ID RR4_SACHY Reviewed; 201 AA.
AC Q6L397;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=Small ribosomal subunit protein uS4c {ECO:0000305};
DE AltName: Full=30S ribosomal protein S4, chloroplastic;
GN Name=rps4; OrderedLocusNames=PS120;
OS Saccharum hybrid (Sugarcane).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum.
OX NCBI_TaxID=15819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SP-80-3280;
RX PubMed=15526204; DOI=10.1007/s00294-004-0542-4;
RA Calsa T. Jr., Carraro D.M., Benatti M.R., Barbosa A.C., Kitajima J.P.,
RA Carrer H.;
RT "Structural features and transcript-editing analysis of sugarcane
RT (Saccharum officinarum L.) chloroplast genome.";
RL Curr. Genet. 46:366-373(2004).
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; AE009947; AAT44695.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6L397; -.
DR SMR; Q6L397; -.
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; RNA-binding S4 domain; 1.
DR HAMAP; MF_01306_B; Ribosomal_uS4_B; 1.
DR InterPro; IPR022801; Ribosomal_uS4.
DR InterPro; IPR005709; Ribosomal_uS4_bac-type.
DR InterPro; IPR018079; Ribosomal_uS4_CS.
DR InterPro; IPR001912; Ribosomal_uS4_N.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR NCBIfam; TIGR01017; rpsD_bact; 1.
DR PANTHER; PTHR11831; 30S 40S RIBOSOMAL PROTEIN; 1.
DR PANTHER; PTHR11831:SF4; 37S RIBOSOMAL PROTEIN NAM9, MITOCHONDRIAL; 1.
DR Pfam; PF00163; Ribosomal_S4; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 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="Small ribosomal subunit protein uS4c"
FT /id="PRO_0000132662"
FT DOMAIN 89..150
FT /note="S4 RNA-binding"
FT REGION 15..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 23463 MW; 8D796F1499057BB5 CRC64;
MSRYRGPRLK KIRRLGALPG LTRKTPKSGS NQKKKFHSGK KEQYRIRLQE KQKLRFHYGL
TERQLLRYVH IAGKAKRSTG QVLLQLLEMR LDNILFRLGM ASTIPGARQL VNHRHILVNG
RIVDIPSFRC KPRDIITTKD NQRSKRLVQN YIASSDPGKL PKHLTVDTLQ YKGLVKKILD
RKWVGLKINE LLVVEYYSRQ T
//
