ID   RL6_AERPE               Reviewed;         182 AA.
AC   Q9YF91;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN   Name=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=APE_0350;
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: This protein binds to the 23S rRNA, and is important in its
CC       secondary structure. It is located near the subunit interface in the
CC       base of the L7/L12 stalk, and near the tRNA binding site of the
CC       peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01365}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR   EMBL; BA000002; BAA79305.1; -; Genomic_DNA.
DR   PIR; E72726; E72726.
DR   AlphaFoldDB; Q9YF91; -.
DR   SMR; Q9YF91; -.
DR   STRING; 272557.APE_0350; -.
DR   EnsemblBacteria; BAA79305; BAA79305; APE_0350.
DR   KEGG; ape:APE_0350; -.
DR   PATRIC; fig|272557.25.peg.270; -.
DR   eggNOG; arCOG04090; Archaea.
DR   OMA; VFQDGIY; -.
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; 3.90.930.12; -; 2.
DR   HAMAP; MF_01365_A; Ribosomal_L6_A; 1.
DR   InterPro; IPR000702; Ribosomal_L6.
DR   InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR   InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR   InterPro; IPR002359; Ribosomal_L6_CS2.
DR   InterPro; IPR019907; Ribosomal_L6P_arc.
DR   PANTHER; PTHR11655; PTHR11655; 1.
DR   Pfam; PF00347; Ribosomal_L6; 2.
DR   PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR   SUPFAM; SSF56053; SSF56053; 2.
DR   TIGRFAMs; TIGR03653; uL6_arch; 1.
DR   PROSITE; PS00700; RIBOSOMAL_L6_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..182
FT                   /note="50S ribosomal protein L6"
FT                   /id="PRO_0000131081"
SQ   SEQUENCE   182 AA;  20266 MW;  FCE5655691974A5C CRC64;
     MAKDVHVVER VEVPEGVTVS IDGMRVKVSG PKGEVERDFS HARGVLIRLE DNSVVVESFF
     AKARQRALVG AIAGHIRNMI KGVQGGFRYK LKIMYSHFPI NVKVEGDKFI ISNFLGEKGL
     RIARIMPGVK VQVKGSDVIV EGIDVEKVAQ TAANIELATK VKDKDRRKFM DGIYIYEREV
     IA