ID   RL5_DUNSA               Reviewed;         271 AA.
AC   O22608;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RPL5; Synonyms=DSRP1;
OS   Dunaliella salina (Green alga) (Protococcus salinus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX   NCBI_TaxID=3046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ko J.H., Lee S.H.;
RT   "A cDNA encodes a protein sequence homologous to the eukaryotic ribosomal
RT   5S RNA-binding protein from Dunaliella salina.";
RL   Submitted (OCT-1997) 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; AF028833; AAB84056.1; -; mRNA.
DR   PIR; T08009; T08009.
DR   AlphaFoldDB; O22608; -.
DR   SMR; O22608; -.
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..271
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000131450"
FT   REGION          245..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  31218 MW;  482F53833D33B57E CRC64;
     MGYVKVVKTS PYFSRYQVKY RRRRQGKTDY RARLRLVRQD KNKYNTHKYR LVVRFSNKNV
     TCQIVYSTIQ GDVVMAAAYS KELPNYGLKV GLTNYSAAYC VGLLVARRIL TKLNLADTYK
     GQEEPDGEDY NVEPVEDGPK PFYCLLDTGL KRTSTGSKVF AAMKGALDGG LDIPHNEKRF
     VGYADKKLDT EVLQKYIYGG HVAEYQETMQ EEEPEKYQAH FSSYVENEIE PDGIEDMYKE
     VHAKIRENPC PPKKERTKPA DAKRWSPQAH L