ID   RS5_METVA               Reviewed;         225 AA.
AC   P14036;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307};
OS   Methanococcus vannielii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2530355; DOI=10.1016/0022-2836(89)90167-8;
RA   Auer J., Spicker G., Boeck A.;
RT   "Organization and structure of the Methanococcus transcriptional unit
RT   homologous to the Escherichia coli 'spectinomycin operon'. Implications for
RT   the evolutionary relationship of 70 S and 80 S ribosomes.";
RL   J. Mol. Biol. 209:21-36(1989).
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}.
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DR   EMBL; X16720; CAA34700.1; -; Genomic_DNA.
DR   PIR; S05624; R3MX5.
DR   AlphaFoldDB; P14036; -.
DR   SMR; P14036; -.
DR   GeneID; 5325893; -.
DR   OMA; KRGCGSW; -.
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_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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..225
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_0000131652"
FT   DOMAIN          57..120
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ   SEQUENCE   225 AA;  24359 MW;  368FCA1439878EB4 CRC64;
     MAEKRAEKRK FNTDSWEPKT QVGRMVKEGT ISDISYIMDK GLPLLEPEIV DVLLPDLEEQ
     VLDVKLVQRM HKSGRRARYR ATVVVGNKNG YVGVGMGKSK EVGPAIRKAI AQAKLSLIKV
     RVGCGSWECG CGSPHSIPFT AKGTCGSVKV ELLPAPRGVG LVAGNVAKAV LGLAGVKDAW
     TTTYGDTRTT YNFAEATFDA LNNLNFVRCL PEQKAKLGLT EGRVL