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Database: UniProt
Entry: Q5E2P1_ALIF1
LinkDB: Q5E2P1_ALIF1
Original site: Q5E2P1_ALIF1 
ID   Q5E2P1_ALIF1            Unreviewed;       309 AA.
AC   Q5E2P1;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=yraL {ECO:0000313|EMBL:AAW86705.1};
GN   Synonyms=rsmI {ECO:0000256|HAMAP-Rule:MF_01877};
GN   OrderedLocusNames=VF_2210 {ECO:0000313|EMBL:AAW86705.1};
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309 {ECO:0000313|EMBL:AAW86705.1, ECO:0000313|Proteomes:UP000000537};
RN   [1] {ECO:0000313|EMBL:AAW86705.1, ECO:0000313|Proteomes:UP000000537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114 {ECO:0000313|Proteomes:UP000000537};
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86705.1; -; Genomic_DNA.
DR   RefSeq; YP_205593.1; NC_006840.2.
DR   AlphaFoldDB; Q5E2P1; -.
DR   STRING; 312309.VF_2210; -.
DR   EnsemblBacteria; AAW86705; AAW86705; VF_2210.
DR   KEGG; vfi:VF_2210; -.
DR   PATRIC; fig|312309.11.peg.2249; -.
DR   eggNOG; COG0313; Bacteria.
DR   HOGENOM; CLU_044779_2_0_6; -.
DR   OrthoDB; 9809084at2; -.
DR   Proteomes; UP000000537; Chromosome I.
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:UP000000537};
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          35..235
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   309 AA;  34367 MW;  AD587226BDAAB5B8 CRC64;
     MKQCIIKIGI IPYINRRRDS KQMTEHNLSV VNTATLYIVP TPIGNLGDIT QRAIEVLKSV
     DLIAAEDTRH TGKLLSHFGI ASQTFALHDH NEQHKADLLI SKLQQGLSIA LVSDAGTPLI
     SDPGYHLVNR CRQANVNVVP LPGACAVITA LSAAGLPSDR FSFEGFLPPK SKGRRDKFEE
     IAQAERTCIF YESPHRIMDS LDDMLTVLGP ERQVVLAREL TKTYETIHGA PLGELIEWIK
     EDDNRKRGEM VLLIHGFRSE AKDELPFEAT RSLSILVKEL PLKKAAAMAA EIHGVKKNAL
     YKWGLEHLD
//
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