ID   RS5_METM6               Reviewed;         229 AA.
AC   A9A9P4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN   Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=MmarC6_1254;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX02067.1; -; Genomic_DNA.
DR   RefSeq; WP_012194002.1; NC_009975.1.
DR   AlphaFoldDB; A9A9P4; -.
DR   SMR; A9A9P4; -.
DR   STRING; 444158.MmarC6_1254; -.
DR   EnsemblBacteria; ABX02067; ABX02067; MmarC6_1254.
DR   GeneID; 5738183; -.
DR   KEGG; mmx:MmarC6_1254; -.
DR   eggNOG; arCOG04087; Archaea.
DR   HOGENOM; CLU_065898_0_1_2; -.
DR   OMA; KRGCGSW; -.
DR   OrthoDB; 60954at2157; -.
DR   PhylomeDB; A9A9P4; -.
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..229
FT                   /note="30S ribosomal protein S5"
FT                   /id="PRO_1000140867"
FT   DOMAIN          61..124
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ   SEQUENCE   229 AA;  24831 MW;  440B07EB36CA850B CRC64;
     MAEKKAEKRA EKRKFNTEAW EPKTQIGRMV KEGTISDINY IMDKGLPLLE PEIVDALLPD
     LEEQVLDVKL VQRMHKSGRR ARYRATVVVG NKNGYVGVGM GKSKEVGPAI RKAIAHAKLS
     LIKVRVGCGS WECGCGSPHS IPFTAKGACG SVKVELLPAP RGVGLVAGNV AKAVLGLAGI
     KDAWTKTFGD TRTTYNFAEA TFDALNNLNF VRCLPAQKEK LGLTEGRVL