ID   RL3_SULAC               Reviewed;         342 AA.
AC   Q4JB40;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Saci_0597;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY79989.1; -; Genomic_DNA.
DR   RefSeq; WP_011277491.1; NC_007181.1.
DR   AlphaFoldDB; Q4JB40; -.
DR   SMR; Q4JB40; -.
DR   STRING; 330779.Saci_0597; -.
DR   EnsemblBacteria; AAY79989; AAY79989; Saci_0597.
DR   GeneID; 3473517; -.
DR   KEGG; sai:Saci_0597; -.
DR   PATRIC; fig|330779.12.peg.576; -.
DR   eggNOG; arCOG04070; Archaea.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   Proteomes; UP000001018; 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..342
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077221"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   342 AA;  38452 MW;  E6FA3023EAE06963 CRC64;
     MGHRKLSSPR RGSAGLRPRK RADEILPTPK NWPLVNLKEP KLLGFIGYKA GMTHVYMIDD
     KPTSPNYGKE VYTPVTIVES PPILGLALRA YHIDSKGELS VLVDYWANFE EGSLKYLKRK
     ITSLKVDSSK MKEKLDLIQK NLNNITYMRL LVSTQPWLVP SLGKKRPEIV EIQIGGGSIQ
     DQLNYGLSLL GKQIPVRDVF REGQLTDIIG VTKGKGFQGV IKRYSVVEFP RWHKHRKGSR
     KIGARGPSIS TPSYVPQPGQ LGFHRRTEYN KRIIKIGDNV NEINPAGGIV NYGLVKNTYL
     VIEGSVLGSR KRPLFLRYPI RPSWSPESAP KITYVNLASQ QG