ID D1YF53_CUTAC Unreviewed; 301 AA. AC D1YF53; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 02-JUN-2021, entry version 44. DE RecName: Full=50S ribosomal protein L4 {ECO:0000256|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000256|HAMAP-Rule:MF_01328, GN ECO:0000313|EMBL:EFB87180.1}; GN ORFNames=HMPREF9206_0443 {ECO:0000313|EMBL:EFB87180.1}; OS Cutibacterium acnes J139. OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae; OC Cutibacterium. OX NCBI_TaxID=679194 {ECO:0000313|EMBL:EFB87180.1, ECO:0000313|Proteomes:UP000003506}; RN [1] {ECO:0000313|EMBL:EFB87180.1, ECO:0000313|Proteomes:UP000003506} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J139 {ECO:0000313|EMBL:EFB87180.1, RC ECO:0000313|Proteomes:UP000003506}; RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L., RA Nelson K.E.; RT "Genome Sequence of Propionibacterium acnes J139."; RL Submitted (DEC-2009) 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 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: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|ARBA:ARBA00010528, ECO:0000256|HAMAP-Rule:MF_01328}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EFB87180.1}. 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; ADFS01000006; EFB87180.1; -; Genomic_DNA. DR RefSeq; WP_002514868.1; NZ_ADFS01000006.1. DR EnsemblBacteria; EFB87180; EFB87180; HMPREF9206_0443. DR Proteomes; UP000003506; 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 Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP- KW Rule:MF_01328}; KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP- KW Rule:MF_01328}; RNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01328}. FT REGION 49..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 301 AA; 32370 MW; DC3ADC1B1300534F CRC64; MNETKTIDVL DVKGKKAGSA ELPGDLFDVN TNIPLIHQVV VAQLAAARQG THATKTRGQV SGGGKKPWRQ KGTGRARQGS TRAPQWVGGG TVHGPQPRSY AQRTPKKMVA AALRGALSDM ARDNRIFVVT SLVDGDKPST KQAKVVLSGV AELRKVLVVL DRSDEIDWLS VRNLSEVHVL AADQLNTYDV VNARTIVFSQ AGLDAFVGAR SANTQTLTAE PEVPETNVAD QHPYGEDSFR GDNPPAGFDI KGNEDSMKFH EPSSPWYGRT IAEVWFRSAA AAEAAGFVNA VKSDSEKEDA K //