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Database: UniProt
Entry: A0A1H2DBQ5_9ACTN
LinkDB: A0A1H2DBQ5_9ACTN
Original site: A0A1H2DBQ5_9ACTN 
ID   A0A1H2DBQ5_9ACTN        Unreviewed;       489 AA.
AC   A0A1H2DBQ5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SDT79686.1};
GN   ORFNames=SAMN04489716_8890 {ECO:0000313|EMBL:SDT79686.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT79686.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT79686.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT79686.1,
RC   ECO:0000313|Proteomes:UP000198688};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT629758; SDT79686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2DBQ5; -.
DR   STRING; 113562.SAMN04489716_8890; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000198688; Chromosome i.
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:UP000198688};
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          199..488
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        424
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         301..307
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         326
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         350
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         371
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   489 AA;  52125 MW;  0BFDF2CC8B2A0A40 CRC64;
     MTEHRASRPH GGRPSRPSGP GSPRDERSGR APRAGRPPAD PARQAAYEAV AAVHRDDAYA
     NLVLSDILRG MGLHGRDAAF ATELTYGTLR AVGTLDLIIA AAAEREVARI DPPARDALRL
     GAYQLLYTRV PTHAAVNQTV DLVRSVAPGA AGFSNAVMRT ISETTLEAWL ERLAPPYETD
     PIGHLSVIHH HPQWVIRSFA EALGGDLEDT ARLLIEDNQP PAVHLCARPG RADAVELADE
     VGGVPGAFSP YSVYLNGGAP REMAAIREGR AHVQDEGSQL VAAALLAAPI EGRDTRWLDL
     CAGPGGKTGL IGAIAAGRGA EVTAVEVAEH RARLVDLATE GMPVTVLPMD GRSVGRDPDL
     PEEGFDRVLV DAPCTGLGSL RRRPESRWRR QPADLPPLTR LQRELLVAAL RAVRPGGVVA
     YVTCSPHMVE TQVTVSEGAR RSGVEVDFVD ARPLLPPGMP GLGAGPTVQL WPHRHGTDAM
     FLAVLRRTS
//
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