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Database: UniProt
Entry: A8A133
LinkDB: A8A133
Original site: A8A133 
ID   RSMF_ECOHS              Reviewed;         479 AA.
AC   A8A133;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   11-JUN-2014, entry version 47.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase F;
DE            EC=2.1.1.178;
DE   AltName: Full=16S rRNA m5C1407 methyltransferase;
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmF;
GN   Name=rsmF; OrderedLocusNames=EcHS_A1926;
OS   Escherichia coli O9:H4 (strain HS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS;
RX   PubMed=18676672; DOI=10.1128/JB.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic
RT   analysis of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 1407
CC       (m5C1407) of 16S rRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(1407) in
CC       16S rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(1407) in
CC       16S rRNA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABV06237.1; Type=Erroneous initiation;
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DR   EMBL; CP000802; ABV06237.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001458620.1; NC_009800.1.
DR   ProteinModelPortal; A8A133; -.
DR   SMR; A8A133; 7-474.
DR   STRING; 331112.EcHS_A1926; -.
DR   EnsemblBacteria; ABV06237; ABV06237; EcHS_A1926.
DR   GeneID; 5592630; -.
DR   KEGG; ecx:EcHS_A1926; -.
DR   PATRIC; 18313834; VBIEscCol77814_1888.
DR   eggNOG; COG0144; -.
DR   HOGENOM; HOG000218115; -.
DR   KO; K11392; -.
DR   OrthoDB; EOG6091D0; -.
DR   BioCyc; ECOL331112:GHHI-1916-MONOMER; -.
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-HAMAP.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01579; 16SrRNA_methyltr_F; 1.
DR   InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023545; rRNA_ssu_MeTfrase_F.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   Pfam; PF01189; Nol1_Nop2_Fmu; 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   Complete proteome; Cytoplasm; Methyltransferase; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    479       Ribosomal RNA small subunit
FT                                methyltransferase F.
FT                                /FTId=PRO_0000382571.
FT   REGION      125    131       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   ACT_SITE    247    247       Nucleophile (By similarity).
FT   BINDING     149    149       S-adenosyl-L-methionine (By similarity).
FT   BINDING     176    176       S-adenosyl-L-methionine (By similarity).
FT   BINDING     194    194       S-adenosyl-L-methionine (By similarity).
SQ   SEQUENCE   479 AA;  53296 MW;  FE9AEC488D6E902D CRC64;
     MAQHTVYFPD AFLTQMREAM PSTLSFDDFL AACQRPLRRS IRVNTLKISV ADFLQLTAPY
     GWTLTPIPWC EEGFWIERDN EDALPLGSTA EHLSGLFYIQ EASSMLPVAA LFADGNAPQR
     VMDVAAAPGS KTTQIAARMN NEGAILANEF SASRVKVLHA NISRCGISNV ALTHFDGRVF
     GVAVPEMFDA ILLDAPCSGE GVVRKDPDAL KNWSPESNQE IAATQRELID SAFHALRPGG
     TLVYSTCTLN REENEAVCMW LKETYPDAVE FLPLGELFPA ANKALTEEGF LHVFPQIYDC
     EGFFVARLRK TQAIPALPAP KYKVGNFPFS PVKDREAGQI RQAAAGVGLN WDENLRLWQR
     DKELWLFPVG IEALIGKVRF SRLGIKLAET HNKGYRWQHE AVIALATPDN VNAFELTPQE
     AEEWYRGRDV YPQAAPVADD VLVTFQHQPI GLAKRIGSRL KNSYPRELVR DGKLFTSNA
//
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