ID   TRMYL_SHEFN             Reviewed;         198 AA.
AC   Q083D7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Sfri_1778;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000447; ABI71628.1; -; Genomic_DNA.
DR   RefSeq; WP_011637244.1; NC_008345.1.
DR   AlphaFoldDB; Q083D7; -.
DR   SMR; Q083D7; -.
DR   STRING; 318167.Sfri_1778; -.
DR   EnsemblBacteria; ABI71628; ABI71628; Sfri_1778.
DR   KEGG; sfr:Sfri_1778; -.
DR   eggNOG; COG1901; Bacteria.
DR   HOGENOM; CLU_107018_0_0_6; -.
DR   OMA; HADHCII; -.
DR   OrthoDB; 1311630at2; -.
DR   Proteomes; UP000000684; 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: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..198
FT                   /note="Putative pseudouridine methyltransferase"
FT                   /id="PRO_1000129786"
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   198 AA;  22362 MW;  A460C3B0F4CFE7F6 CRC64;
     MRAFVVRARA APVDSQQFLA AIGHEAHTEI LAHTLMNTIF VAQSHRDDVV VYLVLESTQD
     FSRTICFRSN ELGHIGGFHE QNLTNKIAKA LTVSKGMAKE QLREVEAGIT VRTVSFEKLI
     QELAEDYQLY MLEKKGTPVR DIEFAANPCF LLTDHIPMPK KSFNSLKRLG TQHINLGPKM
     LFASQCVVLI HNELDMRL