RS5_THEKO
ID RS5_THEKO Reviewed; 235 AA.
AC Q5JJG8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307};
GN Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=TK1521;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85710.1; -; Genomic_DNA.
DR RefSeq; WP_011250472.1; NC_006624.1.
DR PDB; 6SKF; EM; 2.95 A; Ag=1-235.
DR PDB; 6SKG; EM; 2.65 A; Ag=1-235.
DR PDB; 6TH6; EM; 2.55 A; Ag=1-235.
DR PDBsum; 6SKF; -.
DR PDBsum; 6SKG; -.
DR PDBsum; 6TH6; -.
DR AlphaFoldDB; Q5JJG8; -.
DR SMR; Q5JJG8; -.
DR IntAct; Q5JJG8; 1.
DR MINT; Q5JJG8; -.
DR STRING; 69014.TK1521; -.
DR EnsemblBacteria; BAD85710; BAD85710; TK1521.
DR GeneID; 3235849; -.
DR KEGG; tko:TK1521; -.
DR PATRIC; fig|69014.16.peg.1481; -.
DR eggNOG; arCOG04087; Archaea.
DR HOGENOM; CLU_065898_0_1_2; -.
DR InParanoid; Q5JJG8; -.
DR OMA; KRGCGSW; -.
DR OrthoDB; 60954at2157; -.
DR PhylomeDB; Q5JJG8; -.
DR Proteomes; UP000000536; 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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..235
FT /note="30S ribosomal protein S5"
FT /id="PRO_0000131659"
FT DOMAIN 60..123
FT /note="S5 DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01307"
SQ SEQUENCE 235 AA; 26333 MW; E1688AB24FDBFF4C CRC64;
MSDPREIAQR VLEEWEPKTK LGRLVKEGQI TDIHEIFRKG YQIKEPEIVD VLLPEVNLRE
NQEVLDIALT VRMTDSGRRI RFRVLAAVGN RDGYVGLGIG HGREVGIAIR KAINYAKMNI
IEIKRGCGSW ECRCRRPHSI PFAVEGKEGS VRVKLMPGPR GLGLVIGDVG KKILTLAGVQ
DVWSQTLGET RTTVNFAKAV FNALYNTNRV AIKPEDIERY GIVVGRAMPT TFEVE
