ID   RL4_THEON               Reviewed;         255 AA.
AC   B6YSL4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=TON_0067;
OS   Thermococcus onnurineus (strain NA1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1;
RX   PubMed=18790866; DOI=10.1128/jb.00746-08;
RA   Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA   Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA   Colwell R.R., Kim S.-J., Lee J.-H.;
RT   "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT   mixed heterotrophic and carboxydotrophic metabolism.";
RL   J. Bacteriol. 190:7491-7499(2008).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC       initially binds near the 5'-end of the 23S rRNA. It is important during
CC       the early stages of 50S assembly. It makes multiple contacts with
CC       different domains of the 23S rRNA in the assembled 50S subunit and
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01328}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01328}.
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DR   EMBL; CP000855; ACJ15551.1; -; Genomic_DNA.
DR   RefSeq; WP_012571024.1; NC_011529.1.
DR   AlphaFoldDB; B6YSL4; -.
DR   SMR; B6YSL4; -.
DR   STRING; 523850.TON_0067; -.
DR   EnsemblBacteria; ACJ15551; ACJ15551; TON_0067.
DR   GeneID; 7017713; -.
DR   KEGG; ton:TON_0067; -.
DR   PATRIC; fig|523850.10.peg.67; -.
DR   eggNOG; arCOG04071; Archaea.
DR   HOGENOM; CLU_026535_0_0_2; -.
DR   OMA; WHQKVNV; -.
DR   OrthoDB; 65833at2157; -.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.40.1370.10; -; 1.
DR   HAMAP; MF_01328_A; Ribosomal_L4_A; 1.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR   InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR   InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR   InterPro; IPR019970; Ribosomall_L4-archaea.
DR   PANTHER; PTHR19431; PTHR19431; 1.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   SUPFAM; SSF52166; SSF52166; 1.
DR   TIGRFAMs; TIGR03672; rpl4p_arch; 1.
DR   PROSITE; PS00939; RIBOSOMAL_L1E; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..255
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000142197"
SQ   SEQUENCE   255 AA;  28685 MW;  3EEB8B772BB78EA7 CRC64;
     MKVKVFNLEG EPVEEIELPN VFATPFRPDL IRRAVIASWT HRIQPQGRDP LAGKRRVTEN
     IGKGHGMARV ERIKTSPRFA AFVPFARGGR RTHPPKVEKI IWEDINKKER RLAIMSAIAA
     TANYDLVRAR GHIVDNVPQV PLVVVNDLEK VFKTAQTREI FKKLGVWDDI ERAKKNTKIR
     AGKGKMRGRR YKKAKGPLIV VAKNEGIVQG ARNHPGVDVV TVENLGVELL APGTHPGRLT
     IWTKGAIERL REIYG