ID   RL5_TOXCI               Reviewed;         300 AA.
AC   Q5XUC7;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RpL5;
OS   Toxoptera citricida (Brown citrus aphid) (Aphis citricidus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC   Aphidoidea; Aphididae; Aphidini; Aphis; Toxoptera.
OX   NCBI_TaxID=223852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hunter W.B., Dang P.M.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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:P26321}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU).
CC       {ECO:0000250|UniProtKB:P26321}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P26321}. Nucleus
CC       {ECO:0000250|UniProtKB:P26321}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
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DR   EMBL; AY737527; AAU84920.1; -; mRNA.
DR   AlphaFoldDB; Q5XUC7; -.
DR   SMR; Q5XUC7; -.
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:0008097; F:5S rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   HAMAP; MF_01337_A; Ribosomal_L18_A; 1.
DR   InterPro; IPR005485; Rbsml_L5_euk/L18_arc.
DR   InterPro; IPR025607; Rbsml_L5e_C.
DR   PANTHER; PTHR23410; PTHR23410; 1.
DR   Pfam; PF14204; Ribosomal_L18_c; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 1.
DR   PRINTS; PR00058; RIBOSOMALL5.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..300
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000291561"
FT   REGION          246..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   300 AA;  34752 MW;  C2812736084C341F CRC64;
     MGFVKVVKNK QYFKRYQVKF KRRREGKTDY YARKRLIVQD KNKYDTPKYR LIVRFSNRDI
     TCQVAHSRIE GDKIVCAAYS HELPKYGVKV GLTNYAAAYC TGLLVARRLL KKLGLDRLYE
     GLKEANGEEY YVEPADEGPN AFRCNLDVGL MKTSTGARVF GAMKGAVDGG FNIPHSVKRF
     PGYDAEAKEY SAETHRKHIL GLHVAEYMRK LEEEDEDAFN RQFSQYIKLG IVADDLENMY
     KKAHENIRSD PKRDRKPKKD VSKEPKRWNA KKLTNAERKQ RVVEAKAAYL KELQGEEMES