RL24_METST
ID RL24_METST Reviewed; 117 AA.
AC Q2NFW8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=50S ribosomal protein L24 {ECO:0000255|HAMAP-Rule:MF_01326};
GN Name=rpl24 {ECO:0000255|HAMAP-Rule:MF_01326}; OrderedLocusNames=Msp_0897;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57285.1; -; Genomic_DNA.
DR RefSeq; WP_011406484.1; NC_007681.1.
DR AlphaFoldDB; Q2NFW8; -.
DR SMR; Q2NFW8; -.
DR STRING; 339860.Msp_0897; -.
DR EnsemblBacteria; ABC57285; ABC57285; Msp_0897.
DR GeneID; 41325472; -.
DR KEGG; mst:Msp_0897; -.
DR eggNOG; arCOG04094; Archaea.
DR HOGENOM; CLU_093240_2_1_2; -.
DR OMA; VRIMRGD; -.
DR OrthoDB; 107015at2157; -.
DR Proteomes; UP000001931; 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..117
FT /note="50S ribosomal protein L24"
FT /id="PRO_0000241696"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 117 AA; 13519 MW; 6929FDF36FF9104E CRC64;
MSKQPRKQRK ALYTAPLHKR HNSMSVHLSD DLKEEFNRRS FPVRKGDSVE IVRGDFRGTE
GKVEGVDLKN YRVLVDGASS QKQDGSKLYQ PIHPSNLVLT EIYLDDERRN QALNRKV