ID   RSMF_SHEPA              Reviewed;         488 AA.
AC   A8H3W2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Spea_1927;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000851; ABV87249.1; -; Genomic_DNA.
DR   RefSeq; WP_012155167.1; NC_009901.1.
DR   AlphaFoldDB; A8H3W2; -.
DR   SMR; A8H3W2; -.
DR   STRING; 398579.Spea_1927; -.
DR   EnsemblBacteria; ABV87249; ABV87249; Spea_1927.
DR   KEGG; spl:Spea_1927; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   HOGENOM; CLU_005316_6_2_6; -.
DR   OMA; PWCAEGF; -.
DR   Proteomes; UP000002608; 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; 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; 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..488
FT                   /note="Ribosomal RNA small subunit methyltransferase F"
FT                   /id="PRO_1000087932"
FT   ACT_SITE        257
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         135..141
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         186
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT   BINDING         204
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
SQ   SEQUENCE   488 AA;  54754 MW;  ED2AE7152C1F00A3 CRC64;
     MAHFNQNFLD SIERDLPSHL SMEDFIAYSN KPLRLSIRVN TLKISHDNFI DLMTPKGWHF
     EPIPWCKDGF WVTLTQEIQL GNTIEHLQGL FYIQEASSML PPTALFEPLE VAVAAENTED
     DGSDDFSNKI VLDMASAPGS KTTQIAALMK NQGLLIANEY SASRVKVLHA NVARMGVANC
     ALTHFDARVF GEYMFETFDS ILLDAPCSGE GTIRKDPDAL KNWDNNDDKG IVETQKALIE
     SAFLALKVGG SLVYSTCALS RQENQDVCHH LKSLYGDAVE FGSLATLFPQ ADKACTEEGF
     LHVWPQIYDS EGFFVAKIYK TSAVERQLPE PRKQKNFPFT LAKPKQVEEL AQYFRDSFSI
     SLPDNAQVMV RDLEFWLFPS PVIPLIGKMR YQRIGIKLAD ALKKGYKVRH EAVLALSSPT
     RFELSDEQAK EFLMGRDISL LEKGKPQGEV IVSYASNPLG VAKHLGNKLK NNLPRDLVKD
     KIALYSHN