ID   TRMY_PYRAE              Reviewed;         138 AA.
AC   Q8ZVQ3;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase;
DE            EC=2.1.1.257;
GN   Name=trmY; OrderedLocusNames=PAE2175;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at
CC       position 54 (Psi54) in tRNAs. {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.
CC       {ECO:0000305}.
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DR   EMBL; AE009441; AAL64003.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZVQ3; -.
DR   SMR; Q8ZVQ3; -.
DR   STRING; 178306.PAE2175; -.
DR   EnsemblBacteria; AAL64003; AAL64003; PAE2175.
DR   KEGG; pai:PAE2175; -.
DR   PATRIC; fig|178306.9.peg.1613; -.
DR   eggNOG; arCOG01239; Archaea.
DR   HOGENOM; CLU_1656942_0_0_2; -.
DR   OMA; PYMSWQA; -.
DR   Proteomes; UP000002439; 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   Gene3D; 3.40.1280.10; -; 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..138
FT                   /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT                   /id="PRO_0000157952"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  15818 MW;  DB88C30BAC221619 CRC64;
     MKNRFDVLVD FVIESITGGV REVYVMLCDG STYLITSLPS QRARAVARWL LSRQPFKTSL
     QAIIAKYRSV YYLHERGRDI SEARLDGNGL YIFGDHDGLS REDEELLAKH AEWISLGSTP
     YMSWHAAAYL AYLLKRQV