ID   RL22_PYRAR              Reviewed;         185 AA.
AC   A4WIY9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Pars_0770;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=340102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000660; ABP50356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WIY9; -.
DR   SMR; A4WIY9; -.
DR   STRING; 340102.Pars_0770; -.
DR   PRIDE; A4WIY9; -.
DR   EnsemblBacteria; ABP50356; ABP50356; Pars_0770.
DR   KEGG; pas:Pars_0770; -.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OMA; ANAEYKG; -.
DR   PhylomeDB; A4WIY9; -.
DR   Proteomes; UP000001567; 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..185
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000354546"
SQ   SEQUENCE   185 AA;  21513 MW;  92286D3C80B40260 CRC64;
     MPRHHSYSLS DEKVAELVFR QYGVKITPEQ IAKAYAPEQR MSWKKSIEVA RFITGMTLKQ
     AKAWLEDVVK LKRPIPIKTY KKKQAHHAAP WRGWPVAKWP VKVARRYLQL LENLENNAKF
     KGLDADRVVI VYAAAHKGYR IPNIMPRAFG RATRFDEQTV NVEIVAAELP KEVIPKRYKL
     NLVKR