ID   RL25_ENDTX              Reviewed;         239 AA.
AC   B1GYU9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L25 {ECO:0000255|HAMAP-Rule:MF_01334};
DE   AltName: Full=General stress protein CTC {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Name=rplY {ECO:0000255|HAMAP-Rule:MF_01334};
GN   Synonyms=ctc {ECO:0000255|HAMAP-Rule:MF_01334}; OrderedLocusNames=TGRD_709;
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: This is one of the proteins that binds to the 5S RNA in the
CC       ribosome where it forms part of the central protuberance.
CC       {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; part of the 5S
CC       rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA. Binds to the 5S rRNA
CC       independently of L5 and L18. {ECO:0000255|HAMAP-Rule:MF_01334}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family. CTC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01334}.
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DR   EMBL; AP009510; BAG14192.1; -; Genomic_DNA.
DR   RefSeq; WP_015423713.1; NC_020419.1.
DR   RefSeq; YP_001956653.1; NC_020419.1.
DR   AlphaFoldDB; B1GYU9; -.
DR   SMR; B1GYU9; -.
DR   STRING; 471821.TGRD_709; -.
DR   EnsemblBacteria; BAG14192; BAG14192; TGRD_709.
DR   KEGG; rsd:TGRD_709; -.
DR   HOGENOM; CLU_075939_1_0_0; -.
DR   OMA; HVDFYEV; -.
DR   OrthoDB; 1673077at2; -.
DR   Proteomes; UP000001691; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00495; Ribosomal_L25_TL5_CTC; 1.
DR   Gene3D; 2.170.120.20; -; 1.
DR   Gene3D; 2.40.240.10; -; 1.
DR   HAMAP; MF_01334; Ribosomal_L25_CTC; 1.
DR   InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR   InterPro; IPR029751; Ribosomal_L25.
DR   InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR   InterPro; IPR020057; Ribosomal_L25_b-dom.
DR   InterPro; IPR037121; Ribosomal_L25_C.
DR   InterPro; IPR001021; Ribosomal_L25_long.
DR   Pfam; PF01386; Ribosomal_L25p; 1.
DR   Pfam; PF14693; Ribosomal_TL5_C; 1.
DR   SUPFAM; SSF50715; SSF50715; 1.
DR   TIGRFAMs; TIGR00731; bL25_bact_ctc; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..239
FT                   /note="50S ribosomal protein L25"
FT                   /id="PRO_1000142561"
FT   REGION          211..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  25496 MW;  BCC52F2D0D8038B9 CRC64;
     MKEVILDAQA RTVGSKGDLA FLRKSGKIPA IFYGKGIKPE AIAVSSKVFV SIMEANGANV
     IINLNFKDGK KAAIVKSLDR DFLTQHTIHI DFHAISLEDK IEVLVPVHIA GVADGVKNFG
     GVMEFIVREV KVEAIPRNIP QKISVDVKAL RIGQGITVAD LPELDGVKYV QDSSTLIVHV
     IAVAAVFEEE KPEAMAGGTA TVVQPEVIIS KGKKDKEDEE AEKGTSVASP TTATGGTKK