ID   LAST_SERMA              Reviewed;         196 AA.
AC   P37006;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Uncharacterized tRNA/rRNA methyltransferase LasT {ECO:0000305};
DE            EC=2.1.1.-;
DE   Flags: Fragment;
GN   Name=lasT;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41;
RX   PubMed=8423151; DOI=10.1128/jb.175.3.785-794.1993;
RA   Omori K., Suzuki S., Komatsubara S.;
RT   "Nucleotide sequence of the Serratia marcescens threonine operon and
RT   analysis of the threonine operon mutations which alter feedback inhibition
RT   of both aspartokinase I and homoserine dehydrogenase I.";
RL   J. Bacteriol. 175:785-794(1993).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=8265370; DOI=10.1093/nar/21.23.5519;
RA   Koonin E.V., Rudd K.E.;
RT   "SpoU protein of Escherichia coli belongs to a new family of putative rRNA
RT   methylases.";
RL   Nucleic Acids Res. 21:5519-5519(1993).
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; X60821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P37006; -.
DR   SMR; P37006; -.
DR   STRING; 273526.SMDB11_4763; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           <1..196
FT                   /note="Uncharacterized tRNA/rRNA methyltransferase LasT"
FT                   /id="PRO_0000159776"
FT   BINDING         44..46
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   BINDING         107..109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:P0AE01"
FT   NON_TER         1
SQ   SEQUENCE   196 AA;  21551 MW;  A1A058E1F21D81CD CRC64;
     VDSEAHLQPA ARWVAHGAGE ILDGVQTFAT LEQALADVDF TVATTARSRA RFHYYCTPPE
     LLEQLSERKQ WVGQAALVFG REDSGLTNEE LALADLLTGV PMQADYPSLN LGQAVMVYCY
     QLASLMGVNA APQEAAAPEG QLRALRHRAD ALLDALEVGD DQKLRDWLHQ RLGALPQRDT
     AMLHTLLHDI EKKLAK