ID   RL22_METS3              Reviewed;         154 AA.
AC   A5UL84;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=Msm_0757;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86962.1; -; Genomic_DNA.
DR   RefSeq; WP_004033210.1; NC_009515.1.
DR   AlphaFoldDB; A5UL84; -.
DR   SMR; A5UL84; -.
DR   STRING; 420247.Msm_0757; -.
DR   EnsemblBacteria; ABQ86962; ABQ86962; Msm_0757.
DR   GeneID; 5215859; -.
DR   KEGG; msi:Msm_0757; -.
DR   PATRIC; fig|420247.28.peg.754; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OMA; ANAEYKG; -.
DR   Proteomes; UP000001992; 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..154
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_1000052609"
SQ   SEQUENCE   154 AA;  17319 MW;  FEA6495E557C4BDD CRC64;
     MANKYAYNKE TNEAKTARAM AKSLKISPKH CVEICNAIRG MEVTKAKNYL EDVIDMKKSV
     PFKRHNRQVG HRKGQEGWAA GRYPVKAAEQ VLKVLENAEA NAEYKGMDTE NLFIEHISSH
     RGVVLPGVIP RAFGRMTPFN TPTTHIQIVL QEAN