ID   RL4_PROMA               Reviewed;         211 AA.
AC   Q7V9W3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, 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=Pro_1711;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00755.1; -; Genomic_DNA.
DR   RefSeq; NP_876102.1; NC_005042.1.
DR   RefSeq; WP_011125860.1; NC_005042.1.
DR   AlphaFoldDB; Q7V9W3; -.
DR   SMR; Q7V9W3; -.
DR   STRING; 167539.Pro_1711; -.
DR   EnsemblBacteria; AAQ00755; AAQ00755; Pro_1711.
DR   GeneID; 54201036; -.
DR   KEGG; pma:Pro_1711; -.
DR   PATRIC; fig|167539.5.peg.1806; -.
DR   eggNOG; COG0088; Bacteria.
DR   HOGENOM; CLU_041575_5_2_3; -.
DR   OMA; PQVHILE; -.
DR   OrthoDB; 1572673at2; -.
DR   Proteomes; UP000001420; 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..211
FT                   /note="50S ribosomal protein L4"
FT                   /id="PRO_0000129256"
FT   REGION          41..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   211 AA;  23297 MW;  1189929012668965 CRC64;
     MANCAVLDWQ GKEAGKASLN LKVAKDSSAV DLMHRAVLRQ QAHSRQGTAS TLTRAEVRGG
     GRKPYKQKGT GRARQGSIRT PLRPGGGIIF GPKPRQYNLS MNRKERRLAL RTALMARFND
     VIAVKDFGSK LKVPKTKEIQ DFLARLDISS NSKVLIILSQ PSDIIRRSVR NLEKVKLIAA
     EHLNVFDLLN ANSLIIGEDA LGKIKEVYGD D