ID   RL24_METKA              Reviewed;         149 AA.
AC   Q8TW19;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN   Name=rpl24 {ECO:0000255|HAMAP-Rule:MF_01326}; Synonyms=rplX;
GN   OrderedLocusNames=MK1219;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02432.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TW19; -.
DR   SMR; Q8TW19; -.
DR   STRING; 190192.MK1219; -.
DR   EnsemblBacteria; AAM02432; AAM02432; MK1219.
DR   KEGG; mka:MK1219; -.
DR   PATRIC; fig|190192.8.peg.1322; -.
DR   HOGENOM; CLU_093240_2_1_2; -.
DR   OMA; VRIMRGD; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
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_A; Ribosomal_L24_A; 1.
DR   InterPro; IPR005824; KOW.
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; PF00467; KOW; 1.
DR   Pfam; PF16906; Ribosomal_L26; 1.
DR   SMART; SM00739; KOW; 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..149
FT                   /note="50S ribosomal protein L24"
FT                   /id="PRO_0000130771"
FT   REGION          114..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   149 AA;  17581 MW;  32F1EEEC6137076E CRC64;
     MRWTKSSQPR KQRKAFFNAP LHKRQKLMSA TLHPELRKKF NRRSLPVRRG DMVRIMRGDF
     KGHEGEVVEV DLKRLRIYVE GATIERANGE KVYYPIHPSN VMIIEPNLDD PMRRKIIERS
     GGTPEVEAVP EKSEEEKEEK EKEEEKSEE