ID A0A075WUN5_9BACT Unreviewed; 280 AA.
AC A0A075WUN5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
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=HL41_08355 {ECO:0000313|EMBL:AIH04665.1};
OS Thermodesulfobacterium commune DSM 2178.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=289377 {ECO:0000313|EMBL:AIH04665.1, ECO:0000313|Proteomes:UP000028481};
RN [1] {ECO:0000313|EMBL:AIH04665.1, ECO:0000313|Proteomes:UP000028481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2178 {ECO:0000313|EMBL:AIH04665.1,
RC ECO:0000313|Proteomes:UP000028481};
RX PubMed=25635017;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of a Sulfate-Reducing Thermophilic Bacterium,
RT Thermodesulfobacterium commune DSM 2178T (Phylum Thermodesulfobacteria).";
RL Genome Announc. 3:0-0(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}.
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DR EMBL; CP008796; AIH04665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075WUN5; -.
DR STRING; 289377.HL41_08355; -.
DR PaxDb; 289377-HL41_08355; -.
DR KEGG; tcm:HL41_08355; -.
DR eggNOG; COG0313; Bacteria.
DR HOGENOM; CLU_044779_2_0_0; -.
DR Proteomes; UP000028481; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028481};
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 9..208
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 280 AA; 31498 MW; FE28786C45DFCB3D CRC64;
MMEKPKGILY VVGVPIGNLG DITLRALEVL KNTEIIVSED TRSIRKLLTH YGCGPKKLIS
LYKDVEVERT HKVLKLLEEG KEVVLTSEAG CPLISDPGAY LVREAHRRGI KIVPVPGVSA
LTCALSASGV DLSSGFIFLG FLPRKKTEQK KVLENLPENF PLIIFESPHR MEKTAKNLLE
ILGNRECFLA RELTKFHEEL TWTDLQTLAN REKFLGEITL IILPQPKTEE KPLVKKKLAG
IKKRIKELKK EGLKPKEMAK IIAEEYNIPV KEVYQLIAEG
//
