ID   RL3_ENDTX               Reviewed;         227 AA.
AC   B1GZ83;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=TGRD_082;
OS   Endomicrobium trichonymphae.
OC   Bacteria; Elusimicrobia; Endomicrobia; Endomicrobiales; Endomicrobiaceae;
OC   Endomicrobium.
OX   NCBI_TaxID=1408204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18391199; DOI=10.1073/pnas.0801389105;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Complete genome of the uncultured termite group 1 bacteria in a single
RT   host protist cell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:5555-5560(2008).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; AP009510; BAG13565.1; -; Genomic_DNA.
DR   RefSeq; WP_015423094.1; NC_020419.1.
DR   RefSeq; YP_001956026.1; NC_020419.1.
DR   AlphaFoldDB; B1GZ83; -.
DR   SMR; B1GZ83; -.
DR   STRING; 471821.TGRD_082; -.
DR   EnsemblBacteria; BAG13565; BAG13565; TGRD_082.
DR   KEGG; rsd:TGRD_082; -.
DR   PATRIC; fig|471821.5.peg.125; -.
DR   HOGENOM; CLU_044142_4_1_0; -.
DR   OMA; KRMAGRY; -.
DR   OrthoDB; 1270636at2; -.
DR   Proteomes; UP000001691; 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   HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11229; PTHR11229; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03625; L3_bact; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..227
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000353618"
FT   REGION          129..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  24659 MW;  D416C66122812299 CRC64;
     MLKFIIGKKI GMTQVFDVKG NLMPVTVVEV GHCVVTDVRT VEKNGYSAVQ LGFGEIKEKG
     LNKAQAVFFK RNNLSYKRTL KEFRVSEVAG FSVGHEIKAD AFKAGDYVDV SAVTKGKGYA
     GVIKRHNFGM QPVSHGQSDR TRSRGSSGAQ GPQKVLKGLK MSGHMGNEYV TVQKLLIVNV
     DAEKNVLLIK GSVPSANRGT LFISSTLKKI PKVLVAVVHK GTKVKKK