ID   RL20_ONYPE              Reviewed;         207 AA.
AC   Q6YPI5;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=50S ribosomal protein L20 {ECO:0000255|HAMAP-Rule:MF_00382};
GN   Name=rplT {ECO:0000255|HAMAP-Rule:MF_00382}; OrderedLocusNames=PAM_742;
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=262768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M;
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(2004).
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; AP006628; BAD04827.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6YPI5; -.
DR   SMR; Q6YPI5; -.
DR   STRING; 262768.PAM_742; -.
DR   PRIDE; Q6YPI5; -.
DR   EnsemblBacteria; BAD04827; BAD04827; PAM_742.
DR   KEGG; poy:PAM_742; -.
DR   eggNOG; COG0292; Bacteria.
DR   HOGENOM; CLU_082429_0_0_14; -.
DR   OMA; RINAGAM; -.
DR   OrthoDB; 1661719at2; -.
DR   BioCyc; OYEL262768:G1G26-897-MON; -.
DR   Proteomes; UP000002523; 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:0006353; P:DNA-templated transcription, termination; 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; IPR011112; Rho_N.
DR   InterPro; IPR036269; Rho_N_sf.
DR   InterPro; IPR005813; Ribosomal_L20.
DR   InterPro; IPR035566; Ribosomal_protein_L20_C.
DR   PANTHER; PTHR10986; PTHR10986; 1.
DR   Pfam; PF07498; Rho_N; 1.
DR   Pfam; PF00453; Ribosomal_L20; 1.
DR   PRINTS; PR00062; RIBOSOMALL20.
DR   SMART; SM00959; Rho_N; 1.
DR   SUPFAM; SSF68912; SSF68912; 1.
DR   SUPFAM; SSF74731; SSF74731; 1.
DR   TIGRFAMs; TIGR01032; rplT_bact; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..207
FT                   /note="50S ribosomal protein L20"
FT                   /id="PRO_0000355476"
FT   REGION          117..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   207 AA;  23759 MW;  B5EB1338A0269C0A CRC64;
     MAKISFTPAR HRRRKKVLKM AKGYFGSKST LYKTAHEQVM RSLQYAYRDR KQRKRDFRKL
     WISRINAGAM LCGMQYSYLM HGLALAKVDV NRKVLADLAH LQPGPVESVK AVEVLQQETQ
     PQPEEKTSLQ PEKVLSTELS EEKSDDTLET KPQTTQVKAK KPSLDLSKML LHELKKLAKE
     HKVPNFHKLK KAEIVTALKK ALAKKII