ID   RL13_SPOFR              Reviewed;         219 AA.
AC   Q962U1;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=60S ribosomal protein L13;
GN   Name=RpL13;
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. As part of the LSU, it is probably required for its formation
CC       and the maturation of rRNAs. {ECO:0000250|UniProtKB:P26373}.
CC   -!- SUBUNIT: Component of the 60S large ribosomal subunit (LSU).
CC       {ECO:0000250|UniProtKB:P26373}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26373}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 family.
CC       {ECO:0000305}.
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DR   EMBL; AF400183; AAK92155.1; -; mRNA.
DR   AlphaFoldDB; Q962U1; -.
DR   SMR; Q962U1; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_00499; Ribosomal_L13e; 1.
DR   InterPro; IPR001380; Ribosomal_L13e.
DR   InterPro; IPR018256; Ribosomal_L13e_CS.
DR   PANTHER; PTHR11722; PTHR11722; 1.
DR   Pfam; PF01294; Ribosomal_L13e; 1.
DR   PROSITE; PS01104; RIBOSOMAL_L13E; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..219
FT                   /note="60S ribosomal protein L13"
FT                   /id="PRO_0000192926"
FT   REGION          198..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   219 AA;  24963 MW;  9FF918EB07CA3449 CRC64;
     MGKGNNMIPN GHFHKDWQRF VKTWFNQPAR RHRRKQNRIK KAKAVAPRPA AGPLRPVVRC
     PTIRYHTKVR AGRGFTLREI RAAGLNPAFA RTIGIAVDPR RRNKSVESLQ VNVQRLKEYR
     ARLILFPKGK KVLKGEANEE ERKLATQLRG PLMPVQQPAP KSIARAITEE EKDFKAYQYL
     RGARSIAKLV GIRAKRLKDA AENPDDVTKA PTAVKRNKT