RL11_TETTH
ID RL11_TETTH Reviewed; 172 AA.
AC P24119;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=60S ribosomal protein L11;
DE AltName: Full=L21;
GN Name=RPL11;
OS Tetrahymena thermophila.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2016059; DOI=10.1016/0378-1119(91)90169-c;
RA Rosendahl G., Andreasen P.H., Kristiansen K.;
RT "Structure and evolution of the Tetrahymena thermophila gene encoding
RT ribosomal protein L21.";
RL Gene 98:161-167(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 60S RIBOSOME.
RX PubMed=22052974; DOI=10.1126/science.1211204;
RA Klinge S., Voigts-Hoffmann F., Leibundgut M., Arpagaus S., Ban N.;
RT "Crystal structure of the eukaryotic 60S ribosomal subunit in complex with
RT initiation factor 6.";
RL Science 334:941-948(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37892; AAB00917.1; -; Genomic_DNA.
DR PIR; JU0456; JU0456.
DR PDB; 4V8P; X-ray; 3.52 A; BD/CD/ED/GD=1-172.
DR PDBsum; 4V8P; -.
DR AlphaFoldDB; P24119; -.
DR SMR; P24119; -.
DR IntAct; P24119; 1.
DR OMA; QTETIKW; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..172
FT /note="60S ribosomal protein L11"
FT /id="PRO_0000125093"
SQ SEQUENCE 172 AA; 19718 MW; 1BD0B725D23A9338 CRC64;
MTDKKENKMR EVKIAKLVIN CCVGESGDKL TKAAKVLKDL SGQEPVFSRA RYTIRSFGIK
RNEKMAVHVT IRGDKARDIL TRGLKVKEME LRKKNFSNTG NFGFGIQEHI DLGMKYDPST
GIFGMDFYVV LERPGTRVAR RRRATSRVGN NQMISKEECI NWFKTEFEGN VY