ID RL4_THET2 Reviewed; 205 AA. AC Q72I05; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000255|HAMAP-Rule:MF_01328}; DE AltName: Full=50S ribosomal protein L4 {ECO:0000305}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=TT_C1327; 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 the primary rRNA binding proteins, this protein CC initially binds near the 5'-end of the 23S rRNA. It is important during CC the early stages of 50S assembly. It makes multiple contacts with CC different domains of the 23S rRNA in the assembled 50S subunit and CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family. CC {ECO:0000255|HAMAP-Rule:MF_01328}. 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; AAS81669.1; -; Genomic_DNA. DR RefSeq; WP_011173713.1; NZ_CP133179.1. DR PDB; 4V4I; X-ray; 3.71 A; D=1-205. DR PDB; 4V4J; X-ray; 3.83 A; D=1-205. DR PDB; 4V63; X-ray; 3.21 A; BF/DF=1-205. DR PDB; 4V67; X-ray; 3.00 A; BF/DF=1-205. DR PDB; 4V7P; X-ray; 3.62 A; BE/CE=1-205. DR PDB; 4V83; X-ray; 3.50 A; BE/DE=1-202. DR PDB; 4V84; X-ray; 3.40 A; BE/DE=1-202. DR PDB; 4V9J; X-ray; 3.86 A; BF/DF=1-203. DR PDB; 4V9K; X-ray; 3.50 A; BF/DF=1-203. DR PDB; 4V9L; X-ray; 3.50 A; BF/DF=1-203. DR PDB; 4V9M; X-ray; 4.00 A; BF/DF=1-203. DR PDB; 4V9N; X-ray; 3.40 A; BF/DF=1-202. DR PDB; 4V9Q; X-ray; 3.40 A; AF/CF=1-202. DR PDB; 4W29; X-ray; 3.80 A; BF/DF=1-203. DR PDB; 4XEJ; X-ray; 3.80 A; AL04/BL04=1-202. DR PDB; 5J4D; X-ray; 3.10 A; G/LB=1-205. DR PDB; 6B4V; X-ray; 3.40 A; G/KB=1-205. DR PDB; 6BOH; X-ray; 3.40 A; G/LB=1-205. DR PDB; 6BOK; X-ray; 3.55 A; G/JB=1-205. DR PDB; 6N1D; X-ray; 3.20 A; AL04/BL04=1-205. 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; 6B4V; -. DR PDBsum; 6BOH; -. DR PDBsum; 6BOK; -. DR PDBsum; 6N1D; -. DR AlphaFoldDB; Q72I05; -. DR SMR; Q72I05; -. DR IntAct; Q72I05; 4. DR GeneID; 3167923; -. DR KEGG; tth:TT_C1327; -. DR eggNOG; COG0088; Bacteria. DR HOGENOM; CLU_041575_5_1_0; -. DR OrthoDB; 9803201at2; -. DR EvolutionaryTrace; Q72I05; -. 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 Gene3D; 3.40.1370.10; -; 1. DR HAMAP; MF_01328_B; Ribosomal_uL4_B; 1. DR InterPro; IPR002136; Ribosomal_uL4. DR InterPro; IPR013005; Ribosomal_uL4-like. DR InterPro; IPR023574; Ribosomal_uL4_dom_sf. DR NCBIfam; TIGR03953; rplD_bact; 1. DR PANTHER; PTHR10746:SF6; 39S RIBOSOMAL PROTEIN L4, MITOCHONDRIAL; 1. DR PANTHER; PTHR10746; 50S RIBOSOMAL PROTEIN L4; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; Ribosomal protein L4; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..205 FT /note="Large ribosomal subunit protein uL4" FT /id="PRO_0000242455" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:4V9N" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 48..51 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:4V9K" FT STRAND 62..65 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:4V9K" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:4V84" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 98..115 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:4V63" FT TURN 125..129 FT /evidence="ECO:0007829|PDB:4V9L" FT HELIX 131..139 FT /evidence="ECO:0007829|PDB:4V63" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 156..164 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 168..171 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:4V84" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:4V63" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:4V63" FT HELIX 191..200 FT /evidence="ECO:0007829|PDB:4V63" SQ SEQUENCE 205 AA; 22708 MW; FC50A700F8CBC324 CRC64; MYQIPVLSPS GRRELAADLP AEINPHLLWE VVRWQLAKRR RGTASTKTRG EVAYSGRKIW PQKHTGRARH GDIGAPIFVG GGVVFGPKPR DYSYTLPKKV RKKGLAMAVA DRAREGKLLL VEAFAGVNGK TKEFLAWAKE AGLDGSESVL LVTGNELVRR AARNLPWVVT LAPEGLNVYD IVRTERLVMD LDAWEVFQNR IGGEA //