RL11_MEDSA
ID RL11_MEDSA Reviewed; 181 AA.
AC P46287;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=60S ribosomal protein L11;
DE AltName: Full=L5;
GN Name=RPL11; Synonyms=RPL5;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nagyszenasi; TISSUE=Leaf;
RX PubMed=7811977; DOI=10.1007/bf00040700;
RA Asemota O., Breda C., Sallaud C., El-Turk J., De Kozak I., Buffard D.,
RA Esnault R., Kondorosi A.;
RT "Cloning and expression of a cDNA encoding a cytoplasmic L5 ribosomal
RT protein from alfalfa (Medicago sativa L.).";
RL Plant Mol. Biol. 26:1201-1205(1994).
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:P0C0W9}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C0W9}. Cytoplasm
CC {ECO:0000250|UniProtKB:P0C0W9}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL5 family.
CC {ECO:0000305}.
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DR EMBL; X78284; CAA55090.1; -; mRNA.
DR PIR; S51819; S51819.
DR AlphaFoldDB; P46287; -.
DR SMR; P46287; -.
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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.1440.10; -; 1.
DR InterPro; IPR002132; Ribosomal_L5.
DR InterPro; IPR031309; Ribosomal_L5_C.
DR InterPro; IPR020929; Ribosomal_L5_CS.
DR InterPro; IPR022803; Ribosomal_L5_dom_sf.
DR InterPro; IPR031310; Ribosomal_L5_N.
DR PANTHER; PTHR11994; PTHR11994; 1.
DR Pfam; PF00281; Ribosomal_L5; 1.
DR Pfam; PF00673; Ribosomal_L5_C; 1.
DR PIRSF; PIRSF002161; Ribosomal_L5; 1.
DR SUPFAM; SSF55282; SSF55282; 1.
DR PROSITE; PS00358; RIBOSOMAL_L5; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..181
FT /note="60S ribosomal protein L11"
FT /id="PRO_0000125098"
SQ SEQUENCE 181 AA; 20683 MW; EF4D61FB554FAF8A CRC64;
MASEKKLSNP MREIKVQKLV LNISVGESGD RLTRAAKVLE QLSGQTPVFS KARYTVRSFG
IRRNEKIACY VTVRGDKAMQ LLESGLKVKE YELLRRNFSD TGCFGFGIQE HIDLGIKYDP
STGIYGMDFF VVLERPGYRV GRRRRCKARV GIQHRVTKDD AMKWFQVKYE GVILNKSQAI
V