ID   RL22_PYRIL              Reviewed;         185 AA.
AC   A1RVA1;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Pisl_1732;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4184 / JCM 9189 / GEO3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL88883.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000504; ABL88883.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_053240571.1; NC_008701.1.
DR   AlphaFoldDB; A1RVA1; -.
DR   SMR; A1RVA1; -.
DR   STRING; 384616.Pisl_1732; -.
DR   EnsemblBacteria; ABL88883; ABL88883; Pisl_1732.
DR   GeneID; 4618131; -.
DR   KEGG; pis:Pisl_1732; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OrthoDB; 103467at2157; -.
DR   Proteomes; UP000002595; 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_0000354548"
SQ   SEQUENCE   185 AA;  21554 MW;  9C7E85FDD7A2A831 CRC64;
     MPQHQNYSLS EEDVIQLVFR KYGVKITSEQ IVRAYAPEQK MSWKKSVEVA RFIKGMTLRQ
     AKSWLEDVVK MKRPIPIKTF KKKQAHHAVP WSGWPVAKWP VKVAKRFLDL LENLENNAKF
     RGLDVERVVI VHAAAHKGYR IPNIMPRAFG RATRFDEQTV NVEVIAAELP KEVVPKRYKL
     NLVKR