RR4_WELMI
ID RR4_WELMI Reviewed; 201 AA.
AC B2Y1V2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4;
OS Welwitschia mirabilis (Tree tumbo) (Welwitschia bainesii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Gnetopsida; Gnetidae; Welwitschiales; Welwitschiaceae;
OC Welwitschia.
OX NCBI_TaxID=3377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18452621; DOI=10.1186/1471-2148-8-130;
RA McCoy S.R., Kuehl J.V., Boore J.L., Raubeson L.A.;
RT "The complete plastid genome sequence of Welwitschia mirabilis: an
RT unusually compact plastome with accelerated divergence rates.";
RL BMC Evol. Biol. 8:130-130(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19166950; DOI=10.1016/j.ympev.2008.12.026;
RA Wu C.-S., Lai Y.-T., Lin C.-P., Wang Y.-N., Chaw S.-M.;
RT "Evolution of reduced and compact chloroplast genomes (cpDNAs) in
RT gnetophytes: Selection toward a lower-cost strategy.";
RL Mol. Phylogenet. Evol. 52:115-124(2009).
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; EU342371; ABY26782.1; -; Genomic_DNA.
DR EMBL; AP009568; BAH11236.1; -; Genomic_DNA.
DR RefSeq; YP_001876569.1; NC_010654.1.
DR AlphaFoldDB; B2Y1V2; -.
DR SMR; B2Y1V2; -.
DR GeneID; 6276222; -.
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; 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; 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_1000165373"
FT DOMAIN 91..151
FT /note="S4 RNA-binding"
SQ SEQUENCE 201 AA; 24065 MW; 9B42A9544F7EB793 CRC64;
MSRYLGPRFK IIRRLKTLPG LTSKRPKYKK RVRRRFSRPW WKKSQHLICL QEKQKIRFHY
GLTERQLRQY INIAKRAQGS TGQVLLQLLE MRLDNIIFQL GIARTIPAAR QIVNHRHVLV
NGRVVDIPSY RCKPQDVLTI KTKNPEELRT IINKNRSKFR RKVPYHLTLD LAQNKGIVNK
IIDRKDIQLK IQEMLVIEYY C