ID   RL3_CALMQ               Reviewed;         347 AA.
AC   A8MB75;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=Cmaq_0317;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW01165.1; -; Genomic_DNA.
DR   RefSeq; WP_012185385.1; NC_009954.1.
DR   AlphaFoldDB; A8MB75; -.
DR   SMR; A8MB75; -.
DR   STRING; 397948.Cmaq_0317; -.
DR   EnsemblBacteria; ABW01165; ABW01165; Cmaq_0317.
DR   GeneID; 5710162; -.
DR   KEGG; cma:Cmaq_0317; -.
DR   eggNOG; arCOG04070; Archaea.
DR   HOGENOM; CLU_033361_2_0_2; -.
DR   OMA; HQRTEYN; -.
DR   OrthoDB; 31722at2157; -.
DR   Proteomes; UP000001137; 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..347
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000353621"
SQ   SEQUENCE   347 AA;  38535 MW;  E2C78E387F1C207E CRC64;
     MGLKIHRPRR GSMAYYPRKR ASDIVPRIRN WPVIDLGKPT LLGFVGYKAG MVHVTVVDDR
     KTSPFFGKEL VKAVTVVETP PLYVVGLRAY AINPLKAELV SVGEAWVNIP NEVRKYIARR
     IPTLPEKFDT DKALADLQGL LDSVSYIKVI AMTQPYKAGV GKKTPEVLEI PVGGVPTIDE
     QFKYASGLLG KEVKPTDVFK PGQLVDVIGV TKGKGTQGVI KRFGVKELPR WHKHRKGSRR
     TGTVGPKPAV MYTQPRMGQM GFHRRTEYNK RILKISDNGS EITPKGGFKH YGIVRSGYML
     IEGSTPGVVK RLIAFRYPIR PPFNYDLKQV QAPSVTWVSV MGVSGVS