ID   A0A238Z5X8_9ACTN        Unreviewed;       462 AA.
AC   A0A238Z5X8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SNR78378.1};
GN   ORFNames=SAMN06272737_12539 {ECO:0000313|EMBL:SNR78378.1};
OS   Blastococcus mobilis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938746 {ECO:0000313|EMBL:SNR78378.1, ECO:0000313|Proteomes:UP000198403};
RN   [1] {ECO:0000313|EMBL:SNR78378.1, ECO:0000313|Proteomes:UP000198403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44272 {ECO:0000313|EMBL:SNR78378.1,
RC   ECO:0000313|Proteomes:UP000198403};
RA   Kim H.J., Triplett B.A.;
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}.
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DR   EMBL; FZNO01000025; SNR78378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238Z5X8; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000198403; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 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; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   Pfam; PF01029; NusB; 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:UP000198403};
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          184..461
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        400
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         281..287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         347
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   462 AA;  49242 MW;  B68C9F27DC9F30B5 CRC64;
     MTRPPRRPGR TPGRRHPATR RRELDGARLT AYDVLDGVSS RAAYANLLLP QLLRERQLDV
     RDAAFATQLA YGTLRAQGTL DAILAGLVSR PLGELDPRVL DLLRLGAYQL IDLRVPSHAA
     VDTTVDLTRA IVGTGASGLV NAVLRKVAAG GDRDQWLSTL GVAGEERLAL ATNHPRWIVD
     AWRDALGGEG ELEPALLADD AAPEVHLVAR RMGRDALVEE SGGEAGPWSP FAVRLHGGDP
     GRLASVRSGV AAVQDEGSQV AGLLLTRAPL EGRDEAWLDM CAGPGGKAGL LAAVRPEGVR
     LTAADRAPHR AELVRKALAG EADVEVLAAD GTAPPWESGS FDRVLLDAPC TGLGALRRRP
     EVRWRRTEDD VPPLADLQAE LLASALASVR VGGVVAYVTC SPHTAETADV VDAAAARDGV
     EVLPVAPLFP EIPGIERDDY GQLWPHRHGT DAMFMALLRR TR
//