ID   RL5_EIMTE               Reviewed;         311 AA.
AC   Q5EY89;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RPL5;
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Weybridge;
RX   PubMed=15664658; DOI=10.1016/j.molbiopara.2004.11.011;
RA   Schaap D., Arts G., van Poppel N.F., Vermeulen A.N.;
RT   "De novo ribosome biosynthesis is transcriptionally regulated in Eimeria
RT   tenella, dependent on its life cycle stage.";
RL   Mol. Biochem. Parasitol. 139:239-248(2005).
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; AY588943; AAT97351.1; -; mRNA.
DR   RefSeq; XP_013228068.1; XM_013372614.1.
DR   AlphaFoldDB; Q5EY89; -.
DR   SMR; Q5EY89; -.
DR   GeneID; 25253703; -.
DR   VEuPathDB; ToxoDB:ETH2_1353100; -.
DR   VEuPathDB; ToxoDB:ETH_00022955; -.
DR   OMA; KSQFQGY; -.
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..311
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000291564"
SQ   SEQUENCE   311 AA;  35951 MW;  E138A5341F92E90B CRC64;
     MAFVKAIKNK AYFKRFQVKY RRRREGKTDY AARRRLILQD KNKYNAPKYR FVVRVTNSRV
     LCQVMYATLQ GDRLVCSADS QELTRYGIKV GLTNYSAAYA TGLLLARRLL KQKGLADEFK
     GLEKPSGEEY HIEEVSEERR PFKCVLDVGI VATTVGNRVF GAMKGACDGG LHIPHSNKRF
     PGFTKGEDGA DDSYNPEVHR ARIYGLHVAE YMRTLKEEDP ERYQAQFSAY IRNKIDPDSI
     EKMYEEAFQK IRANPDPVKK EAREVKRVRQ GAMIKTAKSQ YVRNVKLDKE TRKERVLKKI
     QMVADKMAEE E