ID RL4_AGARV Reviewed; 206 AA. AC C4ZBD5; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 13-NOV-2019, entry version 54. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; GN OrderedLocusNames=EUBREC_0419; OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC OS 5835 / VPI 0990) (Eubacterium rectale). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=515619; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990; RX PubMed=19321416; DOI=10.1073/pnas.0901529106; RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S., RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L., RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C., RA Hettich R.L., Gordon J.I.; RT "Characterizing a model human gut microbiota composed of members of RT its two dominant bacterial phyla."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009). 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: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. {ECO:0000255|HAMAP- CC Rule:MF_01328}. 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; CP001107; ACR74210.1; -; Genomic_DNA. DR RefSeq; WP_012741328.1; NC_012781.1. DR EnsemblBacteria; ACR74210; ACR74210; EUBREC_0419. DR GeneID; 41341236; -. DR KEGG; ere:EUBREC_0419; -. DR HOGENOM; HOG000248767; -. DR KO; K02926; -. DR OMA; PQVHILE; -. DR OrthoDB; 1572673at2; -. DR Proteomes; UP000001477; Chromosome. 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; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 206 50S ribosomal protein L4. FT /FTId=PRO_1000214572. SQ SEQUENCE 206 AA; 22910 MW; D6796080DB209E8E CRC64; MANVAVYNME GKEVDKIELN DSIFGVEINE HLVHMAVLQQ LANKRQGTQK AKTRSEVRGG GRKPWRQKGT GHARQGSTRS PQWTGGGVVF APTPRDYSFK LNKKEKRAAL KSALTSRVVE NKFVVVDELK LDEIKTKKFV EVLKNLNVEK ALVVLNDMDE KVIASAANIP TVKTTQTNEL NVFDVLKYDT VVVTKAAVAT IEEVYA //