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TRMY_THEKO
ID   TRMY_THEKO              Reviewed;         198 AA.
AC   Q5JF45;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587};
DE            EC=2.1.1.257 {ECO:0000255|HAMAP-Rule:MF_00587};
GN   Name=trmY {ECO:0000255|HAMAP-Rule:MF_00587}; OrderedLocusNames=TK0554;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at
CC       position 54 (Psi54) in tRNAs. {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pseudouridine(54) in tRNA + S-adenosyl-L-methionine = H(+) +
CC         N(1)-methylpseudouridine(54) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:55292, Rhea:RHEA-COMP:14140, Rhea:RHEA-COMP:14141,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; EC=2.1.1.257;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00587};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00587}.
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DR   EMBL; AP006878; BAD84743.1; -; Genomic_DNA.
DR   RefSeq; WP_011249509.1; NC_006624.1.
DR   AlphaFoldDB; Q5JF45; -.
DR   SMR; Q5JF45; -.
DR   STRING; 69014.TK0554; -.
DR   EnsemblBacteria; BAD84743; BAD84743; TK0554.
DR   GeneID; 3234892; -.
DR   KEGG; tko:TK0554; -.
DR   PATRIC; fig|69014.16.peg.542; -.
DR   eggNOG; arCOG01239; Archaea.
DR   HOGENOM; CLU_107018_0_0_2; -.
DR   InParanoid; Q5JF45; -.
DR   OMA; HADHCII; -.
DR   OrthoDB; 126445at2157; -.
DR   PhylomeDB; Q5JF45; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   CDD; cd18087; TrmY-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00587; tRNA_methyltr_TrmY; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR007158; TrmY.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR40703; PTHR40703; 1.
DR   Pfam; PF04013; Methyltrn_RNA_2; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..198
FT                   /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT                   /id="PRO_0000157955"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         155
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ   SEQUENCE   198 AA;  22465 MW;  AA143D8C6DD317BA CRC64;
     MRTFILKANT AVTSPDFSLK DLPGTGGRID LLCRFLNSAF LLSHGIRKDV RVFMTLYGRP
     NPPKTIHFEG PKLKVRLNPD ERSTALILKK ALKIGEDLRE PTKEVEVFPG VYVSNMTFED
     VVRRVMKDST LYYLVEDGKP ITEIEFPQNP AFVLGDHLGL SKEDERFLEG IAKKVRIGRR
     SYLASHVVAF VNIWLDGM
 
 
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