIFLDR YFQGKEFEFE FRGRINVQPA ERGKIVKIIP DEIECLDLLK
KYGASEQLIE HVKAVEGLAL KIAERCNADK RVIVAGSLLH DIGRTRTNGI DHAVAGAEIL
RSENIHDSVV SAVERHIGAG ITREEAARLG LPEKDYVPET LEEMIVAQAD NLFAGNKRLR
LEEVLNIYRK RGLDSAAERI KELHRRISAI AGIDIDEIR