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RR4_CYAM1
ID   RR4_CYAM1               Reviewed;         190 AA.
AC   O22020;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ohta N., Sato N., Ueda K., Kuroiwa T.;
RT   "Analysis of a plastid gene cluster reveals a close relationship between
RT   Cyanidioschyzon and Cyanidium.";
RL   J. Plant Res. 110:235-245(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC       {ECO:0000250}.
CC   -!- FUNCTION: With S5 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC       interaction surface between S4 and S5 is involved in control of
CC       translational fidelity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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DR   EMBL; D63675; BAA22816.1; -; Genomic_DNA.
DR   EMBL; AB002583; BAC76103.1; -; Genomic_DNA.
DR   RefSeq; NP_848941.1; NC_004799.1.
DR   AlphaFoldDB; O22020; -.
DR   SMR; O22020; -.
DR   STRING; 45157.CMV009CT; -.
DR   GeneID; 845011; -.
DR   KEGG; cme:CymeCp009; -.
DR   eggNOG; KOG3301; Eukaryota.
DR   HOGENOM; CLU_092403_0_1_1; -.
DR   Proteomes; UP000007014; Chloroplast.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
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   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; -; 1.
DR   HAMAP; MF_01306_B; Ribosomal_S4_B; 1.
DR   InterPro; IPR022801; Ribosomal_S4/S9.
DR   InterPro; IPR001912; Ribosomal_S4/S9_N.
DR   InterPro; IPR005709; Ribosomal_S4_bac-type.
DR   InterPro; IPR018079; Ribosomal_S4_CS.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   PANTHER; PTHR11831; PTHR11831; 1.
DR   Pfam; PF00163; Ribosomal_S4; 1.
DR   Pfam; PF01479; S4; 1.
DR   SMART; SM01390; Ribosomal_S4; 1.
DR   SMART; SM00363; S4; 1.
DR   TIGRFAMs; TIGR01017; rpsD_bact; 1.
DR   PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Plastid; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..190
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000132563"
FT   DOMAIN          92..152
FT                   /note="S4 RNA-binding"
FT   CONFLICT        14
FT                   /note="R -> RR (in Ref. 1; BAA22816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="V -> G (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="E -> G (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  21574 MW;  05FE6C0983410762 CRC64;
     MSRYLGPRVR IIRRLGILPA FTNKSPNKRT GVPGEHAHKT RKLSEYAGVL QGEQKLQYYY
     GITNNQLARY FRQAKKSRAS TGIELLKMLE TRLDHVVYRA GFAPTLPAAR QLVNHGHVKV
     NGNQVTIASF ACQVNHIIEV KAKSPSSAQL PPYLQVENQF VKMIQPVEKD WLAFRVNELL
     VVEYYTRVGA
 
 
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