ID A0A1A9I1A6_9BACT Unreviewed; 460 AA.
AC A0A1A9I1A6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ANH81115.1};
GN ORFNames=A8C56_09100 {ECO:0000313|EMBL:ANH81115.1};
OS Niabella ginsenosidivorans.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=1176587 {ECO:0000313|EMBL:ANH81115.1, ECO:0000313|Proteomes:UP000077667};
RN [1] {ECO:0000313|EMBL:ANH81115.1, ECO:0000313|Proteomes:UP000077667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS26 {ECO:0000313|EMBL:ANH81115.1,
RC ECO:0000313|Proteomes:UP000077667};
RA Im W.T., Siddiqi M.Z.;
RT "Niabella ginsenosidivorans BS26 whole genome sequencing.";
RL Submitted (MAY-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|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP015772; ANH81115.1; -; Genomic_DNA.
DR RefSeq; WP_067754798.1; NZ_CP015772.1.
DR AlphaFoldDB; A0A1A9I1A6; -.
DR STRING; 1176587.A8C56_09100; -.
DR KEGG; nia:A8C56_09100; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000077667; Chromosome.
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:UP000077667};
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 11..300
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 115..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 460 AA; 51492 MW; 7C8F97B76E75CFC9 CRC64;
MQLPPTLIRS LEGLPGFDEK AFIDVHNANA PVTSVRLNPL KTTHVQLLTE GRQISAAKVP
WSVYGYYLDQ RPSFTFDPLF HAGTYYVQEA SSLFLEEALR QTVDLKEDLK ILDLCAAPGG
KSTHLQSLIA ANSLLVSNEV IRSRASVLRD NIVKWGASNV AVTNNDPKDF ARLPGFFDVV
VVDAPCSGSG LFRRDSEAIE EWSENNVMLC SQRQQRILAD VLPALKQGGV LVYSTCSYSR
QEDEAVLQWL AGTFDLEPVT LQLNPAWNII ETQSGPHTGY RFWPHLLKGE GLFMTVLRKN
AAAGTTGKYR PKTKALSAKA AAPLGQWLQA EGSRFVNFGD KIYAWPEPLF EWLDFLAQQL
KIIYSGTLAG EMIRDKLIPD HALAMSPLIT KDAARLTLSE EDAIRYLQRK ELADTVPVSR
GWQLAAFRGF PIGWMNVLAN RINNYYPKEL RILKEQRLNQ
//
