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Database: UniProt
Entry: A0A1G6V6A2_9PSEU
LinkDB: A0A1G6V6A2_9PSEU
Original site: A0A1G6V6A2_9PSEU 
ID   A0A1G6V6A2_9PSEU        Unreviewed;       475 AA.
AC   A0A1G6V6A2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SDD49200.1};
GN   ORFNames=DES30_103282 {ECO:0000313|EMBL:PWV80191.1},
GN   SAMN05421630_10967 {ECO:0000313|EMBL:SDD49200.1};
OS   Prauserella marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=530584 {ECO:0000313|EMBL:SDD49200.1, ECO:0000313|Proteomes:UP000199494};
RN   [1] {ECO:0000313|EMBL:SDD49200.1, ECO:0000313|Proteomes:UP000199494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5506 {ECO:0000313|EMBL:SDD49200.1,
RC   ECO:0000313|Proteomes:UP000199494};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PWV80191.1, ECO:0000313|Proteomes:UP000246674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45268 {ECO:0000313|EMBL:PWV80191.1,
RC   ECO:0000313|Proteomes:UP000246674};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; QGTN01000003; PWV80191.1; -; Genomic_DNA.
DR   EMBL; FMZE01000009; SDD49200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6V6A2; -.
DR   STRING; 530584.SAMN05421630_10967; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000199494; Unassembled WGS sequence.
DR   Proteomes; UP000246674; 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; 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; 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:UP000199494};
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          189..475
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         296..302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         361
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   475 AA;  50503 MW;  86AF1B856DFEA8D0 CRC64;
     MTPGRQGKPD RSRRPAPRKQ GPRKPPAQDP ARRVALDVLR AVSERDAYAN LMLPEELRRR
     RITGRDAALA TELTYGTLRA QGLLDEIITA CLDRPLSEVD KVVLDALRLG AYQLLRTRIP
     PHAAVASTVD LVREETGSHV AGFANAVLRN VSEKDEADWM RQLTPDAETD PIGNLAMRTS
     HPRWVARSFA EALGDKGAEL EAALLADDTR PAVHLLAKPG EITADELAAI TGGDPAPYSP
     YGVHLPTGGG DLAEAEPIKE KLAVVQDEGS QLVTIAATNV PVDGGSGGDT RWLDLCAGPG
     GKATLLGSLA ATAGVTVDAV EKAPHRAKLV ERATEGLPVT VHVADGRDPG LDGGYDRVLV
     DAPCSGLGAL RRRPEARWRR QPSDVADLTR LQGELLASAF GLVRAGGLVA YVVCSPHLAE
     TEGVFGNAAR RAGAEVIDAR EYFPGVPLLG DGPYVQLWPH RHGTDAMFVA LAIAR
//
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