ID A0A108TB15_BACSE Unreviewed; 492 AA.
AC A0A108TB15;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ribosomal RNA small subunit methyltransferase F {ECO:0000313|EMBL:KWR56680.1};
DE EC=2.1.1.178 {ECO:0000313|EMBL:KWR56680.1};
DE SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:RGR27126.1};
GN Name=rsmF {ECO:0000313|EMBL:KWR56680.1};
GN ORFNames=AA415_00991 {ECO:0000313|EMBL:KWR56680.1}, DWY58_12350
GN {ECO:0000313|EMBL:RGR27126.1};
OS Bacteroides stercoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR56680.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR56680.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR56680.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(2016).
RN [2] {ECO:0000313|EMBL:KWR56680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR56680.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RGR27126.1, ECO:0000313|Proteomes:UP000284161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF25-6 {ECO:0000313|EMBL:RGR27126.1,
RC ECO:0000313|Proteomes:UP000284161};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
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|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:KWR56680.1}.
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DR EMBL; LRGC01000003; KWR56680.1; -; Genomic_DNA.
DR EMBL; QRUB01000012; RGR27126.1; -; Genomic_DNA.
DR RefSeq; WP_060385437.1; NZ_QRUE01000014.1.
DR AlphaFoldDB; A0A108TB15; -.
DR STRING; 46506.AA415_00991; -.
DR PATRIC; fig|46506.5.peg.1066; -.
DR Proteomes; UP000056419; Unassembled WGS sequence.
DR Proteomes; UP000284161; 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:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.30.130.60; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF13636; Methyltranf_PUA; 1.
DR PRINTS; PR02008; RCMTFAMILY.
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:UP000056419};
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 1..294
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 228
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 107..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 492 AA; 55197 MW; 04D9596F37E7BBF1 CRC64;
MELPVSFADY TRTLLGDEDY KELVTSLESE QSVSIRLNPL KPFAFRSGEH AVPWCTSGFY
LEERPTFTFD PLFHAGCYYV QEASSMFVEQ ALKQYMGEEP VVMLDLCAAP GGKSTHIRSL
LPDNSLLIAN EVIRNRSQIL AENLTKWGHP DVVVTNSDPS DFTPLEDFFD VILTDVPCSG
EGMFRKDPVA ISEWSPENVE ICRQRQRRII ADIWPCLKPG GILIYSTCTY NTKENEENIR
WIRDEFGAEV LPLDVAEEWN ITGNLLQGES FPVYRFLPHK TQGEGFFLAV LRKPGMSVRN
SGDKQLISLA IAPETPGLRV EKSREKGRKV QGKGKQTPGL SKEQLAILQK WIFTADKYEF
IQKGGNVSAF PKCYIPELSA LQSSLRIVQA GLEIAGQKGK DWIPCHALAV SGILVSDAFP
CEEISYEQAI AYLRKEAVTL SDAAPRGVVL LTYKHVPLGF VKNIGNRANN LYPQEWRIRS
GYLPETVVKV HS
//
