ID A0A1M6VUG2_9BACT Unreviewed; 419 AA.
AC A0A1M6VUG2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:SHK85039.1};
GN ORFNames=SAMN05444266_101364 {ECO:0000313|EMBL:SHK85039.1};
OS Chitinophaga jiangningensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHK85039.1, ECO:0000313|Proteomes:UP000184420};
RN [1] {ECO:0000313|EMBL:SHK85039.1, ECO:0000313|Proteomes:UP000184420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27406 {ECO:0000313|EMBL:SHK85039.1,
RC ECO:0000313|Proteomes:UP000184420};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRBL01000001; SHK85039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6VUG2; -.
DR STRING; 1419482.SAMN05444266_101364; -.
DR Proteomes; UP000184420; 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 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:UP000184420};
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 159..419
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 271
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 419 AA; 47713 MW; C1C9FDA118FADB62 CRC64;
MRFNPRLSDG PQARCSTGKL KDAIMPYLRT MTRWESYLVS AAKVINAYKG DLPLHHFLKK
FFKQHPQMGS RDRRWISQLV YHYFRLGWWK RDMEVSERLL LGTFLCEQKS NDLLAQLQPA
WNEQIDASLA EKLQLSNAGE LTAEQLFPFT DELSEGIDAN AFALSYLNQP HFFLRIRNNR
QDKILAILKQ ANIAYELSEN RTTLALPNGT KIEELIPDKS WYEVQDASSQ QTGLLFKPSR
GQRWWDCCAA SGGKSILLKD QEPNVQLLVS DVRRSILENL QQRFAAAGVK NYEARVADLT
NPAFPGTMGN VKFDGIILDA PCSGSGTWGR TPESLAFFKK EEIQRYQDLQ KRIADNVIHF
VKPGGVLIYI TCSVFKKENE EVAAFIEANS NLRREEGGVI PGYESGADTM YAVRFRRVG
//
