ID D2RIY2_ACIFV Unreviewed; 276 AA.
AC D2RIY2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=Acfer_0640 {ECO:0000313|EMBL:ADB47034.1};
OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS 106432 / VR4).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB47034.1, ECO:0000313|Proteomes:UP000001902};
RN [1] {ECO:0000313|EMBL:ADB47034.1, ECO:0000313|Proteomes:UP000001902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC {ECO:0000313|Proteomes:UP000001902};
RX PubMed=21304687; DOI=10.4056/sigs.1002553;
RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acidaminococcus fermentans type strain
RT (VR4).";
RL Stand. Genomic Sci. 3:1-14(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001859; ADB47034.1; -; Genomic_DNA.
DR RefSeq; WP_012938024.1; NZ_CP085936.1.
DR AlphaFoldDB; D2RIY2; -.
DR STRING; 591001.Acfer_0640; -.
DR GeneID; 78334395; -.
DR KEGG; afn:Acfer_0640; -.
DR eggNOG; COG0313; Bacteria.
DR HOGENOM; CLU_044779_4_0_9; -.
DR OrthoDB; 9809084at2; -.
DR Proteomes; UP000001902; 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:UP000001902};
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 7..204
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 276 AA; 30730 MW; B6E2A293E406A963 CRC64;
MENKKGTLYL CATPIGNLED MTPRAVRVLR EADLIAAEDT RHTRQLLTHF GIHGQLISYH
EHNKEKQGPV LLAALEEGKD IALVTDAGFP GISDPGEMIA QQAIAAGLPV VPVPGANACL
TALVASGLPS TPFFFGAFLP KSRKNRKEKL EEWKNIPATL VLYEAPHRIL DVLQDMEEVW
GDRKMTLGRE LTKLHEEFFR GTISTCRQHL LENPPRGEFV LVVEQGTVEK QEPQGDPLDA
VKDLMARGTD KKEALAQVAK AYKVPKRELY NRLVRE
//