ID   RL24_DEIDV              Reviewed;         115 AA.
AC   C1CXF5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; OrderedLocusNames=Deide_18840;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC       the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01326}.
CC   -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01326}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01326}.
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DR   EMBL; CP001114; ACO46872.1; -; Genomic_DNA.
DR   RefSeq; WP_012693994.1; NC_012526.1.
DR   AlphaFoldDB; C1CXF5; -.
DR   SMR; C1CXF5; -.
DR   STRING; 546414.Deide_18840; -.
DR   PaxDb; C1CXF5; -.
DR   PRIDE; C1CXF5; -.
DR   EnsemblBacteria; ACO46872; ACO46872; Deide_18840.
DR   KEGG; ddr:Deide_18840; -.
DR   eggNOG; COG0198; Bacteria.
DR   HOGENOM; CLU_093315_2_0_0; -.
DR   OMA; HVKPTQE; -.
DR   OrthoDB; 2040741at2; -.
DR   Proteomes; UP000002208; 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   CDD; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041988; KOW_RPL26/RPL24.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR003256; Ribosomal_L24.
DR   InterPro; IPR005825; Ribosomal_L24/26_CS.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR12903; PTHR12903; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF17136; ribosomal_L24; 1.
DR   SMART; SM00739; KOW; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01079; rplX_bact; 1.
DR   PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..115
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_1000214537"
SQ   SEQUENCE   115 AA;  12189 MW;  D8285D23E67EF83D CRC64;
     MPRPSAGSHH SDKLHVKKGD TVVVLSGKHK GKTGKVLLAL PRDQKVIVEG VNLVTKHVKP
     SASNPQGGIE QREGALHASK VSIVDPETGK ATRIRKQIVD GKKVRVAVAS GKVID