ID   RL11_SPOFR              Reviewed;         195 AA.
AC   Q962U2;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=60S ribosomal protein L11;
GN   Name=RpL11;
OS   Spodoptera frugiperda (Fall armyworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14668217; DOI=10.1093/bioinformatics/btg324;
RA   Landais I., Ogliastro M., Mita K., Nohata J., Lopez-Ferber M.,
RA   Duonor-Cerutti M., Shimada T., Fournier P., Devauchelle G.;
RT   "Annotation pattern of ESTs from Spodoptera frugiperda Sf9 cells and
RT   analysis of the ribosomal protein genes reveal insect-specific features and
RT   unexpectedly low codon usage bias.";
RL   Bioinformatics 19:2343-2350(2003).
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; AF400182; AAK92154.1; -; mRNA.
DR   AlphaFoldDB; Q962U2; -.
DR   SMR; Q962U2; -.
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   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..195
FT                   /note="60S ribosomal protein L11"
FT                   /id="PRO_0000125090"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   195 AA;  22346 MW;  A34A304552E1BFB5 CRC64;
     MARVPPPALK KDKKEKKPPK DNSKNVMRNL HIRKLCLNIC VGESGDRLTR AAKVLEQLTG
     QQPVFSKARY TVRSFGIRRN EKIAVHCTVR GAKAEEILER GLKVREYELR RDNFSATGNF
     GFGIQEHIDL GIKYDPSIGI YGLDFYVVLG PTRIQCTTQK TQDWQGWIPP IVLTKEDAMK
     WFQQKYDGII LNSKK