(data stored in SCRATCH zone)

SWISSPROT: Q13E52_RHOPS

ID   Q13E52_RHOPS            Unreviewed;       317 AA.
AC   Q13E52;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 78.
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=RPD_0399 {ECO:0000313|EMBL:ABE37637.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37637.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37637.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37637.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine
CC       1402 (C1402) in 16S rRNA. {ECO:0000256|HAMAP-Rule:MF_01877}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine =
CC         2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42924, Rhea:RHEA-COMP:10285,
CC         Rhea:RHEA-COMP:10286, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC         EC=2.1.1.198; 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
CC       family. {ECO:0000256|HAMAP-Rule:MF_01877}.
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DR   EMBL; CP000283; ABE37637.1; -; Genomic_DNA.
DR   RefSeq; WP_011500825.1; NC_007958.1.
DR   STRING; 316057.RPD_0399; -.
DR   EnsemblBacteria; ABE37637; ABE37637; RPD_0399.
DR   KEGG; rpd:RPD_0399; -.
DR   eggNOG; ENOG4105CU0; Bacteria.
DR   eggNOG; COG0313; LUCA.
DR   HOGENOM; HOG000195941; -.
DR   KO; K07056; -.
DR   OMA; RTMVFFE; -.
DR   OrthoDB; 1059309at2; -.
DR   BioCyc; RPAL316057:RPD_RS02055-MONOMER; -.
DR   Proteomes; UP000001818; 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   GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR   CDD; cd11648; RsmI; 1.
DR   Gene3D; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 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   PANTHER; PTHR46111; PTHR46111; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF005917; MTase_YraL; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR00096; TIGR00096; 1.
DR   PROSITE; PS01296; RSMI; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13E52.
DR   SWISS-2DPAGE; Q13E52.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01877};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01877};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01877};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01877};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01877}.
FT   DOMAIN       38    237       TP_methylase. {ECO:0000259|Pfam:PF00590}.
SQ   SEQUENCE   317 AA;  34052 MW;  5A8686A992F0803E CRC64;
     MRAKAAPTIP STTESEPESR AFLVAGQKLI APRAAPGLHL VATPIGNLGD ITLRALETLA
     GVDVIACEDT RITHRLTERY GISAQLKPYH EHNAAQARPK ILKKLAQGGS VALVSDAGTP
     LISDPGYKLV REAYDAGHDV VALPGASAVL AALALAALPT DRFFFDGFLP AKQGARRSRL
     SELAAIDATL VLFEAGSRIH NSLRDLAEVL GGREAAICRE LTKLHQEVRR APLTTLAETA
     ETLETRGEFV VVIGPPDPGA RMMTQDALDT WLRDALQRDS VKDAVAQAVD ISGRPRREIY
     ARALELARQR EADDGQD
//

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