ID   RR4_EPIVI               Reviewed;         202 AA.
AC   P30056;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Plastid 30S ribosomal protein S4;
GN   Name=rps4;
OS   Epifagus virginiana (Beechdrops) (Orobanche virginiana).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Orobanchaceae; Orobancheae; Epifagus.
OX   NCBI_TaxID=4177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1332054; DOI=10.1073/pnas.89.22.10648;
RA   Wolfe K.H., Morden C.W., Palmer J.D.;
RT   "Function and evolution of a minimal plastid genome from a
RT   nonphotosynthetic parasitic plant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10648-10652(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1404416; DOI=10.1007/bf00161168;
RA   Wolfe K.H., Morden C.W., Ems S.C., Palmer J.D.;
RT   "Rapid evolution of the plastid translational apparatus in a
RT   nonphotosynthetic plant: loss or accelerated sequence evolution of tRNA and
RT   ribosomal protein genes.";
RL   J. Mol. Evol. 35:304-317(1992).
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.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC       {ECO:0000305}.
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DR   EMBL; M81884; AAA65853.1; -; Genomic_DNA.
DR   PIR; S78382; S78382.
DR   RefSeq; NP_054379.1; NC_001568.1.
DR   AlphaFoldDB; P30056; -.
DR   SMR; P30056; -.
DR   PRIDE; P30056; -.
DR   GeneID; 801419; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..202
FT                   /note="Plastid 30S ribosomal protein S4"
FT                   /id="PRO_0000132572"
FT   DOMAIN          89..152
FT                   /note="S4 RNA-binding"
SQ   SEQUENCE   202 AA;  23824 MW;  78857286516BA691 CRC64;
     MSRYRGPSLK KIRRLGALPG LTNKRSKAEN DFIKKLRSDK KSQYRIRLEE KQKLRFNYGL
     RERQLRKYFS IAIKTRGSTG KVLMQLLEMR LDNIIFRLGM ASTIPAARQL VNHRHVLVNG
     RIVDIPSYRC KSRDIIMARD EQQSNTFINN CINYSTHNRM EAPNHLTLLH PFKGLVNQII
     DSKWVGFKIN ELLVVEYYFR KT