ID   RL3_THEON               Reviewed;         347 AA.
AC   B6YSL3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=TON_0066;
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, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L24e. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; CP000855; ACJ15550.1; -; Genomic_DNA.
DR   RefSeq; WP_012571023.1; NC_011529.1.
DR   AlphaFoldDB; B6YSL3; -.
DR   SMR; B6YSL3; -.
DR   STRING; 523850.TON_0066; -.
DR   EnsemblBacteria; ACJ15550; ACJ15550; TON_0066.
DR   GeneID; 7017712; -.
DR   KEGG; ton:TON_0066; -.
DR   PATRIC; fig|523850.10.peg.66; -.
DR   eggNOG; arCOG04070; Archaea.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   OrthoDB; 31722at2157; -.
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; 4.10.960.10; -; 1.
DR   HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR   InterPro; IPR045077; L3_arc_euk.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019928; Ribosomal_L3_arc.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11363; PTHR11363; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03626; L3_arch; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..347
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000141934"
FT   REGION          325..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   347 AA;  39717 MW;  93CE5B9EFE577DBF CRC64;
     MGKIHRPRRG SLAYSPRKRA KSIVPRIRKW PKDSEVRMLG FAGYKAGMTH ILMIDDRPGL
     TKGKEIFMPV TVVEVPPLFV YGIRAYRQGY LGLETATEVW FHELNDYVKR RIKTLPKDYN
     EEAFQAKLGQ LEDLVNDGEI VDVRLLVHTQ PWLIKLKKKP EVMEYAIGGD DVKAKFDYAK
     EKIGKELRAS EVLHEGELLD VIAVTKGKGT QGPVKRWGIK IQFHKAQRAG KGRHVGNLGP
     WHPTRVMWTV PQAGQMGFHH RTEFNKRLIA IGENGKLKLD EKNEIEITPK GGFPHYGIIR
     SDFLMIQGTI PGSFKRIIRV RPAIRPPKKK PPVERPQITY ISRESKQ