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RSMI_MICOL
ID   RSMI_MICOL              Reviewed;         313 AA.
AC   Q08329;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 76.
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};
DE   Flags: Fragment;
GN   Name=rsmI {ECO:0000255|HAMAP-Rule:MF_01877};
OS   Micromonospora olivasterospora.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Micromonospora.
OX   NCBI_TaxID=1880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8486289; DOI=10.1016/0378-1119(93)90617-c;
RA   Ohta T., Hasegawa M.;
RT   "Analysis of the self-defense gene (fmrO) of a fortimicin A (astromicin)
RT   producer, Micromonospora olivasterospora: comparison with other
RT   aminoglycoside-resistance-encoding genes.";
RL   Gene 127:63-69(1993).
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; D13171; BAA02452.1; -; Genomic_DNA.
DR   PIR; PN0543; PN0543.
DR   AlphaFoldDB; Q08329; -.
DR   SMR; Q08329; -.
DR   PRIDE; Q08329; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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;
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..>313
FT                   /note="Ribosomal RNA small subunit methyltransferase I"
FT                   /id="PRO_0000211964"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         313
SQ   SEQUENCE   313 AA;  33906 MW;  E0192C23B9024F37 CRC64;
     MASIQLARTT RGGDGVARAD GTRQADEAGS GTLYLVPTPI GNPGDITLRA IEVLRRVGVV
     ASEDTRHTYR LFQSLEIDAR LVSYHDHNEE SRSRQLLGLL REGTDVALVS DAGTPLVNDP
     GYRLVAAAVE ADVPVRPLPG ATASVTALIG SGMPNHQFHY VGFLPRKEAA RRAALTALRS
     TPATLIFFEA PHRIVAMLAD LAAVLGDRPA ALARNLTKDD EEFLRGRLNE LTARLRVEQV
     VRGQFTVVVA GSPEAHADED RALAARLTET LVRHGAEARL IREVVREVTG LPRNWVYEQV
     RLATERSGPL GNS
 
 
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