ID   RR5_GUITH               Reviewed;         169 AA.
AC   O46910;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=30S ribosomal protein S5, chloroplastic;
GN   Name=rps5;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9137835; DOI=10.1080/15216549700202101;
RA   Wang S.L., Liu X.-Q., Douglas S.E.;
RT   "The large ribosomal protein gene cluster of a cryptomonad plastid: gene
RT   organization, sequence and evolutionary implications.";
RL   Biochem. Mol. Biol. Int. 41:1035-1044(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(1999).
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; AF041468; AAC35719.1; -; Genomic_DNA.
DR   RefSeq; NP_050785.1; NC_000926.1.
DR   AlphaFoldDB; O46910; -.
DR   SMR; O46910; -.
DR   GeneID; 857093; -.
DR   HOGENOM; CLU_065898_2_2_1; -.
DR   OMA; FGLHCNP; -.
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..169
FT                   /note="30S ribosomal protein S5, chloroplastic"
FT                   /id="PRO_0000131668"
FT   DOMAIN          17..80
FT                   /note="S5 DRBM"
SQ   SEQUENCE   169 AA;  17979 MW;  BFFED7F4AC326986 CRC64;
     MLNAKKSNKT KEKETDWQER VIQVRRVTKV VKGGKKLSFR AIIILGNERG QVGVGVGKAS
     DVIGAVKKAV TDGRKNLINI PLTNQNSIPH IVQGYSGAAK VIIKPSAPGS GVIAGGSVRT
     ILELAGIKNI LAKQLGSSNP LNNARAAANA LINLRTYTSV LNDRNLDLH