ID RL24_THET2 Reviewed; 110 AA. AC Q72I15; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Large ribosomal subunit protein uL24 {ECO:0000255|HAMAP-Rule:MF_01326}; DE AltName: Full=50S ribosomal protein L24 {ECO:0000305}; GN Name=rplX {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=TT_C1317; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). 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. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family. CC {ECO:0000255|HAMAP-Rule:MF_01326}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017221; AAS81659.1; -; Genomic_DNA. DR RefSeq; WP_011173707.1; NZ_CP133179.1. DR PDB; 4V4I; X-ray; 3.71 A; S=1-110. DR PDB; 4V4J; X-ray; 3.83 A; S=1-110. DR PDB; 4V63; X-ray; 3.21 A; BY/DY=1-110. DR PDB; 4V67; X-ray; 3.00 A; BY/DY=1-110. DR PDB; 4V7P; X-ray; 3.62 A; BU/CU=2-110. DR PDB; 4V83; X-ray; 3.50 A; BU/DU=2-101. DR PDB; 4V84; X-ray; 3.40 A; BU/DU=2-101. DR PDB; 4V9J; X-ray; 3.86 A; BY/DY=2-108. DR PDB; 4V9K; X-ray; 3.50 A; BY/DY=2-108. DR PDB; 4V9L; X-ray; 3.50 A; BY/DY=2-108. DR PDB; 4V9M; X-ray; 4.00 A; BY/DY=2-108. DR PDB; 4V9N; X-ray; 3.40 A; BY/DY=2-101. DR PDB; 4V9Q; X-ray; 3.40 A; AU/CU=2-101. DR PDB; 4W29; X-ray; 3.80 A; BY/DY=2-108. DR PDB; 4XEJ; X-ray; 3.80 A; AL24/BL24=2-101. DR PDB; 5J4D; X-ray; 3.10 A; AC/V=1-110. DR PDB; 5V8I; X-ray; 3.25 A; 1Y/2Y=1-110. DR PDB; 6B4V; X-ray; 3.40 A; V/ZB=1-110. DR PDB; 6BOH; X-ray; 3.40 A; AC/V=1-110. DR PDB; 6BOK; X-ray; 3.55 A; V/YB=1-110. DR PDB; 6N1D; X-ray; 3.20 A; AL24/BL24=1-110. DR PDBsum; 4V4I; -. DR PDBsum; 4V4J; -. DR PDBsum; 4V63; -. DR PDBsum; 4V67; -. DR PDBsum; 4V7P; -. DR PDBsum; 4V83; -. DR PDBsum; 4V84; -. DR PDBsum; 4V9J; -. DR PDBsum; 4V9K; -. DR PDBsum; 4V9L; -. DR PDBsum; 4V9M; -. DR PDBsum; 4V9N; -. DR PDBsum; 4V9Q; -. DR PDBsum; 4W29; -. DR PDBsum; 4XEJ; -. DR PDBsum; 5J4D; -. DR PDBsum; 5V8I; -. DR PDBsum; 6B4V; -. DR PDBsum; 6BOH; -. DR PDBsum; 6BOK; -. DR PDBsum; 6N1D; -. DR AlphaFoldDB; Q72I15; -. DR SMR; Q72I15; -. DR IntAct; Q72I15; 4. DR GeneID; 3169836; -. DR KEGG; tth:TT_C1317; -. DR eggNOG; COG0198; Bacteria. DR HOGENOM; CLU_093315_2_3_0; -. DR OrthoDB; 9807419at2; -. DR EvolutionaryTrace; Q72I15; -. DR Proteomes; UP000000592; Chromosome. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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_uL24_B; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR003256; Ribosomal_uL24. DR InterPro; IPR005825; Ribosomal_uL24_CS. DR InterPro; IPR041988; Ribosomal_uL24_KOW. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR NCBIfam; TIGR01079; rplX_bact; 1. DR PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1. DR PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1. DR Pfam; PF00467; KOW; 1. DR Pfam; PF17136; ribosomal_L24; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..110 FT /note="Large ribosomal subunit protein uL24" FT /id="PRO_0000241679" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 19..22 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:4V84" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 69..71 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:4V67" SQ SEQUENCE 110 AA; 12057 MW; A9E773D9A86B819A CRC64; MRVKMHVKKG DTVLVASGKY KGRVGKVKEV LPKKYAVIVE GVNIVKKAVR VSPKYPQGGF IEKEAPLHAS KVRPICPACG KPTRVRKKFL ENGKKIRVCA KCGGALDTEE //