ID   RL5_LYSTE               Reviewed;         297 AA.
AC   Q56FG6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RpL5;
OS   Lysiphlebus testaceipes (Greenbugs aphid parastoid).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida;
OC   Ichneumonoidea; Braconidae; Aphidiinae; Lysiphlebus.
OX   NCBI_TaxID=77504;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Florida;
RA   Weathersbee A.A. III, Hunter W.B., Panchal T.D., Dang P.M.;
RT   "Ribosomal protein sequences from Lysiphlebus testaceipes.";
RL   Submitted (MAR-2005) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY961534; AAX62436.1; -; mRNA.
DR   AlphaFoldDB; Q56FG6; -.
DR   SMR; Q56FG6; -.
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..297
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000291560"
SQ   SEQUENCE   297 AA;  34414 MW;  A9629D7EBE1264D4 CRC64;
     MGFVKVVKNK QYFKRFQVKY KRRREGKTDY YARKRLTVQD KSKYNTPKYR LIVRLSNKDI
     TCQIAYSRIE GDRIVCAAYS HELPKYGIKV GLTNYAAAYC TGLLLARRLL KQLKLDTLYT
     GTTEVDGDEY NVEEHDDGPG AFRCYLDTGL MRTTTGARIF GAMKGAVDGG LNIPHSTKRF
     PGYDNESKSF NADVHRQHIF AHHIANYMKT LEENEPENFQ RQFSQYIKNG ITADGIEEMY
     KKAHEAIRAD PDRAEIVKTK EPVKKRWNRA KLTLSERKDR VKQIKASFQK KLEETEA