ID   RL4_SYNSC               Reviewed;         211 AA.
AC   Q3AMN1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Name=rplD {ECO:0000255|HAMAP-Rule:MF_01328};
GN   Synonyms=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328};
GN   OrderedLocusNames=Syncc9605_0375;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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; CP000110; ABB34151.1; -; Genomic_DNA.
DR   RefSeq; WP_011363388.1; NC_007516.1.
DR   AlphaFoldDB; Q3AMN1; -.
DR   SMR; Q3AMN1; -.
DR   STRING; 110662.Syncc9605_0375; -.
DR   PRIDE; Q3AMN1; -.
DR   EnsemblBacteria; ABB34151; ABB34151; Syncc9605_0375.
DR   KEGG; syd:Syncc9605_0375; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_3; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
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   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..211
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000242448"
FT   REGION          41..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  22920 MW;  B767C55B76051D08 CRC64;
     MASCVVRDWQ GKEAGKATLD LKVAKETTAV DLMHRAVLRQ QAHARQGTAS TLTRSEVRGG
     GRKPYKQKGT GRARQGSIRT PLKPGGGIIF GPKPRTYNLA MNRKERRLAL RTALMARIDD
     VTVVQDFGAS LEAPKTREIT DALGRLGVAA GSKVLIVLTN PSDVVRRSVR NLEKVKLISA
     DQLNVFDLLH ANALVLGEEA LATIQEVYGD D