ID   TRMYL_VIBPA             Reviewed;         199 AA.
AC   Q87JV8;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Putative pseudouridine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587};
DE            EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00587};
GN   OrderedLocusNames=VPA0140;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000032; BAC61483.1; -; Genomic_DNA.
DR   RefSeq; NP_799650.1; NC_004605.1.
DR   RefSeq; WP_005459965.1; NC_004605.1.
DR   AlphaFoldDB; Q87JV8; -.
DR   SMR; Q87JV8; -.
DR   STRING; 223926.28808278; -.
DR   EnsemblBacteria; BAC61483; BAC61483; BAC61483.
DR   GeneID; 1190819; -.
DR   KEGG; vpa:VPA0140; -.
DR   PATRIC; fig|223926.6.peg.3099; -.
DR   eggNOG; COG1901; Bacteria.
DR   HOGENOM; CLU_107018_0_0_6; -.
DR   OMA; HADHCII; -.
DR   Proteomes; UP000002493; Chromosome 2.
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:InterPro.
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.
FT   CHAIN           1..199
FT                   /note="Putative pseudouridine methyltransferase"
FT                   /id="PRO_0000157957"
FT   BINDING         132
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   199 AA;  22278 MW;  DE51A3F190DE2F4F CRC64;
     MRSFVLRARA APTTSKALLE GVGNEAHTEI LAHTMMNTMF VAQSHREDVV VHLVLESTKD
     YSRTITIRSN DITNIGGFHE STLIAAVARA LDASVGMGKE QLREVEPGIT VRTVSFERLV
     QELAEDHQLY MLDKKGEFVR DAEIGENPCF LLTDHIPMPK KSFNSLKRLG TEKISLGPKM
     LFASQCVVLI HNELDIREF