ID   RR5_CYACA               Reviewed;         168 AA.
AC   Q9TLU8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=30S ribosomal protein S5, chloroplastic;
GN   Name=rps5;
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 88-168.
RC   STRAIN=RK-1;
RX   PubMed=8980520; DOI=10.1007/bf00020209;
RA   Vogel H., Fischer S., Valentin K.-U.;
RT   "A model for the evolution of the plastid sec apparatus inferred from secY
RT   gene phylogeny.";
RL   Plant Mol. Biol. 32:685-692(1996).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The N-terminal domain interacts with the head of the 30S
CC       subunit; the C-terminal domain interacts with the body and contacts
CC       protein S4. The interaction surface between S4 and S5 is involved in
CC       control of translational fidelity.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC       {ECO:0000305}.
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DR   EMBL; AF022186; AAF12923.1; -; Genomic_DNA.
DR   RefSeq; NP_045171.1; NC_001840.1.
DR   AlphaFoldDB; Q9TLU8; -.
DR   SMR; Q9TLU8; -.
DR   GeneID; 800242; -.
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   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_B; Ribosomal_S5_B; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005712; Ribosomal_S5_bac-type.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   PANTHER; PTHR13718; PTHR13718; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01021; rpsE_bact; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..168
FT                   /note="30S ribosomal protein S5, chloroplastic"
FT                   /id="PRO_0000131666"
FT   DOMAIN          17..80
FT                   /note="S5 DRBM"
SQ   SEQUENCE   168 AA;  17516 MW;  4EF080B9276E413C CRC64;
     MSRDTSANSS GQQNYTWSER VIQITRVTKV VKGGKKLSFR AIIVIGNNQG SVGVGVGKAS
     DVIGAVKKGV SDCKKQIIEF PLTSSSTISH AVEGRFGAAS VILKPSVQGS GVIAGGAMRT
     VIELSGIKNI VAKQLGTKNH LNNAKATINA LSKLNSKSSQ LSLMSFSN