TRM56_ARCFU
ID TRM56_ARCFU Reviewed; 168 AA.
AC O29507;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=AF_0751;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of a protein AF_0751 from Archaeoglobus fulgidus.";
RL Submitted (DEC-2006) to the PDB data bank.
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:0000305|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000305}.
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DR EMBL; AE000782; AAB90489.1; -; Genomic_DNA.
DR PIR; G69343; G69343.
DR RefSeq; WP_010878254.1; NC_000917.1.
DR PDB; 2O3A; X-ray; 2.20 A; A/B=2-168.
DR PDBsum; 2O3A; -.
DR AlphaFoldDB; O29507; -.
DR SMR; O29507; -.
DR STRING; 224325.AF_0751; -.
DR EnsemblBacteria; AAB90489; AAB90489; AF_0751.
DR GeneID; 24794349; -.
DR KEGG; afu:AF_0751; -.
DR eggNOG; arCOG01857; Archaea.
DR HOGENOM; CLU_123709_0_0_2; -.
DR OMA; VVHLTMY; -.
DR OrthoDB; 83050at2157; -.
DR PhylomeDB; O29507; -.
DR EvolutionaryTrace; O29507; -.
DR Proteomes; UP000002199; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..168
FT /note="tRNA (cytidine(56)-2'-O)-methyltransferase"
FT /id="PRO_0000146926"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 104..108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:2O3A"
FT HELIX 129..140
FT /evidence="ECO:0007829|PDB:2O3A"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2O3A"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2O3A"
SQ SEQUENCE 168 AA; 19026 MW; ACEDE86A81D3C308 CRC64;
MEVYVLRLGH RPERDKRIST HVALTARAFG AKGIYFDTED KSVFESVRDV VERWGGDFFI
KAVSWKKLLR EFDGLKVHLT MYGIPLPQKL EEIKRADKVL VVVGAEKVPP EVYELCDLNI
SIGTQPHSEV AALAVFLDRV LGKVFDISFD DAKIKVIPSE RGKRVVSE
