ID A0A1X3CS86_9NEIS Unreviewed; 419 AA.
AC A0A1X3CS86;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BWD10_05300 {ECO:0000313|EMBL:OSI10468.1};
OS Neisseria zoodegmatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=326523 {ECO:0000313|EMBL:OSI10468.1, ECO:0000313|Proteomes:UP000193466};
RN [1] {ECO:0000313|EMBL:OSI10468.1, ECO:0000313|Proteomes:UP000193466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21643 {ECO:0000313|EMBL:OSI10468.1,
RC ECO:0000313|Proteomes:UP000193466};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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|ARBA:ARBA00007494,
CC 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:OSI10468.1}.
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DR EMBL; MTBM01000005; OSI10468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3CS86; -.
DR STRING; 326523.BWD10_05300; -.
DR Proteomes; UP000193466; 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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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};
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 164..419
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 252..258
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 320
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 419 AA; 46692 MW; F9E71F970F626C90 CRC64;
MSMALAQKLA ADTITAVASG QNLQDALANV RAAHPELSPQ ENGALQDIAY GCQRYGGSLR
YMLGKMLNKP ITEPKLESLL IAALYQLNHT ANAPHAVVNE AVDTAAKIGK GQYRSFTNAI
LRRFLREREK LNAGCKHNDV AKYNLPEWWV RYLQNHYPKH WHNMVAAWQQ HPPMTLRINR
RKSDAQTYLK LLAQEGIAAT ALDDYAVMLA EAVPVNRLPG FSDGLVSVQD FGAQQAGYLL
NPQNGERILD ACAAPGGKTG HILELADCNL TALDIDEGRL KRVADNLNRL NAHAEALICA
DAQDIEKWYD GRPFDAILAD VPCTASGVLK RNPDIRWLRR PGDAVKTARQ QEALLDALWQ
TLTKNGRMLL ATCSIFVEEN EQQLQKFLNR HADARCVESH VLLPNKQQDG FYYALIQKQ
//
