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Database: UniProt
Entry: A0A1Y0C5G4_9MYCO
LinkDB: A0A1Y0C5G4_9MYCO
Original site: A0A1Y0C5G4_9MYCO 
ID   A0A1Y0C5G4_9MYCO        Unreviewed;       463 AA.
AC   A0A1Y0C5G4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:ART70315.1};
GN   ORFNames=BTO20_18675 {ECO:0000313|EMBL:ART70315.1};
OS   Mycobacterium dioxanotrophicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=482462 {ECO:0000313|EMBL:ART70315.1, ECO:0000313|Proteomes:UP000195331};
RN   [1] {ECO:0000313|EMBL:ART70315.1, ECO:0000313|Proteomes:UP000195331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-06 {ECO:0000313|EMBL:ART70315.1,
RC   ECO:0000313|Proteomes:UP000195331};
RA   He Y.;
RT   "Whole Genome Sequence of 1,4-Dioxane Degrading Bacterium Mycobacterium
RT   dioxanotrophicus PH-06.";
RL   Submitted (APR-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; CP020809; ART70315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0C5G4; -.
DR   KEGG; mdx:BTO20_18675; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000195331; Chromosome.
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   CDD; cd00620; Methyltransferase_Sun; 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; IPR048019; RsmB-like_N.
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:UP000195331};
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          181..463
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         284..290
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   463 AA;  49353 MW;  D2B1C58BCDC86C1C CRC64;
     MTRPDKRPPQ RKRQPRRTPL DPARRAAFDV LRAVSERDAY ANLALPALLT ERKIEGRDAA
     FATELTYGAC RARGLLDAVI EKASGRPTDR IDPVLLDLLR LGAYQLLRTR VEPHAAVSTT
     VDQAGIEFDT ARAGFVNGVM RTISSRDEQA WTDELAPAAD TDPVGHAAFV HAHPRWIAQA
     FTDALGARAS ELDALLTSDD ERPLVHLAAR PGVLTADALA EQSGGTVGKY SPYAVYLPGG
     DPGRLSAVRD GGAQVQDEGS QLVARALTLA ALDGPDTGRW LDLCAGPGGK TALLAAMGTA
     SGARITAVEP GERRADLVEE NTRGLGVDVH RVDGRESGLT PGFDRVLVDA PCTGLGALRR
     RPEARWRRAP GDVPGLAKLQ KELLAAAIKL TRPGGVVLYA TCSPHLAETV GVVADALRRQ
     PVTALDTREL FAPADDLGAG PYVQLWPHQH GTDAMFAAAL RVR
//
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