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Database: UniProt
Entry: A0A1D8RWG2_9GAMM
LinkDB: A0A1D8RWG2_9GAMM
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ID   A0A1D8RWG2_9GAMM        Unreviewed;       348 AA.
AC   A0A1D8RWG2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase C {ECO:0000256|HAMAP-Rule:MF_01862};
DE            EC=2.1.1.172 {ECO:0000256|HAMAP-Rule:MF_01862};
DE   AltName: Full=16S rRNA m2G1207 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862};
DE   AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN   Name=rsmC {ECO:0000256|HAMAP-Rule:MF_01862};
GN   ORFNames=A3Q34_11610 {ECO:0000313|EMBL:AOW77449.1};
OS   Colwellia sp. PAMC 20917.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW77449.1, ECO:0000313|Proteomes:UP000177820};
RN   [1] {ECO:0000313|EMBL:AOW77449.1, ECO:0000313|Proteomes:UP000177820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW77449.1,
RC   ECO:0000313|Proteomes:UP000177820};
RA   Kim H.-W.;
RT   "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the guanine in position 1207 of 16S
CC       rRNA in the 30S particle. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01862};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01862}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmC family.
CC       {ECO:0000256|HAMAP-Rule:MF_01862}.
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DR   EMBL; CP014944; AOW77449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D8RWG2; -.
DR   STRING; 1816218.A3Q34_11610; -.
DR   KEGG; coz:A3Q34_11610; -.
DR   OrthoDB; 9816072at2; -.
DR   Proteomes; UP000177820; Chromosome.
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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR046977; RsmC/RlmG.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR   PANTHER; PTHR47816:SF4; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR   Pfam; PF05175; MTS; 1.
DR   Pfam; PF08468; MTS_N; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01862};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01862,
KW   ECO:0000313|EMBL:AOW77449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000177820};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01862};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01862};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01862, ECO:0000313|EMBL:AOW77449.1}.
FT   DOMAIN          11..170
FT                   /note="Methyltransferase small N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08468"
FT   DOMAIN          179..344
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
SQ   SEQUENCE   348 AA;  38703 MW;  94AF7126C45B080C CRC64;
     MRITLLDNIN QLLLRNPDLL KAKAPLFINL PIDDFFQEYH ALHAQAAMTC YNTNYQSHLQ
     AKRLDLTHMT AVFNVYYQSK AAHDLVIIQF PKSKAELTFM LAMIKDSIAN DCLVLVVGEN
     KSGIKSLAKL TEHQLGDCAK IDAARHCLLF ASNILATQES FILDNWLKPY SFMIKDTSVD
     VVALPGVFSQ NGLDIGTQVL LENLPKKITG EILDFGCGAG VIASYLGKVF PEIKLHLLDV
     SALALYSAQA TLKLNNLTGH VFPSDSLSDL KGKYDYVISN PPFHQGLKTN YQATETFLSK
     IKPHLKPKGQ VTVVANSFLR YQPIMEEAIG RTQVLAKQKG FSLYHCSI
//
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