RSMF_SHIDS
ID RSMF_SHIDS Reviewed; 479 AA.
AC Q32F19;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase F {ECO:0000255|HAMAP-Rule:MF_01579};
DE EC=2.1.1.178 {ECO:0000255|HAMAP-Rule:MF_01579};
DE AltName: Full=16S rRNA m5C1407 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01579};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmF {ECO:0000255|HAMAP-Rule:MF_01579};
GN Name=rsmF {ECO:0000255|HAMAP-Rule:MF_01579}; OrderedLocusNames=SDY_1986;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Specifically methylates the cytosine at position 1407
CC (m5C1407) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01579}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1407) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(1407) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42756, Rhea:RHEA-COMP:10223, Rhea:RHEA-COMP:10224,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.178;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01579};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01579}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|HAMAP-Rule:MF_01579}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB62086.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB62086.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_403577.1; NC_007606.1.
DR AlphaFoldDB; Q32F19; -.
DR SMR; Q32F19; -.
DR STRING; 300267.SDY_1986; -.
DR EnsemblBacteria; ABB62086; ABB62086; SDY_1986.
DR KEGG; sdy:SDY_1986; -.
DR PATRIC; fig|300267.13.peg.2397; -.
DR HOGENOM; CLU_005316_6_2_6; -.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01579; 16SrRNA_methyltr_F; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023545; rRNA_ssu_MeTfrase_F.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 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; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..479
FT /note="Ribosomal RNA small subunit methyltransferase F"
FT /id="PRO_0000285018"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 125..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
SQ SEQUENCE 479 AA; 53384 MW; F3843CDBBAA553F4 CRC64;
MAQHTVYFPD AFLTQMREAM PSTPSFDDFL AACQRPLRRS IRVNTLKISV ADFLRLTAPY
GWTLTPIPWC EEGFWIERDN EDALPLGSTA EHLSGLFYIQ EASSMLPVAA LFADGNAPQR
VMDIAAAPGS KTTQIAARMN NEGTILANEF SASRVKVLHA NISRCGISNV ALTHFDGRVF
GAAVPEMFDA ILLDAPCSGE GVVRKDPDAL KNWSPESNQE IAATQRELID SAFHALRLGG
TLVYSTCTLN REENEAVCLW LKETYPDAVE FLPLGDLFPG TNKALTEEGF LHVFPQIYDC
EGFFVARLRK TQAIPALPTP KYKVGNFPFS PVKDREAGQI RQAAASVGLN WDENLRPWQR
DKELWLFPVG IEALIGKVRF SRLGIKLAET HNKGYRWQHE AVIALASPDN ENAFELTPQE
AEEWYRGRDV YPQAAPVADD VLVTFQHQPI GLAKRIGSRL KNSYPRELVR DGKLFTSNA
