ID   RL4_DEIGD               Reviewed;         213 AA.
AC   Q1IX73;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=Dgeo_1866;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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: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; CP000359; ABF46161.1; -; Genomic_DNA.
DR   RefSeq; WP_011530991.1; NC_008025.1.
DR   AlphaFoldDB; Q1IX73; -.
DR   SMR; Q1IX73; -.
DR   STRING; 319795.Dgeo_1866; -.
DR   EnsemblBacteria; ABF46161; ABF46161; Dgeo_1866.
DR   KEGG; dge:Dgeo_1866; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_1_0; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..213
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_1000052391"
FT   REGION          41..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   213 AA;  23008 MW;  12BD4BF71AE9076A CRC64;
     MAQINVIGQN GGRSIDLDLP EVNPHVLHEV VTWQLAGRRR GTASTKTRAE VSRSGKKMYS
     QKGTGNARHG DRSVPTFVGG GVAFGPKPRS YSYTLPRKVR QLGLAMALAD RQQQGKLTAV
     DGFGLDGKTK SFVSWAKENG LDGSERVLIV TDDELTRRAA RNVAWATVLP VAGLNVYDIL
     RHERLVIDAV ALEPAQELET VPAEGNVQEG AAL