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RSMI_TREPA
ID   RSMI_TREPA              Reviewed;         274 AA.
AC   O83940;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase I {ECO:0000255|HAMAP-Rule:MF_01877};
DE            EC=2.1.1.198 {ECO:0000255|HAMAP-Rule:MF_01877};
DE   AltName: Full=16S rRNA 2'-O-ribose C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01877};
DE   AltName: Full=rRNA (cytidine-2'-O-)-methyltransferase RsmI {ECO:0000255|HAMAP-Rule:MF_01877};
GN   Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877}; OrderedLocusNames=TP_0975;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402
CC       (C1402) in 16S rRNA. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01877};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01877}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmI family.
CC       {ECO:0000255|HAMAP-Rule:MF_01877}.
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DR   EMBL; AE000520; AAC65931.1; -; Genomic_DNA.
DR   PIR; E71257; E71257.
DR   RefSeq; WP_010882419.1; NC_021490.2.
DR   AlphaFoldDB; O83940; -.
DR   SMR; O83940; -.
DR   STRING; 243276.TPANIC_0975; -.
DR   EnsemblBacteria; AAC65931; AAC65931; TP_0975.
DR   GeneID; 57879484; -.
DR   KEGG; tpa:TP_0975; -.
DR   eggNOG; COG0313; Bacteria.
DR   HOGENOM; CLU_044779_4_0_12; -.
DR   OMA; RTMVFFE; -.
DR   OrthoDB; 1059309at2; -.
DR   Proteomes; UP000000811; 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; -; 2.
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; 2.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF005917; MTase_YraL; 1.
DR   SUPFAM; SSF53790; SSF53790; 2.
DR   PROSITE; PS01296; RSMI; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..274
FT                   /note="Ribosomal RNA small subunit methyltransferase I"
FT                   /id="PRO_0000211960"
SQ   SEQUENCE   274 AA;  29532 MW;  4596A0E7067D12B2 CRC64;
     MGTLYVVATP IGNLADITLR ALDVLRTVDV VACEDTRRTR ALLSHFGIHK RLVSCRAHNE
     AQAARRLIHF LSTPISAFLS PEKGRGRQSA RRTRARPGET VGTAALQLAA EATGEQEVCG
     SPHAQVAYVS DAGTPGVSDP GAVLVRAVRD AGHTVVPIPG ASALTTLLSV AGVRDKTVLF
     EGFLSPHPGR RRARLVQLCA QRVAFVLYES PYRVQKLLED LVAVAPESQV VLGRELTKVH
     EELCVGTALR VMESFCARTR VRGECVLLVS AEKF
 
 
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