RSMC_ALIFM
ID RSMC_ALIFM Reviewed; 339 AA.
AC B5FAM0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000255|HAMAP-Rule:MF_01862};
DE EC=2.1.1.172 {ECO:0000255|HAMAP-Rule:MF_01862};
DE AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01862};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000255|HAMAP-Rule:MF_01862};
GN Name=rsmC {ECO:0000255|HAMAP-Rule:MF_01862}; OrderedLocusNames=VFMJ11_2245;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC rRNA in the 30S particle. {ECO:0000255|HAMAP-Rule:MF_01862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1207) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1207) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42736, Rhea:RHEA-COMP:10213, Rhea:RHEA-COMP:10214,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.172;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01862};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01862}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01862}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC {ECO:0000255|HAMAP-Rule:MF_01862}.
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DR EMBL; CP001139; ACH65964.1; -; Genomic_DNA.
DR RefSeq; WP_012533401.1; NC_011184.1.
DR AlphaFoldDB; B5FAM0; -.
DR SMR; B5FAM0; -.
DR EnsemblBacteria; ACH65964; ACH65964; VFMJ11_2245.
DR KEGG; vfm:VFMJ11_2245; -.
DR HOGENOM; CLU_049581_0_1_6; -.
DR OMA; RHCQLWQ; -.
DR Proteomes; UP000001857; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052914; F:16S rRNA (guanine(1207)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 2.
DR HAMAP; MF_01862; 16SrRNA_methyltr_C; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR013675; Mtase_sm_N.
DR InterPro; IPR023543; rRNA_ssu_MeTfrase_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF05175; MTS; 1.
DR Pfam; PF08468; MTS_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..339
FT /note="Ribosomal RNA small subunit methyltransferase C"
FT /id="PRO_0000369794"
SQ SEQUENCE 339 AA; 38119 MW; E92A9C6B30EDD82B CRC64;
MSYSAPSQIT QRQLAYFEGK HVLIAGELID DFPFELAKHC ESTSIFTTNY SYYKQFAEHD
SIHCYFGSEL TETTNADMIL LYWPKAKAEA EYLLTMLLAK LGKSTEIVVV GENRSGVKSI
EKMFADFGPI NKFDSARRCS FYWGQCTEEA PTFNQQDWFK EYQVEFENHT IEVRSLPGVF
SHGEFDKGSE LLLQTLPALR GHVLDFGCGA GVIGSVMKTI NPKIHLDMVD ISALAIASSI
ETLKANNLEG CVFASDVYSD TKENYQFIVS NPPFHAGLKT HYSSTEELLE KAPQNLTHEG
QLILVANSFL QYPPIIEKAF GECLTLAKNN KFKIYSAQK