ID A0A0G0MW47_9BACT Unreviewed; 224 AA.
AC A0A0G0MW47;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000256|HAMAP-Rule:MF_01877};
DE EC=2.1.1.198 {ECO:0000256|HAMAP-Rule:MF_01877};
DE AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01877};
DE AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN Name=rsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN ORFNames=UT30_C0005G0039 {ECO:0000313|EMBL:KKR04636.1};
OS Candidatus Uhrbacteria bacterium GW2011_GWF2_39_13.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1618995 {ECO:0000313|EMBL:KKR04636.1, ECO:0000313|Proteomes:UP000033935};
RN [1] {ECO:0000313|EMBL:KKR04636.1, ECO:0000313|Proteomes:UP000033935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC (C1402) in 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42924, Rhea:RHEA-COMP:10285, Rhea:RHEA-COMP:10286,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.198;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01877};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01877}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC {ECO:0000256|HAMAP-Rule:MF_01877}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKR04636.1}.
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DR EMBL; LBWG01000005; KKR04636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MW47; -.
DR PATRIC; fig|1618995.3.peg.298; -.
DR Proteomes; UP000033935; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070677; F:rRNA (cytosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd11648; RsmI; 1.
DR HAMAP; MF_01877; 16SrRNA_methyltr_I; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR008189; rRNA_ssu_MeTfrase_I.
DR NCBIfam; TIGR00096; 16S rRNA (cytidine(1402)-2'-O)-methyltransferase; 1.
DR PANTHER; PTHR46111; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR PANTHER; PTHR46111:SF1; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE I; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF005917; MTase_YraL; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01877};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01877};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01877};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01877}.
FT DOMAIN 3..204
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 224 AA; 24702 MW; E1815661F391D8D1 CRC64;
MATLFVVATP IGNLSDLSER AKKTLSCVQT ILCEDTRVTG KLLSVYGIHV PLLSYHQHSG
QFKTQKIIEL LEEQKDLALV TDAGTPAISD PGGKLVEELL AHFGDNLTIT PIPGPSALIA
ALSIAGVSAD EFTFLGFPPH KKGRQTFFDH LTQMSSTVVI YESTHRILKT LDEIHKRTPE
RHLIVCRELT KMYETIYRGS AQEVTVKLQS TSIKGEFVLV FSPL
//