ID   RL24_NITMS              Reviewed;         168 AA.
AC   A9A5I4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rpl24 {ECO:0000255|HAMAP-Rule:MF_01326}; OrderedLocusNames=Nmar_0799;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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: Located at the polypeptide exit tunnel on the outside of the
CC       subunit. {ECO:0000255|HAMAP-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; CP000866; ABX12695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A5I4; -.
DR   SMR; A9A5I4; -.
DR   STRING; 436308.Nmar_0799; -.
DR   EnsemblBacteria; ABX12695; ABX12695; Nmar_0799.
DR   KEGG; nmr:Nmar_0799; -.
DR   eggNOG; arCOG04094; Archaea.
DR   HOGENOM; CLU_093240_2_0_2; -.
DR   OMA; VRIMRGD; -.
DR   PhylomeDB; A9A5I4; -.
DR   Proteomes; UP000000792; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR   CDD; cd06089; KOW_RPL26; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_01326_A; Ribosomal_L24_A; 1.
DR   InterPro; IPR041988; KOW_RPL26/RPL24.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR005825; Ribosomal_L24/26_CS.
DR   InterPro; IPR005756; Ribosomal_L26/L24P_euk/arc.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11143; PTHR11143; 1.
DR   Pfam; PF16906; Ribosomal_L26; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   TIGRFAMs; TIGR01080; rplX_A_E; 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..168
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_0000355737"
FT   REGION          112..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   168 AA;  18948 MW;  5FB0DA322AC381E2 CRC64;
     MKPTKMRNKM IYRASYQTKS KQLGSALSKD LQKKYGKRSV RVNEGDSVTI LRGEFKGVDG
     KVAEVSTAKS SVAIEGVKKE KTKGDKFDVF IHTSNLLVTS LNTEDKWRIA KLEGKDPRKQ
     PKEAPKAAEK PAKEEPKKET PKAEEKPAKE EPKETKVEKK SEEKEDEN