LAST_ECOLI
ID LAST_ECOLI Reviewed; 228 AA.
AC P37005; Q2M5R4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase LasT {ECO:0000305};
DE EC=2.1.1.-;
GN Name=lasT; Synonyms=yjtD; OrderedLocusNames=b4403, JW4366;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-175.
RC STRAIN=K12;
RX PubMed=8022271; DOI=10.1111/j.1365-2958.1994.tb00374.x;
RA Compan I., Touati D.;
RT "Anaerobic activation of arcA transcription in Escherichia coli: roles of
RT Fnr and ArcA.";
RL Mol. Microbiol. 11:955-964(1994).
RN [5]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (MAR-1994).
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; U14003; AAA97299.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77356.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78392.1; -; Genomic_DNA.
DR EMBL; L20873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S56627; S56627.
DR RefSeq; NP_418820.1; NC_000913.3.
DR RefSeq; WP_001223132.1; NZ_LN832404.1.
DR AlphaFoldDB; P37005; -.
DR SMR; P37005; -.
DR BioGRID; 4262790; 19.
DR DIP; DIP-10084N; -.
DR IntAct; P37005; 9.
DR STRING; 511145.b4403; -.
DR jPOST; P37005; -.
DR PaxDb; P37005; -.
DR PRIDE; P37005; -.
DR EnsemblBacteria; AAC77356; AAC77356; b4403.
DR EnsemblBacteria; BAE78392; BAE78392; BAE78392.
DR GeneID; 948924; -.
DR KEGG; ecj:JW4366; -.
DR KEGG; eco:b4403; -.
DR PATRIC; fig|1411691.4.peg.2282; -.
DR EchoBASE; EB2215; -.
DR eggNOG; COG0565; Bacteria.
DR HOGENOM; CLU_056931_3_1_6; -.
DR InParanoid; P37005; -.
DR OMA; GFTELRI; -.
DR PhylomeDB; P37005; -.
DR BioCyc; EcoCyc:EG12309-MON; -.
DR PRO; PR:P37005; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42786; PTHR42786; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF004808; LasT; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00050; rRNA_methyl_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..228
FT /note="Uncharacterized tRNA/rRNA methyltransferase LasT"
FT /id="PRO_0000159775"
FT BINDING 77..79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0AE01"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0AE01"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0AE01"
FT BINDING 140..142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0AE01"
FT CONFLICT 31
FT /note="L -> V (in Ref. 4; L20873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 25259 MW; 5B493EE3510820F7 CRC64;
MRITIILVAP ARAENIGAAA RAMKTMGFSD LRIVDSQAHL EPATRWVAHG SGDIIDNIKV
FPTLAESLHD VDFTVATTAR SRAKYHYYAT PVELVPLLEE KSSWMSHAAL VFGREDSGLT
NEELALADVL TGVPMVADYP SLNLGQAVMV YCYQLATLIQ QPAKSDATAD QHQLQALRER
AMTLLTTLAV ADDIKLVDWL QQRLGLLEQR DTAMLHRLLH DIEKNITK