ID   TRMY_METMA              Reviewed;         211 AA.
AC   Q8PU23;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=MM_2534;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32230.1; -; Genomic_DNA.
DR   RefSeq; WP_011034450.1; NC_003901.1.
DR   AlphaFoldDB; Q8PU23; -.
DR   SMR; Q8PU23; -.
DR   STRING; 192952.MM_2534; -.
DR   EnsemblBacteria; AAM32230; AAM32230; MM_2534.
DR   GeneID; 44088166; -.
DR   GeneID; 66135495; -.
DR   KEGG; mma:MM_2534; -.
DR   PATRIC; fig|192952.21.peg.2905; -.
DR   eggNOG; arCOG01239; Archaea.
DR   HOGENOM; CLU_107018_0_0_2; -.
DR   OMA; HADHCII; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-UniRule.
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..211
FT                   /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT                   /id="PRO_0000157950"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ   SEQUENCE   211 AA;  23249 MW;  4A629BF0BC7AD7B2 CRC64;
     MRDIVIIGHK AKTSGDFSLN DLPGSAGRMD ILCRCVSSAL FLSFGMRRDV NVHLLLLGEP
     DPGKIIRFEG LHLRYLNPDE RSSGSLIQKA LLKNAAGQDI RSTPGVWTRT GDLNSLLASF
     EGRTLLYLRE DGKDFREIAR EIQDPVFILG DHTGVTEEEE KQLLEAGAQV ISVGPISLHS
     NHCITLIHNE LDRAEAERGE IPGGNISRPE D