ID RL3_THET2 Reviewed; 206 AA. AC Q72I04; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=Large ribosomal subunit protein uL3 {ECO:0000255|HAMAP-Rule:MF_01325}; DE AltName: Full=50S ribosomal protein L3 {ECO:0000305}; GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; GN OrderedLocusNames=TT_C1328; 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, it binds directly CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S CC subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family. CC {ECO:0000255|HAMAP-Rule:MF_01325}. 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; AAS81670.1; -; Genomic_DNA. DR RefSeq; WP_011173714.1; NZ_CP133179.1. DR PDB; 4V4I; X-ray; 3.71 A; C=1-206. DR PDB; 4V4J; X-ray; 3.83 A; C=1-206. DR PDB; 4V63; X-ray; 3.21 A; BE/DE=1-206. DR PDB; 4V67; X-ray; 3.00 A; BE/DE=1-206. DR PDB; 4V7P; X-ray; 3.62 A; BD/CD=1-206. DR PDB; 4V83; X-ray; 3.50 A; BD/DD=1-204. DR PDB; 4V84; X-ray; 3.40 A; BD/DD=1-204. DR PDB; 4V9J; X-ray; 3.86 A; BE/DE=1-205. DR PDB; 4V9K; X-ray; 3.50 A; BE/DE=1-205. DR PDB; 4V9L; X-ray; 3.50 A; BE/DE=1-205. DR PDB; 4V9M; X-ray; 4.00 A; BE/DE=1-205. DR PDB; 4V9N; X-ray; 3.40 A; BE/DE=1-204. DR PDB; 4V9Q; X-ray; 3.40 A; AE/CE=1-204. DR PDB; 4W29; X-ray; 3.80 A; BE/DE=1-205. DR PDB; 4XEJ; X-ray; 3.80 A; AL03/BL03=1-204. DR PDB; 5J4D; X-ray; 3.10 A; F/KB=1-206. DR PDB; 5V8I; X-ray; 3.25 A; 1E/2E=1-206. DR PDB; 6B4V; X-ray; 3.40 A; F/JB=1-206. DR PDB; 6BOH; X-ray; 3.40 A; F/KB=1-206. DR PDB; 6BOK; X-ray; 3.55 A; F/IB=1-206. DR PDB; 6N1D; X-ray; 3.20 A; AL03/BL03=1-206. 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; Q72I04; -. DR SMR; Q72I04; -. DR IntAct; Q72I04; 4. DR GeneID; 3167929; -. DR KEGG; tth:TT_C1328; -. DR eggNOG; COG0087; Bacteria. DR HOGENOM; CLU_044142_4_1_0; -. DR OrthoDB; 9806135at2; -. DR EvolutionaryTrace; Q72I04; -. 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; 3.30.160.810; -; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_01325_B; Ribosomal_uL3_B; 1. DR InterPro; IPR000597; Ribosomal_uL3. DR InterPro; IPR019927; Ribosomal_uL3_bac/org-type. DR InterPro; IPR019926; Ribosomal_uL3_CS. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR03625; L3_bact; 1. DR PANTHER; PTHR11229:SF8; 39S RIBOSOMAL PROTEIN L3, MITOCHONDRIAL; 1. DR PANTHER; PTHR11229; 50S RIBOSOMAL PROTEIN L3; 1. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. PE 1: Evidence at protein level; KW 3D-structure; Ribonucleoprotein; Ribosomal protein; RNA-binding; KW rRNA-binding. FT CHAIN 1..206 FT /note="Large ribosomal subunit protein uL3" FT /id="PRO_0000241428" FT STRAND 3..16 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 19..27 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 56..62 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 63..68 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:4V9L" FT STRAND 101..107 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:4V67" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:4V9Q" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 159..176 FT /evidence="ECO:0007829|PDB:4V67" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:4V67" FT STRAND 194..200 FT /evidence="ECO:0007829|PDB:4V67" SQ SEQUENCE 206 AA; 22408 MW; A920741478CB6028 CRC64; MKGILGVKVG MTRIFRDDRA VPVTVILAGP CPVVQRRTPE KDGYTAVQLG FLPQNPKRVN RPLKGHFAKA GVEPVRILRE IRDFNPEGDT VTVEIFKPGE RVDVTGTSKG RGFAGVMKRW NFAGGPDSHG AHKIHRHPGS IGNRKTPGRV YKGKKMAGHY GAERVTVMNL EVVDVIPEEN LLLVKGAVPG PNGGLVIVRE TKKAAK //