ID   RR4_DAUCA               Reviewed;         201 AA.
AC   Q0G9W0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=30S ribosomal protein S4, chloroplastic;
GN   Name=rps4;
OS   Daucus carota (Wild carrot).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Danvers Half-long;
RX   PubMed=16945140; DOI=10.1186/1471-2164-7-222;
RA   Ruhlman T., Lee S.-B., Jansen R.K., Hostetler J.B., Tallon L.J., Town C.D.,
RA   Daniell H.;
RT   "Complete plastid genome sequence of Daucus carota: implications for
RT   biotechnology and phylogeny of angiosperms.";
RL   BMC Genomics 7:222-222(2006).
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; DQ898156; ABI32426.1; -; Genomic_DNA.
DR   RefSeq; YP_740119.1; NC_008325.1.
DR   AlphaFoldDB; Q0G9W0; -.
DR   SMR; Q0G9W0; -.
DR   EnsemblPlants; KZM81224; KZM81224; DCAR_032486.
DR   GeneID; 4266738; -.
DR   Gramene; KZM81224; KZM81224; DCAR_032486.
DR   OMA; NVVFRMG; -.
DR   OrthoDB; 1507367at2759; -.
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; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..201
FT                   /note="30S ribosomal protein S4, chloroplastic"
FT                   /id="PRO_0000277008"
FT   DOMAIN          89..149
FT                   /note="S4 RNA-binding"
FT   REGION          15..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   201 AA;  23354 MW;  8D73FF65BD45E3CB CRC64;
     MSRYRGPRFK KIRRLGALPG LTNKRPRAGS DLRNQSRSGK KSQYRIRLEE KQKLRFHYGL
     TERQLLKYVR IAGKAKGSTG QVLLQLLEMR LDNILFRLGM ATTIPGARQL VNHRHILVNG
     RIVDIPSYRC KPRDIITARD EQNSRALIQN SFNSPSQDEM PKHLTLQPFQ YKGLVNQIID
     SKWVGLKINE LLVVEYYSRQ T