RR4_VITVI
ID RR4_VITVI Reviewed; 201 AA.
AC Q0ZJ18;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4;
OS Vitis vinifera (Grape).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Maxxa;
RX PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA Daniell H.;
RT "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT genome sequences: effects of taxon sampling and phylogenetic methods on
RT resolving relationships among rosids.";
RL BMC Evol. Biol. 6:32-32(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; DQ424856; ABE47536.1; -; Genomic_DNA.
DR RefSeq; YP_567078.1; NC_007957.1.
DR AlphaFoldDB; Q0ZJ18; -.
DR SMR; Q0ZJ18; -.
DR STRING; 29760.VIT_14s0030g00680.t01; -.
DR GeneID; 4025094; -.
DR KEGG; vvi:4025094; -.
DR eggNOG; KOG3301; Eukaryota.
DR InParanoid; Q0ZJ18; -.
DR OrthoDB; 1507367at2759; -.
DR Proteomes; UP000009183; Chloroplast.
DR ExpressionAtlas; Q0ZJ18; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
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..201
FT /note="30S ribosomal protein S4, chloroplastic"
FT /id="PRO_0000277022"
FT DOMAIN 89..149
FT /note="S4 RNA-binding"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 23240 MW; C44B85616418CC6E CRC64;
MSRYRGPRFK KIRRLGALPG LTSKRPRAGS DLRNQSRSGK RSQYRIRLEE KQKLRFHYGL
TERQLLNYVR IAGKAKGATG RVLLQLLEMR LDNILFRLGM ASTIPGARQL VNHRHILVNG
RIVDIPSYRC KPRDIITAGN EQKSRALIQN VFDSSSHEEL PKHLTLHPFQ FKGLVNQIID
SNWVGLKINE LLVVEYYSRQ T