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Database: UniProt
Entry: L7EWX3_9ACTN
LinkDB: L7EWX3_9ACTN
Original site: L7EWX3_9ACTN 
ID   L7EWX3_9ACTN            Unreviewed;       472 AA.
AC   L7EWX3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=Putative ribosomal RNA small subunit methyltransferase B {ECO:0000313|EMBL:ELP62890.1};
GN   ORFNames=STRTUCAR8_02177 {ECO:0000313|EMBL:ELP62890.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP62890.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP62890.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP62890.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT   that shares virulence genes with other actinobacterial plant pathogens.";
RL   Plasmid 65:118-124(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELP62890.1}.
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DR   EMBL; AEJB01000569; ELP62890.1; -; Genomic_DNA.
DR   RefSeq; WP_006382160.1; NZ_AEJB01000569.1.
DR   AlphaFoldDB; L7EWX3; -.
DR   STRING; 85558.T45_08201; -.
DR   PATRIC; fig|698760.3.peg.8181; -.
DR   Proteomes; UP000010931; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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   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; IPR001678; MeTrfase_RsmB/NOP2.
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; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF53; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE B-RELATED; 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:UP000010931};
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          185..471
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        409
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         288..294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         339
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         356
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   472 AA;  50737 MW;  0EC9649470C782A6 CRC64;
     MSEQPRRPHK PGKPYRRPQK DPVRILAFEA LRAVDERDAY ANLVLPPLLR AARAKGDFDG
     RDAALATELV YGTLRRQGTY DAVIGACVDR PLREVDPPVL DVLSLGVHQL LGTRIPTHAA
     VSASVELARV VLGDGRAKFV NAVLRKVAQH DLDAWIERVA PPYDDDPEDH LAVVHSHPRW
     VVSALWDSLG GGRAGIEELL AADNERPEVT LVARPGRGTT EELLHEEAAV PGRWSPYAVR
     LAEGGEPGAI EAVREGRAGV QDEGSQLVAL ALANAPVDGP DKAWLDGCAG PGGKASLLAA
     LAAQRGASLL ASEKQPHRAG LVAKALAGNP GPYQVVVGDG TRPPWRAGSF DRVLMDVPCT
     GLGALRRRPE ARWRRRPEDL EGFAPLQRAL LTTALESVRV GGIVGYATCS PHLAETRAVV
     DDVLKQHPHA ELVDARPLFE GVTDLGDGPD VQLWPHLHGT DAMYLALIRR TG
//
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