ID A0A1I5WAT4_9FIRM Unreviewed; 442 AA.
AC A0A1I5WAT4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012140};
DE EC=2.1.1.176 {ECO:0000256|ARBA:ARBA00012140};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|ARBA:ARBA00030399};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|ARBA:ARBA00031088};
GN ORFNames=SAMN02910358_00967 {ECO:0000313|EMBL:SFQ16785.1};
OS Lachnospiraceae bacterium XBB1006.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFQ16785.1, ECO:0000313|Proteomes:UP000199554};
RN [1] {ECO:0000313|EMBL:SFQ16785.1, ECO:0000313|Proteomes:UP000199554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB1006 {ECO:0000313|EMBL:SFQ16785.1,
RC ECO:0000313|Proteomes:UP000199554};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC Evidence={ECO:0000256|ARBA:ARBA00000588};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; FOXT01000006; SFQ16785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5WAT4; -.
DR STRING; 1520827.SAMN02910358_00967; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000199554; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; 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; 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; IPR004573; rRNA_ssu_MeTfrase_B.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00563; rsmB; 1.
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; 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:UP000199554};
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 174..442
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 264..270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 340
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 442 AA; 49992 MW; 59CF05D02F1BC179 CRC64;
MTNSVNTREV ILDCLLAVTK EQAFLHVVMR DVLAKYAYLD KRDRSFISRV CHGTMERMPE
LDGIINQFSK VSVRKMKPVI RLILRSALYQ MLYMDSVPNS AAVNEAVKLA SKRGFSGLKG
FVNGVLRNID RNLATISYPS RDHFIDYMEM RYSIFPWMTK LWLTSMSEEQ VEAIGEAFLK
EGPTCVRVMT DRITPQALMK QLVEQGITVA THETREDVLY LSSYDSLGAI KQFRDGLFYV
QDPSSMEVAT VIKPKAGEIG VDVCAAPGGK SIHAAMLLKE QEQQTDKKGR IYARDLTPMK
LALIEENIAR TGMDNITAEI KDARVLDEAM VEKADFVIAD LPCSGLGVLR KKPDIKYRTS
LDNVRELAQL QQEILAVVCQ YVKPGGRLLY STCTINRIEN EENVETFLKE HSEFTRKAQQ
QLLPKDGKQD GFFYCLLEKG AK
//
