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Database: UniProt
Entry: A0A069D709_9BACE
LinkDB: A0A069D709_9BACE
Original site: A0A069D709_9BACE 
ID   A0A069D709_9BACE        Unreviewed;       474 AA.
AC   A0A069D709;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylases {ECO:0000313|EMBL:GAK38076.1};
GN   ORFNames=JCM15093_3372 {ECO:0000313|EMBL:GAK38076.1};
OS   Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK38076.1, ECO:0000313|Proteomes:UP000027601};
RN   [1] {ECO:0000313|EMBL:GAK38076.1, ECO:0000313|Proteomes:UP000027601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK38076.1,
RC   ECO:0000313|Proteomes:UP000027601};
RX   PubMed=25736980;
RA   Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA   Hattori M., Ohkuma M.;
RT   "Distribution and evolution of nitrogen fixation genes in the phylum
RT   bacteroidetes.";
RL   Microbes Environ. 30:44-50(2015).
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:GAK38076.1}.
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DR   EMBL; BAJS01000037; GAK38076.1; -; Genomic_DNA.
DR   RefSeq; WP_024997607.1; NZ_BAJS01000037.1.
DR   AlphaFoldDB; A0A069D709; -.
DR   STRING; 1121097.GCA_000428125_01808; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000027601; 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   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; IPR023267; RCMT.
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   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:UP000027601};
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   ACT_SITE        230
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         109..115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   474 AA;  53803 MW;  6B7B0C2BB1290227 CRC64;
     MNLPADFIAY TRHLLGEEEY DKLYTALQQE TPVSIRFNPL KSMAGYRNDP RLESVPWCST
     GYYLDERFTF TFDPLFHAGC YYVQEASSMF LEQALKQYVN VPSVMLDLCA APGGKSTHCL
     GVLPEGSLLV ANEVIRSRSN ILAENIIKWG NPCVVVTNND PADFTCLEHF FDVILTDVPC
     SGEGMFRKDA TAVTEWSQEN VDVCWKRQRR ILADIWPSLK PGGLLIYSTC TYNTHEDEEN
     LLWMQHELGA EVLPVDTHEE WGIKGCLIDA RLPVYRFMPH ITKGEGFFLA VLRKPYGKEE
     NQRTLSAGGP KSGKSKNKGG VAPLKEFFEK AKTWVDKNEE YQLLSLNPSA IYAFPMQYQN
     ELQLIQKYLH VIFAGVVIGE VKGKDLIPDH SLAMSSVLRS DIFPRVEVAY EQAIAYLRKE
     AVTLDVTAPR GYVLLTYKQL PLGFVKNIGN RANNLYPQEW RIRSGYLPEI VRTL
//
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