ID A0A2K3V218_9DEIO Unreviewed; 323 AA.
AC A0A2K3V218;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ECO:0000313|EMBL:PNY82815.1};
GN ORFNames=CVO96_02260 {ECO:0000313|EMBL:PNY82815.1};
OS Deinococcus koreensis.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2054903 {ECO:0000313|EMBL:PNY82815.1, ECO:0000313|Proteomes:UP000236379};
RN [1] {ECO:0000313|EMBL:PNY82815.1, ECO:0000313|Proteomes:UP000236379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJW1-2 {ECO:0000313|EMBL:PNY82815.1,
RC ECO:0000313|Proteomes:UP000236379};
RA Choi A.;
RT "Deinococcus koreensis sp. nov., a radiation-resistant bacterium isolated
RT from river water.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PNY82815.1}.
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DR EMBL; PPPD01000001; PNY82815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3V218; -.
DR OrthoDB; 9809084at2; -.
DR Proteomes; UP000236379; 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 InterPro; IPR018063; SAM_MeTrfase_RsmI_CS.
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.
DR PROSITE; PS01296; RSMI; 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}; Reference proteome {ECO:0000313|Proteomes:UP000236379};
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 52..249
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 33945 MW; 0A0BF54188D8D9FB CRC64;
MLEPEATEPD EPGPDHGPDP APPPDSAGLP GTQSPETHPH DRSQPVPGAG PRVWLVPTPV
GNLGDITLRA IEVLRGADAV ACEDTRRSGA LLSHLGIRKP LVRLDAHTMH RAAQVLEKHP
RLAYVSDAGT PGISDPGSEL VQAALEAGVP VEALPGATAF VPALVLSGLP TGRFTFEGFL
PRSGRERKER LGAVASRAET SVLYESPHRL GATLRDLAGA CGAGRPASVT RELSKRFEET
VRGPLSELAG HFAAEVRGEI VIVVGGQDQP VAQPQPGDQR DWAQAQAAQG HSARDIRDLL
IARGLRKNDA YALALQVTGA ETA
//
