ID   RL5_BOMMO               Reviewed;         299 AA.
AC   O76190; Q5UAT6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=60S ribosomal protein L5;
GN   Name=RpL5;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Silk gland;
RA   Yang C.S., Sehnal F.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C108;
RA   Heckel D.G., Morgan M., Shimada T., Mita K.;
RT   "Ribosomal proteins of Bombyx mori.";
RL   Submitted (SEP-2004) 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; AF008229; AAC24960.1; -; mRNA.
DR   EMBL; AY769272; AAV34814.1; -; mRNA.
DR   RefSeq; NP_001037008.1; NM_001043543.1.
DR   AlphaFoldDB; O76190; -.
DR   SMR; O76190; -.
DR   STRING; 7091.BGIBMGA007879-TA; -.
DR   PRIDE; O76190; -.
DR   GeneID; 692557; -.
DR   KEGG; bmor:692557; -.
DR   CTD; 6125; -.
DR   eggNOG; KOG0875; Eukaryota.
DR   HOGENOM; CLU_056222_1_0_1; -.
DR   InParanoid; O76190; -.
DR   OrthoDB; 999609at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..299
FT                   /note="60S ribosomal protein L5"
FT                   /id="PRO_0000131442"
FT   CONFLICT        157
FT                   /note="R -> A (in Ref. 2; AAV34814)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  34379 MW;  A8FD49E0E92B9C70 CRC64;
     MGFVKVVKNK QYFKRYQVKF KRRREGKTDY YARKRLVVQD KNKYNTPKYR LIVRLSNKDV
     TCQVAYSRIE GDHIVCAAYS HELPRYGVKV GLTNYAAAYS TGLLLARRLL QRLGLDTLYT
     GTTDVTGDEY NVEPVDNGPG AFRCYLDVGL ARTTTGRRVF GAMKGAVDGG LNVPHSIKRF
     PGYDAESKKF NAEVHRAHIF GLHVAEYMRS LEQDDEDSFK RQFSKYIKLG VTADAIEAIY
     KKAHEAIRAD PSHKKKELKK DSVKQKRWNK RKLTLAERKN RIKQKKASFI KRLQAQAEA