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Database: UniProt
Entry: A0A078KMG4_9FIRM
LinkDB: A0A078KMG4_9FIRM
Original site: A0A078KMG4_9FIRM 
ID   A0A078KMG4_9FIRM        Unreviewed;       453 AA.
AC   A0A078KMG4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=CCDG5_0601 {ECO:0000313|EMBL:CDZ23732.1};
OS   [Clostridium] cellulosi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Oscillospiraceae incertae sedis.
OX   NCBI_TaxID=29343 {ECO:0000313|EMBL:CDZ23732.1, ECO:0000313|Proteomes:UP000032431};
RN   [1] {ECO:0000313|Proteomes:UP000032431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5 {ECO:0000313|Proteomes:UP000032431};
RA   Wibberg D.;
RL   Submitted (JUL-2014) 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; LM995447; CDZ23732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078KMG4; -.
DR   STRING; 29343.CCDG5_0601; -.
DR   KEGG; ccel:CCDG5_0601; -.
DR   PATRIC; fig|29343.3.peg.624; -.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000032431; Chromosome.
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; 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:UP000032431};
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          24..300
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   453 AA;  49233 MW;  9E1C3C88E73DC369 CRC64;
     MQNPLPEAFL ERMKSLSGFD FESFLKCYSE PPYRGLRVNT LKCSVNEFKR IFPYELSATP
     FAEEGFYIGN EITGRHPFHH AGLFYFQEPS AMSAVTALDV KPGMKVLDLC AAPGGKSTQA
     AAKLAGDGFI LCNEVIASRA KILLSNIERC GVRNAAVTNE KTDILCSRLS GFFDRVLVDA
     PCSGEGMFRR DPEAVKEWNA GSPAACARRQ AGILDDAAKA VAPGGVLVYS TCTFSPDENE
     GVINAFLKAH PDFEIEEISA DFGRAACPEW AGASEDIKKA RRVFPTDGGE GHFVAKMRCR
     GGCLSKYKEA KRKIDKNSEK LFLDFYNAQF GESLYGDLYE AAGKIFILPH GMPDLSGINV
     VRAGVFAGII KGSRFEPAHA LYMAAKSYTC LNSADFQPES VSLAKFLHGE EIEAPSGLEK
     GYAAVKVQGF VTGFGKVSGG VIKNHYPKGL RNL
//
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