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Database: UniProt
Entry: A0A0R1K7E7_9LACO
LinkDB: A0A0R1K7E7_9LACO
Original site: A0A0R1K7E7_9LACO 
ID   A0A0R1K7E7_9LACO        Unreviewed;       458 AA.
AC   A0A0R1K7E7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:KRK77107.1};
GN   ORFNames=FD30_GL000468 {ECO:0000313|EMBL:KRK77107.1};
OS   Levilactobacillus namurensis DSM 19117.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77107.1, ECO:0000313|Proteomes:UP000051162};
RN   [1] {ECO:0000313|EMBL:KRK77107.1, ECO:0000313|Proteomes:UP000051162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77107.1,
RC   ECO:0000313|Proteomes:UP000051162};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
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:KRK77107.1}.
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DR   EMBL; AZDT01000010; KRK77107.1; -; Genomic_DNA.
DR   RefSeq; WP_056943666.1; NZ_AZDT01000010.1.
DR   AlphaFoldDB; A0A0R1K7E7; -.
DR   STRING; 1423773.FD30_GL000468; -.
DR   GeneID; 84781591; -.
DR   PATRIC; fig|1423773.3.peg.479; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000051162; 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: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};
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..294
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        224
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         102..108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   458 AA;  50438 MW;  6FA625847556BE34 CRC64;
     MNLPDDFVTK YQRLLGDEAP AFLASLTSTV NTAGYRVNPE RKVPANLTTA KPVPYAQWGY
     YGAVKGRSLA HQSGAVYSQE PSAMFVGATA APAKGERVLD LCAAPGGKTT HLASYLQGTG
     LLVTNEINRK RVRVLAENVE RFGVANAVIL NDSPDTLSPV FPDYFDKVLV DAPCSGEGMF
     RKDPAAMDYW SLAYVEDCVT RQREILTEAV KMVKPGGQLI YSTCTFAPEE DEQMMAWVLK
     TFPEFHLVPV EKSGGVVDAR PEWADGNPEL KKAARLFPHL LQGEGHFVAK LERTSAAEPT
     RPRGQAQLGT ALSRDQRQLW QDFAQQVLGT EALPAGELVT VKDQLFAVPQ DLPALKRAHV
     FRPGLHLGTF KKNRFEPAYA LALASEPQRV NHTLAIDLDQ WQKWVHGDTI ALATAPAKGW
     YLLTCQQQPV GFGKVVGQTV KNFFPKGLRF TVYPEDLN
//
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