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 27-MAR-2024, entry version 50.
DE RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000305};
DE AltName: 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:0022626; C:cytosolic ribosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; 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 CDD; cd00432; Ribosomal_L18_L5e; 1.
DR Gene3D; 3.30.420.100; -; 1.
DR HAMAP; MF_01337_A; Ribosomal_uL18_A; 1.
DR InterPro; IPR005485; Rbsml_uL18_euk/arc.
DR InterPro; IPR025607; Ribosomal_uL18_C_euk.
DR PANTHER; PTHR23410:SF12; 60S RIBOSOMAL PROTEIN L5; 1.
DR PANTHER; PTHR23410; RIBOSOMAL PROTEIN L5-RELATED; 1.
DR Pfam; PF14204; Ribosomal_L18_c; 1.
DR Pfam; PF17144; Ribosomal_L5e; 1.
DR PRINTS; PR00058; RIBOSOMALL5.
DR SUPFAM; SSF53137; Translational machinery components; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..293
FT /note="Large ribosomal subunit protein uL18"
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
//
