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Database: UniProt
Entry: M5J7A2_9LACO
LinkDB: M5J7A2_9LACO
Original site: M5J7A2_9LACO 
ID   M5J7A2_9LACO            Unreviewed;       466 AA.
AC   M5J7A2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=23S rRNA m(5)C methyltransferase {ECO:0000313|EMBL:EKW98554.1};
GN   ORFNames=D271_06080 {ECO:0000313|EMBL:EKW98554.1};
OS   Ligilactobacillus saerimneri 30a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW98554.1, ECO:0000313|Proteomes:UP000011912};
RN   [1] {ECO:0000313|EMBL:EKW98554.1, ECO:0000313|Proteomes:UP000011912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30a {ECO:0000313|EMBL:EKW98554.1,
RC   ECO:0000313|Proteomes:UP000011912};
RX   PubMed=23405290;
RA   Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA   Lolkema J.S., Lucas P.M.;
RT   "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT   sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT   Biogenic Amines.";
RL   Genome Announc. 1:E00097-E00012(2013).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKW98554.1}.
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DR   EMBL; ANAG01000017; EKW98554.1; -; Genomic_DNA.
DR   RefSeq; WP_009554466.1; NZ_ANAG01000017.1.
DR   AlphaFoldDB; M5J7A2; -.
DR   STRING; 1227363.D271_06080; -.
DR   GeneID; 80987091; -.
DR   PATRIC; fig|1227363.6.peg.1194; -.
DR   Proteomes; UP000011912; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; 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; 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; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
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; 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:UP000011912};
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..295
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          301..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        225
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         103..109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   466 AA;  52120 MW;  A587F008E843A36B CRC64;
     MQLPQAFIDK YTNLLGDEAP AFFASLDQDV EHGFRLNPLK AKYQDVALDL HHPVPFVQDA
     YYGTVSGKSL AHQAGYVYSQ DISAMYVAEV AAAQPGERVL DLCAAPGGKS TQLAAQLQNQ
     GLLVSNEINT KRARILAENM ERIGATNVIV LNEDPANMEQ YFPAYFDKIV VDAPCSGEGM
     FRKDHNAVTY WHEHYPAECA VRQKNILNSA LKMLRPGGQL VYSTCTFAPE EDEQIAAWLL
     ATYPELEMVA VPKVAGMTPG QTAFADNDSE MTKAVRMMPH HFQGEGQFVA KFQLAQTAPE
     LAPVPTTKKK KRRGKQARGK SNSLSKEQLA LWEEFKQSFF MDRGGQKFST NNLRLNGNYL
     YYYDASWPDI DQMKYVRPGI LLGEFKKHRF EPSYALALAV QPAEIQAKLD LDESEWRQYV
     GGNTVQYTGP SQPNGWYLLV CAGKPFAMGK LVNGIIKNFF PKGLRF
//
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