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Database: UniProt
Entry: A0A257FMC3_9BURK
LinkDB: A0A257FMC3_9BURK
Original site: A0A257FMC3_9BURK 
ID   A0A257FMC3_9BURK        Unreviewed;       464 AA.
AC   A0A257FMC3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=16S rRNA (Cytosine(967)-C(5))-methyltransferase {ECO:0000313|EMBL:OYU26931.1};
GN   ORFNames=CFE41_14105 {ECO:0000313|EMBL:OYU26931.1};
OS   Burkholderiales bacterium PBB2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015564 {ECO:0000313|EMBL:OYU26931.1, ECO:0000313|Proteomes:UP000215624};
RN   [1] {ECO:0000313|EMBL:OYU26931.1, ECO:0000313|Proteomes:UP000215624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB2 {ECO:0000313|EMBL:OYU26931.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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: 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:OYU26931.1}.
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DR   EMBL; NKIM01000020; OYU26931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257FMC3; -.
DR   Proteomes; UP000215624; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   Gene3D; 1.10.287.730; Helix hairpin bin; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
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:UP000215624};
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          170..462
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        389
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         269..275
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         291
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         336
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   464 AA;  49176 MW;  A7CC640A8C49EAD8 CRC64;
     MAPPLHKLLL QVGDAVQAVR AGRSLTELLA QCPAELRPAT QSLSFHVLRH LGAAEALRAV
     LAPKSPPPKV EGLLLTALAL LWDAGGGPGS APYADHTVVD QAVSAVRKRM PASAGFVNAV
     LRRFLRERAD LQAQVTAAEA GPAGEVARYN HPRWWIDKVQ ADWPEVWDQL LLANNSHPPM
     TLRVNARQGS TAEYLQRLQE AGIAAQSLGA LAPQALVLER AVPVTSLPGF AEGAVSVQDA
     AAQLAGPLTV LAQDGLPALP AGARVLDACS APGGKTAHLL ELADLDLLAL DSDAQRLRRV
     QDNLQRLGQQ AQLKAADARD TASWWDGRPF DAILLDAPCS ASGIVRRHPD VRWLRRPGDI
     AQLAAIQAQL LDALWPLLKP GGRLVYATCS LFKAEGEQQV DAFLQRQADA MRPALQAVTG
     HLLPLAHNGA PPDGASPDAS SSASPGTEAL FDGFFYAVLS KRAA
//
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