ID   RL5_SUBDO               Reviewed;         293 AA.
AC   Q4KTI3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RPL5;
OS   Suberites domuncula (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha; Suberitida;
OC   Suberitidae; Suberites.
OX   NCBI_TaxID=55567;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16229974; DOI=10.1016/j.gene.2005.08.015;
RA   Perina D., Cetkovic H., Harcet M., Premzl M., Lukic-Bilela L.,
RA   Mueller W.E.G., Gamulin V.;
RT   "The complete set of ribosomal proteins from the marine sponge Suberites
RT   domuncula.";
RL   Gene 366:275-284(2006).
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; AY857416; AAX48835.1; -; mRNA.
DR   AlphaFoldDB; Q4KTI3; -.
DR   SMR; Q4KTI3; -.
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..293
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000291566"
FT   REGION          247..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..283
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   293 AA;  33965 MW;  4533AC81577BBC1A CRC64;
     MPFVKVIKNK AYFKRYQVKF RRRREGKTDY RARKRLVVQD KNKYNTPKYR IVIRFTNTDI
     ICQIIYAKIE GDKVLVSAYA HELPRYGVKV GLTNYAAAYC TGLLLARRLL TNLGLADKYA
     GQTDIDGEDF NVEHMGDGPR PFRAFLDVGL TRTTTGNRVF AAMKGAVDGG IDIPHSPSRF
     VGYDEESSQL EADKLRQYIF GGHVSDYMKY LQEEDEEKYK AHFSRFIKEG ITADSMEQMY
     RDAHAKIRAN PAHEKKQPRD GLVKKRWNRA KMSLKQKRDR VKQKKAAYLK TLE