TRMY_HALMA
ID TRMY_HALMA Reviewed; 198 AA.
AC Q5UXQ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=rrnAC3253;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV47950.1; -; Genomic_DNA.
DR RefSeq; WP_004964221.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UXQ3; -.
DR SMR; Q5UXQ3; -.
DR STRING; 272569.rrnAC3253; -.
DR EnsemblBacteria; AAV47950; AAV47950; rrnAC3253.
DR GeneID; 40154051; -.
DR GeneID; 64823498; -.
DR KEGG; hma:rrnAC3253; -.
DR PATRIC; fig|272569.17.peg.3784; -.
DR eggNOG; arCOG01239; Archaea.
DR HOGENOM; CLU_107018_0_0_2; -.
DR OMA; HADHCII; -.
DR Proteomes; UP000001169; Chromosome I.
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..198
FT /note="tRNA (pseudouridine(54)-N(1))-methyltransferase"
FT /id="PRO_1000025463"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00587"
SQ SEQUENCE 198 AA; 21790 MW; F297A9D9FB2EF2D9 CRC64;
MRQFVIIGHD APTTPEFSLD DLAGAAGRLD VLCRCVTSAF FLSHAIREDV RVHLILGDEY
TVTFEGSDLR RLNPDERSTA ALIRKALEER EEAIGHIPVE TSPGVSLTRR GFEGTLDDVA
RRGTVVQLHE DGDPIVGVAP PSDPVFVLSD HHDFRDEEAA LLADRADERV SLGPKALHAD
HSITVAHNYL DTAGFERY
