RR4_EUGGR
ID RR4_EUGGR Reviewed; 205 AA.
AC P27418;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4;
OS Euglena gracilis.
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=1909420; DOI=10.1007/bf00282464;
RA Stevenson J.K., Drager R.G., Copertino D.W., Christopher D.A.,
RA Jenkins K.P., Yepiz-Plascencia G., Hallick R.B.;
RT "Intercistronic group III introns in polycistronic ribosomal protein
RT operons of chloroplasts.";
RL Mol. Gen. Genet. 228:183-192(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA Spielmann A., Stutz E.;
RT "Complete sequence of Euglena gracilis chloroplast DNA.";
RL Nucleic Acids Res. 21:3537-3544(1993).
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; Z11874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M22010; AAA84230.1; -; Genomic_DNA.
DR EMBL; X70810; CAA50134.1; -; Genomic_DNA.
DR PIR; S34919; S34919.
DR RefSeq; NP_041947.1; NC_001603.2.
DR AlphaFoldDB; P27418; -.
DR SMR; P27418; -.
DR GeneID; 807517; -.
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..205
FT /note="30S ribosomal protein S4, chloroplastic"
FT /id="PRO_0000132584"
FT DOMAIN 93..161
FT /note="S4 RNA-binding"
FT REGION 16..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 205 AA; 23696 MW; AD32C99FB1808DFA CRC64;
MSRYRGPRLR IVRRIGKLPS LTNKTSKKRK SPGQPATSFK RKKKISKYNI RLKEKQKLRF
NYGITERQLL NYVKKSRKKK GSSGRFLLTF LEMRLDNIVH RIGFAPTIMA AKQLINHGHI
CVDDKVINIP SFICQPKSII KPKKSTVSEN VIQKNIESKE LLLIPPHLSL NKKNLEAKII
GLINRKAISL IVNELLVIEF YSRKV
