ID   RL22_THEVO              Reviewed;         148 AA.
AC   Q97BX2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=TV0333;
GN   ORFNames=TVG0335848;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA. It makes
CC       multiple contacts with different domains of the 23S rRNA in the
CC       assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC   -!- FUNCTION: The globular domain of the protein is located near the
CC       polypeptide exit tunnel on the outside of the subunit, while an
CC       extended beta-hairpin is found that lines the wall of the exit tunnel
CC       in the center of the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01331}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR   EMBL; BA000011; BAB59475.1; -; Genomic_DNA.
DR   RefSeq; WP_048054074.1; NC_002689.2.
DR   AlphaFoldDB; Q97BX2; -.
DR   SMR; Q97BX2; -.
DR   STRING; 273116.14324548; -.
DR   EnsemblBacteria; BAB59475; BAB59475; BAB59475.
DR   GeneID; 1440845; -.
DR   KEGG; tvo:TVG0335848; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OMA; ANAEYKG; -.
DR   OrthoDB; 103467at2157; -.
DR   PhylomeDB; Q97BX2; -.
DR   Proteomes; UP000001017; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00336; Ribosomal_L22; 1.
DR   Gene3D; 3.90.470.10; -; 1.
DR   HAMAP; MF_01331_A; Ribosomal_L22_A; 1.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR   InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR   PANTHER; PTHR11593; PTHR11593; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; SSF54843; 1.
DR   TIGRFAMs; TIGR01038; uL22_arch_euk; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..148
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000125291"
SQ   SEQUENCE   148 AA;  16557 MW;  8F82F3D5192F4D90 CRC64;
     MKGYSMSVDE NNARARIVEA DISLKDAVNI AHHIRGMKLD YAKQILEDVV SKKYAIPYFR
     YLDSVSHRPG KGPGRYPVKA AKVFIDLLSN VENNAEFKGM NTDSLIIKHV AANKGRMIKK
     YTPKAYGRAG ANFKDLINLE VIVTEGDQ