ID   RL5_HELAN               Reviewed;         297 AA.
AC   O65353;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RPL5A;
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. HA300; TISSUE=Pollen;
RA   Eliasson A., Hammann P., Steinmetz A.;
RT   "Coding sequence for an RPL5A-related protein from sunflower.";
RL   Submitted (MAY-1998) 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; AF066077; AAC17448.1; -; mRNA.
DR   PIR; T12615; T12615.
DR   AlphaFoldDB; O65353; -.
DR   SMR; O65353; -.
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_0000131446"
FT   REGION          258..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  33914 MW;  AA6707B1B9B0692B CRC64;
     MGFVKVVKNK QYFKRYQVKF KRRREGKTDY FARKRLIAQD KNKYNTPKYR LVVRFSNRDI
     TCQVAYSRIE GDKILCAAYA HELPQYGVKV GLTNYAAAYC TGLLLARKLL SQLGLDKLYI
     GSTEVTGEEF NVKPVEDGPG AFRCYLDVGL MRTTTGARVF GAMKGAVDGG LNILHSTKRF
     PGFDSESKEF NADVHRQHIF GQHVAEYMRQ LAEEDDEAYK RQFSQYIKLG LNADAIEGLY
     KKAHEAIRAN PARKTVAKKA HPKKRWTEKK LTREQRQGKV AAAKAEWLKK IEAGEVE