ID   RL3_AERPE               Reviewed;         344 AA.
AC   Q9YFM2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN   Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=APE_0227;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC       near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L14 and L24e. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR   EMBL; BA000002; BAA79139.1; -; Genomic_DNA.
DR   PIR; A72780; A72780.
DR   AlphaFoldDB; Q9YFM2; -.
DR   SMR; Q9YFM2; -.
DR   STRING; 272557.APE_0227; -.
DR   EnsemblBacteria; BAA79139; BAA79139; APE_0227.
DR   KEGG; ape:APE_0227; -.
DR   PATRIC; fig|272557.25.peg.161; -.
DR   eggNOG; arCOG04070; Archaea.
DR   OMA; HQRTEYN; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F: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   Gene3D; 4.10.960.10; -; 1.
DR   HAMAP; MF_01325_A; Ribosomal_L3_A; 1.
DR   InterPro; IPR045077; L3_arc_euk.
DR   InterPro; IPR000597; Ribosomal_L3.
DR   InterPro; IPR019928; Ribosomal_L3_arc.
DR   InterPro; IPR019926; Ribosomal_L3_CS.
DR   InterPro; IPR044892; Ribosomal_L3_dom_3_arc_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR11363; PTHR11363; 1.
DR   Pfam; PF00297; Ribosomal_L3; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   TIGRFAMs; TIGR03626; L3_arch; 1.
DR   PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..344
FT                   /note="50S ribosomal protein L3"
FT                   /id="PRO_0000077205"
SQ   SEQUENCE   344 AA;  38643 MW;  55F8511293BC8580 CRC64;
     MGARKKRAPR RGSLGFSPRK RASRLVPRVK RWPEVDIGKP VPLAFLGYRA GMTHVFMVDD
     RPGRPTSGKE IFVPVTIVET PPMFVAAVRL YGYDPNRGRY SLGEAWAQPP PELELQRRIS
     TLGSFDTDKM LKSLEERLDK AEDVRLIAAS QPKLAGGLSK KKPDLLEIKV GGVSDVTKLF
     DYAKDVLGNL IAVNDVFEEG QLVDVIAVTK GKGFQGVIKR WGVKELPRWH KHRKGSRRIG
     ARSHGRSTFW ETPQAGQTGF HRRTEYNKRI LMIDDDGYKV TPAGGFLRYG VVRSTFVMLS
     GSIPGTPKRP IVMRWAIRPP EWYLKLGVRK PEITYISLAS KQGV