ID   RS5_PYRAE               Reviewed;         218 AA.
AC   Q8ZXN9;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=PAE1182;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- FUNCTION: With S4 and S12 plays an important role in translational
CC       accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4.
CC       {ECO:0000255|HAMAP-Rule:MF_01307}.
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:0000255|HAMAP-Rule:MF_01307}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009441; AAL63307.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZXN9; -.
DR   SMR; Q8ZXN9; -.
DR   STRING; 178306.PAE1182; -.
DR   PRIDE; Q8ZXN9; -.
DR   EnsemblBacteria; AAL63307; AAL63307; PAE1182.
DR   KEGG; pai:PAE1182; -.
DR   PATRIC; fig|178306.9.peg.873; -.
DR   eggNOG; arCOG04087; Archaea.
DR   HOGENOM; CLU_065898_0_1_2; -.
DR   InParanoid; Q8ZXN9; -.
DR   OMA; KRGCGSW; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_01307_A; Ribosomal_S5_A; 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..218
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131656"
FT   DOMAIN          66..129
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ   SEQUENCE   218 AA;  24235 MW;  B454D009FFA57606 CRC64;
     MRVKAKIFIR PLFATYVSVI DLSLWEPRTE LGRMVKEGKI RTIDEIFANN YIIKEPEIVD
     ILLPGLKQEL LNVNLVQRQT HAGERNQFQA VVAVGNEDGY VGVGIGKARQ VRQAIEKATR
     EAKLNLVPVR RGCGSWKCSC DEPHSVPFVV RGKSGSVEIT LIPAPKGVGL VAGDVAKAVL
     RLAGIKDVWT KTRGDTRTTL NFAMAVYNAL RNTYYFKI