RSMF_VIBCH
ID RSMF_VIBCH Reviewed; 473 AA.
AC Q9KRY1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 110.
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=VC_1502;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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=AAF94657.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94657.1; ALT_INIT; Genomic_DNA.
DR PIR; A82193; A82193.
DR RefSeq; NP_231143.1; NC_002505.1.
DR RefSeq; WP_000553486.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRY1; -.
DR SMR; Q9KRY1; -.
DR STRING; 243277.VC_1502; -.
DR DNASU; 2614008; -.
DR EnsemblBacteria; AAF94657; AAF94657; VC_1502.
DR GeneID; 57740162; -.
DR KEGG; vch:VC_1502; -.
DR PATRIC; fig|243277.26.peg.1429; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG3270; Bacteria.
DR HOGENOM; CLU_005316_6_2_6; -.
DR OMA; PWCAEGF; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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..473
FT /note="Ribosomal RNA small subunit methyltransferase F"
FT /id="PRO_0000285022"
FT ACT_SITE 245
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 123..129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01579"
SQ SEQUENCE 473 AA; 52559 MW; EACEE8EA70F54370 CRC64;
MHPNISLPEP FIASMAKILP DPTQLADFIA ACQRPLRKSI RVNTLKISVA EFCQRAAEKE
WQLTPVPWCE NGFWIDADES LVPLGNTAEH MAGLFYIQEA SSMMPVSALF MGNAHYDSVL
DMAAAPGSKT TQMAALMDNQ GVLVANEFSA SRVKVLHANI ERCGIRNTAL SNFDGCVFGG
WLPERFDAVL IDAPCSGEGT IRKDPDAMKN WSLESIQSIA NTQKALIESA FQALKVGGTL
VYSTCTLSRE ENQQVCWHLK QTYGDAVSFE SLGNLFEHAS LALTEEGFLH IFPQMYDCEG
FFVAKIRKLA SVPTPEVNKR LGKFPFNKAS HKQQAEIAQQ LHKSLGIELP SDAQVWLRDN
DVWLFPEALE PLLGELRFSR MGIKIAEAHK SGYRWQHQVA TCLASSSASH SVELDTTQAR
EWFMGRDVRP EGQSGQGEVI IRYANDVIGL GKWVGNRVKN GLPRELVRDK NLF
