ID   RL11_LEICH              Reviewed;         188 AA.
AC   P42922;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=60S ribosomal protein L11;
GN   Name=RPL11;
OS   Leishmania chagasi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=44271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7477109; DOI=10.1016/0166-6851(94)00055-r;
RA   Love D.C., Wilson M.E., Mosser D.M.;
RT   "Cloning and characterization of the ribosomal l11 gene from Leishmania
RT   spp.";
RL   Mol. Biochem. Parasitol. 71:261-264(1995).
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. {ECO:0000250|UniProtKB:P0C0W9}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P0C0W9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P0C0W9}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC       {ECO:0000305}.
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DR   EMBL; U16018; AAC46921.1; -; mRNA.
DR   AlphaFoldDB; P42922; -.
DR   SMR; P42922; -.
DR   PRIDE; P42922; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.30.1440.10; -; 1.
DR   InterPro; IPR002132; Ribosomal_L5.
DR   InterPro; IPR031309; Ribosomal_L5_C.
DR   InterPro; IPR020929; Ribosomal_L5_CS.
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.
DR   PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..188
FT                   /note="60S ribosomal protein L11"
FT                   /id="PRO_0000125091"
SQ   SEQUENCE   188 AA;  21661 MW;  9E63D283E0E2E96E CRC64;
     MVAESKAANP MREIVVKKLC INICVGESGD RLTRASKVLE QLCEQTPVLS RARLTVRTFG
     IRRNEKIAVH CTVRGKKAEE LLEKGLKVKE FELKSYNFSD TGSFGFGIDE HIDLGIKYDP
     STGIYGMDFY VVLGRRGERV AHRKRKCSRV GHSHHVTKEE AMKWFEKVHD GIIFQAKKKK
     KMIRRRRR