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   10-OCT-2018, entry version 50.
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}.
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DR   EMBL; CP001107; ACR74210.1; -; Genomic_DNA.
DR   RefSeq; WP_012741328.1; NC_012781.1.
DR   EnsemblBacteria; ACR74210; ACR74210; EUBREC_0419.
DR   KEGG; ere:EUBREC_0419; -.
DR   HOGENOM; HOG000248767; -.
DR   KO; K02926; -.
DR   OMA; DYSFKLN; -.
DR   OrthoDB; POG091H027V; -.
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
//