ID   A0A235B7Y6_9BACL        Unreviewed;       459 AA.
AC   A0A235B7Y6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:OYD08342.1};
GN   ORFNames=CHM34_05715 {ECO:0000313|EMBL:OYD08342.1};
OS   Paludifilum halophilum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Paludifilum.
OX   NCBI_TaxID=1642702 {ECO:0000313|EMBL:OYD08342.1, ECO:0000313|Proteomes:UP000215459};
RN   [1] {ECO:0000313|EMBL:OYD08342.1, ECO:0000313|Proteomes:UP000215459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102817 {ECO:0000313|EMBL:OYD08342.1,
RC   ECO:0000313|Proteomes:UP000215459};
RA   Belbahri L.;
RT   "The genome sequence of Paludifilum halophilum highlights mechanisms for
RT   microbial adaptation to high salt environemnts.";
RL   Submitted (JUL-2017) 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}.
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:OYD08342.1}.
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DR   EMBL; NOWF01000003; OYD08342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235B7Y6; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000215459; 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; 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; 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; 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:UP000215459};
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          22..302
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        232
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         110..116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   459 AA;  51706 MW;  076BE2C94C136936 CRC64;
     MHLPEEYLNQ MKKLLGEEYP AFLATYEKPP SRGLRVNTLK IPVKEMLERI SFQLKPIPWC
     ETGFFYDHDQ DRPGKHVFHA AGLYYIQDPS AMAAAEALNP QPGEKVLDLC AAPGGKTTQI
     AAKMEGQGLL VANEISPQRR KALVENLERC GISHTTVLGE SPERLAERFS GFFDRILIDA
     PCSGEGMFRK DPDTCERWST KATKQCAGVQ SEILNAASPM LRPGGILTYS TCTFNPRENE
     EILQRFLEAH PDYETTPVPG FHHFQPARPE WGDSSPGLSR AARLWPHHLH GEGHFIAVLK
     KAEGPEGTKQ RPGKFPPVSA DAVKTYQEFV REVLSTGATE GPFTLYGDHL YQIREDLPSL
     KGLKVERPGF YLGQVKRKRF VPSHTWAMTL TPGRVQRTLS FDVEDPDLYR YLRGEALPLH
     NGKKGWTLVT VDRFPLGWGK ISGGLLKNHY PKRLRWDPI
//