RL5_CUCSA
ID RL5_CUCSA Reviewed; 302 AA.
AC Q6UNT2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=60S ribosomal protein L5;
GN Name=RPL5;
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15045660; DOI=10.1055/s-2004-817803;
RA Kim M.-S., Kim Y.C., Cho B.H.;
RT "Gene expression analysis in cucumber leaves primed by root colonization
RT with Pseudomonas chlororaphis O6 upon challenge-inoculation with
RT Corynespora cassicola.";
RL Plant Biol. 6:105-108(2004).
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; AY365248; AAQ72789.1; -; mRNA.
DR RefSeq; NP_001267659.1; NM_001280730.1.
DR AlphaFoldDB; Q6UNT2; -.
DR SMR; Q6UNT2; -.
DR STRING; 3659.XP_004171966.1; -.
DR PRIDE; Q6UNT2; -.
DR EnsemblPlants; KGN51654; KGN51654; Csa_5G588730.
DR GeneID; 101216379; -.
DR Gramene; KGN51654; KGN51654; Csa_5G588730.
DR KEGG; csv:101216379; -.
DR eggNOG; KOG0875; Eukaryota.
DR OMA; KSQFQGY; -.
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..302
FT /note="60S ribosomal protein L5"
FT /id="PRO_0000131445"
SQ SEQUENCE 302 AA; 34329 MW; 229AA398BE8BCB2A CRC64;
MAFAKAQKTK AYFKRYQVKF KRRREGKTDY RARIRLINQD KNKYNTPKYR FVVRTSNKDI
TAQIISASIA GDLVLASAYS HELPQYGLEV GLTNYAAAYC TGLLLARRVL KMLEMDAEYE
GNVEATGEDY SVEPADTRRP FRALLDVGLI RTTTGNRVFG ALKGALDGGL DIPHSDKRFA
GYAKNGQQLD VEVHRKYIFG GHVAAYMRTL MEDEPEKYQS HFSEYIKKGI EADELEGLYK
KVHAAIRANP IAKKSDKPQP KAHKRYNLKK LTYDERKARL VERLNALNSA ADGDDDDDED
DE