RS4_THEKO
ID RS4_THEKO Reviewed; 180 AA.
AC Q5JJF2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306};
GN Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=TK1505;
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: One of the primary rRNA binding proteins, it binds directly
CC to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- FUNCTION: With S5 and S12 plays an important role in translational
CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. The
CC interaction surface between S4 and S5 is involved in control of
CC translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS4 family.
CC {ECO:0000255|HAMAP-Rule:MF_01306}.
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; AP006878; BAD85694.1; -; Genomic_DNA.
DR RefSeq; WP_011250456.1; NC_006624.1.
DR PDB; 6SKF; EM; 2.95 A; Ae=1-180.
DR PDB; 6SKG; EM; 2.65 A; Ae=1-180.
DR PDB; 6TH6; EM; 2.55 A; Ae=1-180.
DR PDBsum; 6SKF; -.
DR PDBsum; 6SKG; -.
DR PDBsum; 6TH6; -.
DR AlphaFoldDB; Q5JJF2; -.
DR SMR; Q5JJF2; -.
DR IntAct; Q5JJF2; 1.
DR MINT; Q5JJF2; -.
DR STRING; 69014.TK1505; -.
DR EnsemblBacteria; BAD85694; BAD85694; TK1505.
DR GeneID; 3234628; -.
DR KEGG; tko:TK1505; -.
DR PATRIC; fig|69014.16.peg.1465; -.
DR eggNOG; arCOG04239; Archaea.
DR HOGENOM; CLU_089738_1_1_2; -.
DR InParanoid; Q5JJF2; -.
DR OMA; ARQFITH; -.
DR OrthoDB; 93256at2157; -.
DR PhylomeDB; Q5JJF2; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR HAMAP; MF_01306_A; Ribosomal_S4_A; 1.
DR InterPro; IPR022801; Ribosomal_S4/S9.
DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc.
DR InterPro; IPR001912; Ribosomal_S4/S9_N.
DR InterPro; IPR022802; Ribosomal_S4_arc.
DR InterPro; IPR018079; Ribosomal_S4_CS.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR PANTHER; PTHR11831; PTHR11831; 1.
DR Pfam; PF01479; S4; 1.
DR SMART; SM01390; Ribosomal_S4; 1.
DR SMART; SM00363; S4; 1.
DR TIGRFAMs; TIGR01018; uS4_arch; 1.
DR PROSITE; PS00632; RIBOSOMAL_S4; 1.
DR PROSITE; PS50889; S4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..180
FT /note="30S ribosomal protein S4"
FT /id="PRO_0000132519"
FT DOMAIN 103..165
FT /note="S4 RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01306"
SQ SEQUENCE 180 AA; 21197 MW; D983FD1232BCE2C8 CRC64;
MGDPKRQRKK YETPSHPWIK ERLDRERVLK RNYALKNKKE LWRHETQLKE FRRRARRLLA
ARGKQAEIER QQLLQRLYRL GLLPADAVLD DVLSLTVEDV LERRLQTIVY RKGLARTMKQ
ARQLIVHGHI EVNGQVIRSP GYLVLREEED TITYAKGSPF AKEGHPERMV IEQAKQGGEA
