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TRMY_METM7
ID   TRMY_METM7              Reviewed;         198 AA.
AC   A6VFL5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=MmarC7_0171;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR65241.1; -; Genomic_DNA.
DR   RefSeq; WP_011976578.1; NC_009637.1.
DR   AlphaFoldDB; A6VFL5; -.
DR   SMR; A6VFL5; -.
DR   STRING; 426368.MmarC7_0171; -.
DR   EnsemblBacteria; ABR65241; ABR65241; MmarC7_0171.
DR   GeneID; 5329149; -.
DR   KEGG; mmz:MmarC7_0171; -.
DR   eggNOG; arCOG01239; Archaea.
DR   HOGENOM; CLU_107018_0_0_2; -.
DR   OMA; HADHCII; -.
DR   OrthoDB; 126445at2157; -.
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; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..198
FT                   /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT                   /id="PRO_1000025469"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         153
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         176..181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ   SEQUENCE   198 AA;  22690 MW;  2CC8107A4FFC6D51 CRC64;
     MKEFIIKANK AVTNGEINLK DLPGSSGRLD LLCRCVNSAF FLSHDMRRDT IFYSVNYGDP
     NPPVTLKFVG SELKRVSPDE RSIALFIKKA LEKDATELWK ESTSGIYSSK REFRDIILEK
     KNEGKRIFYL HLNGKPLEDF EFKDDEDFLF VLGDHIGIGD EDEEFLEEIG AEKISLSPLE
     LHADHCIILV HNILDRLK
 
 
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