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RL9_THETH
ID   RL9_THETH               Reviewed;         148 AA.
AC   P27151; Q9LCY9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=50S ribosomal protein L9 {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Name=rplI {ECO:0000255|HAMAP-Rule:MF_00503};
GN   Synonyms=rpl9 {ECO:0000255|HAMAP-Rule:MF_00503};
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VK1;
RA   Shcherbakov D.V., Cherepanova E.A., Garber M.B.;
RT   "Sequencing and analysis of the Thermus thermophilus gene cluster
RT   equivalent to the S6 operon.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-35.
RC   STRAIN=VK1;
RX   PubMed=1637860; DOI=10.1016/0300-9084(92)90110-z;
RA   Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V.,
RA   Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A.,
RA   Svensson L.A.;
RT   "Ribosomal proteins from Thermus thermophilus for structural
RT   investigations.";
RL   Biochimie 74:327-336(1992).
CC   -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_00503}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00503}.
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DR   EMBL; AF146075; AAF27298.1; -; Genomic_DNA.
DR   PIR; E48401; E48401.
DR   AlphaFoldDB; P27151; -.
DR   SMR; P27151; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.430.100; -; 1.
DR   Gene3D; 3.40.5.10; -; 1.
DR   HAMAP; MF_00503; Ribosomal_L9; 1.
DR   InterPro; IPR000244; Ribosomal_L9.
DR   InterPro; IPR009027; Ribosomal_L9/RNase_H1_N.
DR   InterPro; IPR020594; Ribosomal_L9_bac/chp.
DR   InterPro; IPR020069; Ribosomal_L9_C.
DR   InterPro; IPR036791; Ribosomal_L9_C_sf.
DR   InterPro; IPR020070; Ribosomal_L9_N.
DR   InterPro; IPR036935; Ribosomal_L9_N_sf.
DR   PANTHER; PTHR21368; PTHR21368; 1.
DR   Pfam; PF03948; Ribosomal_L9_C; 1.
DR   Pfam; PF01281; Ribosomal_L9_N; 1.
DR   SUPFAM; SSF55653; SSF55653; 1.
DR   SUPFAM; SSF55658; SSF55658; 1.
DR   TIGRFAMs; TIGR00158; L9; 1.
DR   PROSITE; PS00651; RIBOSOMAL_L9; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..148
FT                   /note="50S ribosomal protein L9"
FT                   /id="PRO_0000176697"
FT   CONFLICT        1
FT                   /note="M -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="D -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23..25
FT                   /note="PGY -> RGT (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="L -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   148 AA;  16396 MW;  48ADD134F3506794 CRC64;
     MKVILLEPLE NLGDVGQVVD VKPGYARNYL LPRGLAVLAT ESNLKALEAR IRAQAKRLAE
     RKAEAERLKK ILENLTLTIP VRAGETKIYG SVTAKDIAEA LSRQHGVTID PKRLALEKPI
     KELGEYVLTY KPHPEVPIQL KVSVVAQE
 
 
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