ID   RL11_PYRFU              Reviewed;         164 AA.
AC   Q8TZK0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
DE   AltName: Full=Large ribosomal subunit protein uL11;
GN   Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=PF1991;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2] {ECO:0007744|PDB:4V6U}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.60 ANGSTROMS) IN THE 70S RIBOSOME, AND
RP   SUBUNIT.
RX   PubMed=23222135; DOI=10.1093/nar/gks1259;
RA   Armache J.P., Anger A.M., Marquez V., Franckenberg S., Frohlich T.,
RA   Villa E., Berninghausen O., Thomm M., Arnold G.J., Beckmann R.,
RA   Wilson D.N.;
RT   "Promiscuous behaviour of archaeal ribosomal proteins: implications for
RT   eukaryotic ribosome evolution.";
RL   Nucleic Acids Res. 41:1284-1293(2013).
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC       interact with GTP-bound translation factors. {ECO:0000255|HAMAP-
CC       Rule:MF_00736}.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit
CC       (PubMed:23222135). Interacts with L10 and the large rRNA to form the
CC       base of the stalk. L10 forms an elongated spine to which L12 dimers
CC       bind in a sequential fashion forming a multimeric L10(L12)X complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00736, ECO:0000269|PubMed:23222135}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR   EMBL; AE009950; AAL82115.1; -; Genomic_DNA.
DR   RefSeq; WP_011013135.1; NZ_CP023154.1.
DR   PDB; 4V6U; EM; 6.60 A; BH=1-164.
DR   PDBsum; 4V6U; -.
DR   AlphaFoldDB; Q8TZK0; -.
DR   SMR; Q8TZK0; -.
DR   STRING; 186497.PF1991; -.
DR   PRIDE; Q8TZK0; -.
DR   EnsemblBacteria; AAL82115; AAL82115; PF1991.
DR   GeneID; 41713814; -.
DR   KEGG; pfu:PF1991; -.
DR   PATRIC; fig|186497.12.peg.2067; -.
DR   eggNOG; arCOG04372; Archaea.
DR   HOGENOM; CLU_074237_4_0_2; -.
DR   OMA; CKQFNAK; -.
DR   OrthoDB; 98187at2157; -.
DR   PhylomeDB; Q8TZK0; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00349; Ribosomal_L11; 1.
DR   Gene3D; 1.10.10.250; -; 1.
DR   Gene3D; 3.30.1550.10; -; 1.
DR   HAMAP; MF_00736; Ribosomal_L11; 1.
DR   InterPro; IPR000911; Ribosomal_L11/L12.
DR   InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR   InterPro; IPR020783; Ribosomal_L11_C.
DR   InterPro; IPR036769; Ribosomal_L11_C_sf.
DR   InterPro; IPR020785; Ribosomal_L11_CS.
DR   InterPro; IPR020784; Ribosomal_L11_N.
DR   PANTHER; PTHR11661; PTHR11661; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF46906; SSF46906; 1.
DR   SUPFAM; SSF54747; SSF54747; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..164
FT                   /note="50S ribosomal protein L11"
FT                   /id="PRO_0000104444"
SQ   SEQUENCE   164 AA;  17635 MW;  6C6C5EA7F3A49F82 CRC64;
     MPKQVVEVLV EGGKATPGPP LGPAIGPLGL NVKQVVDKIN EATKDFAGMQ VPVKIIVDPV
     TKQFEIEVGV PPTSQLIKKE LGLEKGSGEP KHNIVGNLTM EQVIKIAKMK KDQMLALTLK
     AAAKEVIGTA LSMGVTVEGK DPREVQKEID EGVYDELFEK AEKE