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Database: UniProt
Entry: A0A372FTZ0_9ACTN
LinkDB: A0A372FTZ0_9ACTN
Original site: A0A372FTZ0_9ACTN 
ID   A0A372FTZ0_9ACTN        Unreviewed;       436 AA.
AC   A0A372FTZ0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=rRNA small subunit methyltransferase B {ECO:0000313|EMBL:RFS44247.1};
GN   ORFNames=D0Q02_23265 {ECO:0000313|EMBL:RFS44247.1};
OS   Micromonospora craniellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS44247.1, ECO:0000313|Proteomes:UP000262621};
RN   [1] {ECO:0000313|EMBL:RFS44247.1, ECO:0000313|Proteomes:UP000262621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63014 {ECO:0000313|EMBL:RFS44247.1,
RC   ECO:0000313|Proteomes:UP000262621};
RA   Li L., Lin H.W.;
RT   "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT   South China Sea.";
RL   Submitted (AUG-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|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:RFS44247.1}.
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DR   EMBL; QVFU01000034; RFS44247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372FTZ0; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000262621; 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; 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:UP000262621};
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          147..436
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        372
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         249..255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         274
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   436 AA;  46194 MW;  72C67AFBA033B138 CRC64;
     MHRDDAYANL VLPAILRDEG LTGRDAAFAT ELTYGTLRHV GTLDAILTAA AGRDVQRIDP
     PVRDALRIGA YQLLHTRVPA HAAVSSTVDL VRVVGPSATG FANAVLREVA ERDNDGWVAR
     LAPPIQTDPI GHLALAYSHP QWIVRAFSEA LGGDLGETTR LLIEDNERPP VHLCARPGLA
     DPVDLADEVG GAPGAFSPYA VYLGGGAPGD LAAVADGRAH VQDEGSQLVA DALAAAPLDG
     PDGRWLDLCA GPGGKSGLLG ALAAQREARL TAVEVAEHRA RLVGNATRAL PVTVLHTDGR
     LVGSEPKLPE EHFDRVLVDA PCTGLGSLRR RPESRWRRQP SDLPALTRLQ RELLTAGLRA
     VRPGGVVAYV TCSPHVVETH VTVTEAARRC GAPVDFVDAR PLLPVGMPGI GDGPTVQLWP
     HRHGTDAMFL ALLRRT
//
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