ID A0A1H8BAV7_9BACT Unreviewed; 389 AA.
AC A0A1H8BAV7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SEM80111.1};
GN ORFNames=SAMN04488505_106185 {ECO:0000313|EMBL:SEM80111.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEM80111.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEM80111.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEM80111.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; FOBB01000006; SEM80111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8BAV7; -.
DR STRING; 573321.SAMN04488505_106185; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000198984; 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; 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; 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:SF77; SUN PROTEIN; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 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:UP000198984};
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 122..389
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 389 AA; 43982 MW; 69C4281EE68E6D71 CRC64;
MTRWENYLLS AEKIVTTYDG SLPLHHFLKP FFKQNPQMGS RDRRWISQLA YAFYRLGHLW
KNEMPVKDRL LLGLFLCETQ SNEILALLKP EWNEQVTLPV AEKLSAVSFN GQSPTPNDIF
PFTASLSEGI DAVAFANAYF VQPRLFIRVR KNKQEAITAL LQDAGVTGEW LADDMLALSN
GTNIETIIKN KDWYEIQDAS SQQTGQLFTP KPGQRWWDAC AASGGKSLLL MDKEPRVQLT
VSDVRVSILQ NLYERFYTAG IKNYETKALD LTLPVPPKTL DYGSFDGIIL DAPCTGSGTW
GRSPEHLYFF EETRINTFHN LQKRIAENVV PLLKKGGSLI YITCSAFKQE NEAVVKHICE
HTGLQWRDGG IITGYNIGAD TMFAAKLMK
//
