ID   RS5_CENSY               Reviewed;         219 AA.
AC   A0RUE7;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=30S ribosomal protein S5;
GN   Name=rps5; OrderedLocusNames=CENSYa_0328;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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   -!- 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; DP000238; ABK76964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RUE7; -.
DR   SMR; A0RUE7; -.
DR   STRING; 414004.CENSYa_0328; -.
DR   EnsemblBacteria; ABK76964; ABK76964; CENSYa_0328.
DR   KEGG; csy:CENSYa_0328; -.
DR   PATRIC; fig|414004.10.peg.293; -.
DR   HOGENOM; CLU_065898_0_1_2; -.
DR   OMA; KRGCGSW; -.
DR   Proteomes; UP000000758; Chromosome.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR000851; Ribosomal_S5.
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; IPR005711; Ribosomal_S5_euk/arc.
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; TIGR01020; uS5_euk_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..219
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000293205"
FT   DOMAIN          68..131
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00268"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  23545 MW;  D7CB1364EBA4D038 CRC64;
     MSHPQSRPGG RDGRPRRRRE PREEAPWVPK TALGKRVNAG EITSLEEIQE AGARIQESGI
     IKKLLPDLKT EVVDVGIIQK MTSNGQSTRF KAIVAAGNEN GYLGIGQGKA KQMRIAIEKA
     NNQALLNVGP IKLGCGSWEC RCDQKHSVPF KVRGKGGSVV IEILPAPRGL GLVAGGKIRR
     LLELAGLKDA YTTAKGSTPT TNSTSKAVLE CLRQTFSQG