ID A0A085B5E2_CUTAC Unreviewed; 301 AA. AC A0A085B5E2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 05-JUN-2019, entry version 18. DE RecName: Full=50S ribosomal protein L4 {ECO:0000256|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328}; GN ORFNames=PAST3_00110 {ECO:0000313|EMBL:KFC17687.1}; OS Cutibacterium acnes HL201PA1. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=1271528 {ECO:0000313|EMBL:KFC17687.1, ECO:0000313|Proteomes:UP000028538}; RN [1] {ECO:0000313|EMBL:KFC17687.1, ECO:0000313|Proteomes:UP000028538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HL201PA1 {ECO:0000313|EMBL:KFC17687.1, RC ECO:0000313|Proteomes:UP000028538}; RA Li H., Tomida S.; RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000256|HAMAP-Rule:MF_01328}. 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 CC during the early stages of 50S assembly. It makes multiple CC contacts with different domains of the 23S rRNA in the assembled CC 50S subunit and ribosome. {ECO:0000256|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP- CC Rule:MF_01328}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family. CC {ECO:0000256|HAMAP-Rule:MF_01328}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KFC17687.1}. 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; AODA01000001; KFC17687.1; -; Genomic_DNA. DR EnsemblBacteria; KFC17687; KFC17687; PAST3_00110. DR PATRIC; fig|1271528.3.peg.22; -. DR Proteomes; UP000028538; Unassembled WGS sequence. 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_L4_B; 1. DR InterPro; IPR002136; Ribosomal_L4/L1e. DR InterPro; IPR023574; Ribosomal_L4_dom_sf. DR InterPro; IPR013005; Ribosomal_uL4/L1e. DR PANTHER; PTHR10746; PTHR10746; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03953; rplD_bact; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028538}; KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01328}; KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01328, KW ECO:0000313|EMBL:KFC17687.1}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}. FT REGION 49 105 Disordered. {ECO:0000256|MobiDB-lite: FT A0A085B5E2}. SQ SEQUENCE 301 AA; 32312 MW; 5AF29701F0D1222B CRC64; MNETKTIDVL DVKGKKAGSA ELPGDLFDVN TNIPLIHQVV VAQLAAARQG THATKTRGQV SGGGKKPWRQ KGTGRARQGS TRAPQWVGGG TVHGPQPRSY AQRTPKKMVA AALRGALSDM ARDNRIFVVT SLVDGDKPST KQAKAVLSGL AELRKVLVVL DRSDEIDWLS VRNLSEVHVL AADQLNTYDV VNARTIVFSQ AGLDAFVGAR SANTQALSAE PEVPETNVAD QHPYGEDSFR GDNPPAGFDI KGNEDSMKFH EPSSPWYGRT IAEVWFRSAA AAEAAGFVNA VKSDSEKEDA K //