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Database: UniProt
Entry: A0A0D6A363_9LACO
LinkDB: A0A0D6A363_9LACO
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ID   A0A0D6A363_9LACO        Unreviewed;       466 AA.
AC   A0A0D6A363;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:QFG51287.1};
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:BAQ57252.1};
GN   ORFNames=LA749_04470 {ECO:0000313|EMBL:QFG51287.1}, LBAT_0863
GN   {ECO:0000313|EMBL:BAQ57252.1};
OS   Lactobacillus acetotolerans.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ57252.1, ECO:0000313|Proteomes:UP000035709};
RN   [1] {ECO:0000313|EMBL:BAQ57252.1, ECO:0000313|Proteomes:UP000035709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ57252.1,
RC   ECO:0000313|Proteomes:UP000035709};
RA   Toh H., Morita H., Fujita N.;
RT   "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QFG51287.1, ECO:0000313|Proteomes:UP000325393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LA749 {ECO:0000313|EMBL:QFG51287.1,
RC   ECO:0000313|Proteomes:UP000325393};
RA   Kim K.;
RT   "Genome sequencing of Lactobacillus acetotolerans.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; AP014808; BAQ57252.1; -; Genomic_DNA.
DR   EMBL; CP044496; QFG51287.1; -; Genomic_DNA.
DR   RefSeq; WP_056969643.1; NZ_CP044496.1.
DR   STRING; 1600.LBAT_0863; -.
DR   GeneID; 78212236; -.
DR   KEGG; lae:LBAT_0863; -.
DR   PATRIC; fig|1600.4.peg.885; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000035709; Chromosome.
DR   Proteomes; UP000325393; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000035709};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          1..297
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        226
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         104..110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   466 AA;  52541 MW;  9DFBE51DDCA61ED3 CRC64;
     MLKLPKEFKD KYRKLLGTDE ADEMFTAMND TNKKSFRINP LKFNTKISYS KKAPVPNLAN
     AYYGAVSGQD PEWVSGTVYS QDPSAMFPAK VANVQPGERV LDLCAAPGGK STGLGEDLKG
     QGVLVANEIS RPRAKVLREN LERWGVSNVL ITSESPEKLA PHFLQFFDKI LVDAPCSGEG
     MFRKNPEAIK YWSEDYVLTC QKRQKEILKE AVKMLRPGGE LIYSTCTFSP EEDEQIVAWL
     VKNFNLVITP IKSIKMDKIS HGHLDWAQNL DGLQNTLRFW PQDGLGEGQF IAKLTMPGVT
     IKAPIKRKNR AKKKLRNKFA LFKDEKELVA AILDKFNLPS ELNDWPKRVL VRKQHVFIPA
     LTGKQLDGLK ILSNGLELGI LKKKRFEPGH QLALVLGQVK QERVIDLPNQ ENYQSYLHGE
     TVKVDSDLRG FVLISCHNLI FSFGKIANNG VIKNYYPKGL RTLKKG
//
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