ID   RL3_METS5               Reviewed;         341 AA.
AC   A4YCW6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Msed_0091;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(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; CP000682; ABP94268.1; -; Genomic_DNA.
DR   RefSeq; WP_011921237.1; NC_009440.1.
DR   AlphaFoldDB; A4YCW6; -.
DR   SMR; A4YCW6; -.
DR   STRING; 399549.Msed_0091; -.
DR   EnsemblBacteria; ABP94268; ABP94268; Msed_0091.
DR   GeneID; 5103899; -.
DR   GeneID; 59456473; -.
DR   KEGG; mse:Msed_0091; -.
DR   eggNOG; arCOG04070; Archaea.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   Proteomes; UP000000242; 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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..341
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_1000073252"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   341 AA;  38332 MW;  7927123E4B84204D CRC64;
     MGHRKLSSPR RGSAGLRPRK RSEELLPSPR SYPEVNLPNP VTLGFVGYKV GMTHIFMIDE
     DRSSSMFGKE IYVPVTVLET PPIYVLALRA YGLNNRGEHS VMGEVWGDLG DFGKFITRRI
     RGLKIDKEKK EHQLKDIESN LESVSYFRLL VSTQPHLIPA LGKKTPDIVE VQIGGGNTKN
     QLEYGLKLLG NTLSVRDVFK EGQLMDIIGV TKGHGFQGVI KRYGVQELPR WHKHRKGSRK
     VGTKGPSLGT PSYVPQPGQM GFHRRTEYNK RILKISDDTK LINPKGGFVR YGLVKNTYLL
     VQGSTIGSIK RPLFLRYPIR PYSAQLPVPK VTYVDVNSKQ G