ID   RL1_PYRFU               Reviewed;         216 AA.
AC   Q8TZJ9;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE   AltName: Full=Large ribosomal subunit protein uL1;
GN   Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=PF1992;
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: Binds directly to 23S rRNA. Probably involved in E site tRNA
CC       release. {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of its operon by binding to its mRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01318, ECO:0000269|PubMed:23222135}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
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; AE009950; AAL82116.1; -; Genomic_DNA.
DR   RefSeq; WP_011013136.1; NZ_CP023154.1.
DR   PDB; 4V4N; EM; 9.00 A; A=1-216.
DR   PDB; 4V6U; EM; 6.60 A; BA=1-216.
DR   PDBsum; 4V4N; -.
DR   PDBsum; 4V6U; -.
DR   AlphaFoldDB; Q8TZJ9; -.
DR   SMR; Q8TZJ9; -.
DR   STRING; 186497.PF1992; -.
DR   EnsemblBacteria; AAL82116; AAL82116; PF1992.
DR   GeneID; 41713815; -.
DR   KEGG; pfu:PF1992; -.
DR   PATRIC; fig|186497.12.peg.2068; -.
DR   eggNOG; arCOG04289; Archaea.
DR   HOGENOM; CLU_062853_4_0_2; -.
DR   OMA; GWTDVDV; -.
DR   OrthoDB; 70269at2157; -.
DR   PhylomeDB; Q8TZJ9; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_A; Ribosomal_L1_A; 1.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR023674; Ribosomal_L1-like.
DR   InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR023669; Ribosomal_L1_arc.
DR   InterPro; IPR023673; Ribosomal_L1_CS.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; SSF56808; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Repressor; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW   tRNA-binding.
FT   CHAIN           1..216
FT                   /note="50S ribosomal protein L1"
FT                   /id="PRO_0000125809"
SQ   SEQUENCE   216 AA;  23852 MW;  5B3B93D187EA6A78 CRC64;
     MPFDRQKIVK AVKEAKARAK PRNFTQSVEV AVNLKDIDLK RPENRFKLEV VLPHGRGKDV
     KIAVIADGAV AEAARKLGLD VISSAELEEI ASSPRQARKL AKKYDFFIAE APLMPKIGRY
     LGRYLGPRNK MPVVVPPTLT DLTPIVEKLK KTVRIQLKNN PVVHAPVGTE KMSDEEIAEN
     IEAVLNAIIG KLERGESQVK SVYVKTTMGP AVKIEG