ID   RL5_STYCL               Reviewed;         295 AA.
AC   Q26481;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RPL5;
OS   Styela clava (Sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Styelidae; Styela.
OX   NCBI_TaxID=7725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Swalla B.J., Jeffery W.R.;
RL   Submitted (JUN-1996) 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; L78668; AAC05598.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q26481; -.
DR   SMR; Q26481; -.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..295
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000131440"
FT   REGION          251..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..277
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  33903 MW;  650D061AEFB42368 CRC64;
     MGFVKVVKNK AYFKRYQVKY KRRRQGKTDY FARKRLVVQD KNKYNTPKYR MIVRFTNKDI
     VCQIAYARIE GDVVICAAYA HELPRYGVKV GLTNYAAAYC TGLLLSRRLL NKFGLDEIYE
     GQTEIDGDEF YVEDVDGKPG AFRAFLDVGL ARTTTGAKVF GAMKGAADGG LDIPHSTKRF
     PGYDDESGDF SAEVHRSHIF GGHVSNYMKE LEEEDEEAFK RQFSQYIKHG VTADTVEEMY
     TKAHAAIRED PTPKKKTDFA GKTKRWNRKK MTFSQRRDRV KQKKASFLRA KQQEG