ID   RL20_DEIDV              Reviewed;         117 AA.
AC   C1D0Q8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382};
GN   Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; OrderedLocusNames=Deide_05920;
OS   Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=546414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX   PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA   de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA   Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA   Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT   "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT   bacterium Deinococcus deserti.";
RL   PLoS Genet. 5:E1000434-E1000434(2009).
CC   -!- FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the
CC       in vitro assembly process of the 50S ribosomal subunit. It is not
CC       involved in the protein synthesizing functions of that subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00382}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00382}.
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DR   EMBL; CP001114; ACO45432.1; -; Genomic_DNA.
DR   RefSeq; WP_012692555.1; NC_012526.1.
DR   AlphaFoldDB; C1D0Q8; -.
DR   SMR; C1D0Q8; -.
DR   STRING; 546414.Deide_05920; -.
DR   PaxDb; C1D0Q8; -.
DR   EnsemblBacteria; ACO45432; ACO45432; Deide_05920.
DR   KEGG; ddr:Deide_05920; -.
DR   eggNOG; COG0292; Bacteria.
DR   HOGENOM; CLU_123265_0_1_0; -.
DR   OMA; GRRKNVW; -.
DR   OrthoDB; 1932144at2; -.
DR   Proteomes; UP000002208; 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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd07026; Ribosomal_L20; 1.
DR   Gene3D; 1.10.1900.20; -; 1.
DR   HAMAP; MF_00382; Ribosomal_L20; 1.
DR   InterPro; IPR005813; Ribosomal_L20.
DR   InterPro; IPR035566; Ribosomal_protein_L20_C.
DR   PANTHER; PTHR10986; PTHR10986; 1.
DR   Pfam; PF00453; Ribosomal_L20; 1.
DR   PRINTS; PR00062; RIBOSOMALL20.
DR   SUPFAM; SSF74731; SSF74731; 1.
DR   TIGRFAMs; TIGR01032; rplT_bact; 1.
DR   PROSITE; PS00937; RIBOSOMAL_L20; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..117
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_1000205706"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   117 AA;  13560 MW;  B4E62CADC4AFD806 CRC64;
     MPRVKTGTVR RRRHKKVLKR AKGFEGSRSK QYRNAFQTLL NAATYEYRDR RNKKRDFRRL
     WVQRINAGAR LHGMNYSTFI GGLKRAGVDL NRKVLADIAA REPEAFKALV DAAKNGK