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Database: UniProt
Entry: A0A172UVB1_9MYCO
LinkDB: A0A172UVB1_9MYCO
Original site: A0A172UVB1_9MYCO 
ID   A0A172UVB1_9MYCO        Unreviewed;       442 AA.
AC   A0A172UVB1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:ANE83022.1};
GN   ORFNames=A7U43_17705 {ECO:0000313|EMBL:ANE83022.1};
OS   Mycobacterium adipatum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1682113 {ECO:0000313|EMBL:ANE83022.1, ECO:0000313|Proteomes:UP000077143};
RN   [1] {ECO:0000313|EMBL:ANE83022.1, ECO:0000313|Proteomes:UP000077143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC-RL4 {ECO:0000313|EMBL:ANE83022.1,
RC   ECO:0000313|Proteomes:UP000077143};
RA   Ren L., Fan S., Ruth N., Jia Y., Wang J., Qiao C.;
RT   "Complete genome sequence of a phthalic acid esters degrading Mycobacterium
RT   sp. YC-RL4.";
RL   Submitted (MAY-2016) 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; CP015596; ANE83022.1; -; Genomic_DNA.
DR   RefSeq; WP_068003027.1; NZ_CP015596.1.
DR   AlphaFoldDB; A0A172UVB1; -.
DR   STRING; 1682113.A7U43_17705; -.
DR   KEGG; madi:A7U43_17705; -.
DR   Proteomes; UP000077143; 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:UP000077143};
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          162..442
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         265..271
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   442 AA;  46411 MW;  E0211B3530ED8958 CRC64;
     MDPARRAAFD VLRAVSERDA YANLTLPVLL RERGITGLDA AFATELAYGT CRTRGLLDAV
     ISSAAGRPVD QIDSVLLDLL RLGAYQLLRT RVDAHAAVDT TVEQAGIEFD SVRAGFVNGV
     LRKIAGQDEQ AWVAELAPAQ ATDPVGHAAF VHAHPRWIAQ AFVDALGARA GELGALLASD
     DARPVVHLAA RPGVLTATDL AAQVAGTVGR YSPYAVYLPG GDPGDLAAVR EGTALVQDEG
     SQLVARAVTL ATVDGPDHGR WLDLCSGPGG KTALIAALAG DARVTAVEPA EHRADFVVQN
     TVGLPVDVVR VDGRASGLEP GFDRVLVDAP CTGLGALRRR PEARWRRQPG DVPTLVKLQR
     ELLAAAIALT RPGGVVLYAT CSPHLAETVG VVADALRRQP VTALDTREFF PGVDQLGAGP
     YVQLWPHLHG TDAMFAAALK VG
//
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