ID   RL18_HALVD              Reviewed;         184 AA.
AC   P50563; D4GTX7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=50S ribosomal protein L18;
DE   AltName: Full=HVOL18;
GN   Name=rpl18; OrderedLocusNames=HVO_2545;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-24.
RX   PubMed=8174557; DOI=10.1111/j.1432-1033.1994.tb18791.x;
RA   McDougall J., Wittmann-Liebold B.;
RT   "Comparative analysis of the protein components from 5S rRNA.protein
RT   complexes of halophilic archaebacteria.";
RL   Eur. J. Biochem. 221:779-785(1994).
CC   -!- FUNCTION: This is one 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. {ECO:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts the 5S and 23S
CC       rRNAs (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001956; ADE05163.1; -; Genomic_DNA.
DR   PIR; I33084; I33084.
DR   RefSeq; WP_004042567.1; NZ_AOHU01000046.1.
DR   AlphaFoldDB; P50563; -.
DR   SMR; P50563; -.
DR   IntAct; P50563; 2.
DR   STRING; 309800.C498_08015; -.
DR   EnsemblBacteria; ADE05163; ADE05163; HVO_2545.
DR   GeneID; 8926004; -.
DR   KEGG; hvo:HVO_2545; -.
DR   eggNOG; arCOG04088; Archaea.
DR   HOGENOM; CLU_056222_2_0_2; -.
DR   OMA; MAHGPRY; -.
DR   OrthoDB; 108717at2157; -.
DR   Proteomes; UP000008243; 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   HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR   InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR   PANTHER; PTHR23410; PTHR23410; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 2.
DR   PRINTS; PR00058; RIBOSOMALL5.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8174557"
FT   CHAIN           2..184
FT                   /note="50S ribosomal protein L18"
FT                   /id="PRO_0000131403"
SQ   SEQUENCE   184 AA;  20198 MW;  AE335C181C9AD261 CRC64;
     MATGPRYKVP MRRRREVRTD YHQRLRLLKS GKPRLVARVS NKHVRAQLVT PGPQGDETHA
     AATSADLDEY GWEAPTGNLP SAYLTGYLAG KRALAAGVEK AVLDIGLNTA TPGNKVFAVQ
     EGAIDAGLEI PHNDAVLADW DRNRGVHIAE YAEQLDEPLY SGEFDATNLP DHFDEVLGNL
     QEDE