ID   RL5_NANEQ               Reviewed;         169 AA.
AC   Q74N79;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333};
GN   Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=NEQ093;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: This is 1 of the proteins that binds and probably mediates
CC       the attachment of the 5S RNA into the large ribosomal subunit, where it
CC       forms part of the central protuberance. In the 70S ribosome it contacts
CC       protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits;
CC       this bridge is implicated in subunit movement. May contact the P site
CC       tRNA; the 5S rRNA and some of its associated proteins might help
CC       stabilize positioning of ribosome-bound tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_01333}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit; contacts the 5S rRNA and
CC       probably tRNA. Forms a bridge to the 30S subunit in the 70S ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01333}.
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DR   EMBL; AE017199; AAR38950.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q74N79; -.
DR   SMR; Q74N79; -.
DR   STRING; 228908.NEQ093; -.
DR   EnsemblBacteria; AAR38950; AAR38950; NEQ093.
DR   KEGG; neq:NEQ093; -.
DR   PATRIC; fig|228908.8.peg.99; -.
DR   HOGENOM; CLU_061015_3_0_2; -.
DR   OMA; ERMYAFL; -.
DR   Proteomes; UP000000578; 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:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   HAMAP; MF_01333_A; Ribosomal_L5_A; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR022804; Ribosomal_L5_arc.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR   InterPro; IPR031310; Ribosomal_L5_N.
DR   PANTHER; PTHR11994; PTHR11994; 1.
DR   Pfam; PF00281; Ribosomal_L5; 1.
DR   Pfam; PF00673; Ribosomal_L5_C; 1.
DR   PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR   SUPFAM; SSF55282; SSF55282; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding; tRNA-binding.
FT   CHAIN           1..169
FT                   /note="50S ribosomal protein L5"
FT                   /id="PRO_0000125062"
SQ   SEQUENCE   169 AA;  19462 MW;  87C561D6CBD77323 CRC64;
     MEHPMRKIRI EKVTLNIGVG ESGEKLDKAY ELLKRLTGQK PVKTKAKVRV EQWHIRPGLP
     IGVKVTLRGE KAYKILKEKL LPAVDFKIKA SSFTDRGFGF GIPEYIMIPG MKYDPELGLI
     GLEAYVTLER PGYRVERRRI KRSKVGSRHR LNKEEIIKWA QEELGVQII