TRMYL_SHEB8
ID TRMYL_SHEB8 Reviewed; 198 AA.
AC A6WPD0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Shew185_2532;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-2007) 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; CP000753; ABS08669.1; -; Genomic_DNA.
DR RefSeq; WP_012089427.1; NC_009665.1.
DR AlphaFoldDB; A6WPD0; -.
DR SMR; A6WPD0; -.
DR KEGG; sbm:Shew185_2532; -.
DR HOGENOM; CLU_107018_0_0_6; -.
DR OMA; HADHCII; -.
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; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..198
FT /note="Putative pseudouridine methyltransferase"
FT /id="PRO_1000129784"
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; 22321 MW; 3C09A8F6DADED443 CRC64;
MRAFVLRARS APTDSQLFLA SVGQEPHTEI LAHTLMNTIF VAQSHRNDVV VYLVLESTHD
FSRTICFDTR NICHIGGFHE QALLTKIAKA LDISRGMTKE QTRVVDEGIT VSTISFEKLV
QDLAVDYQLF MMDKKGTSIR EQEFVGNPCF LLTDHIPMPK KSFNTLKRLG AQKISLGPKM
LFASQCVVLI HNELDINQ