ID   RL22_METM7              Reviewed;         153 AA.
AC   A6VGY9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=MmarC7_0648;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR65715.1; -; Genomic_DNA.
DR   RefSeq; WP_011867950.1; NC_009637.1.
DR   AlphaFoldDB; A6VGY9; -.
DR   SMR; A6VGY9; -.
DR   STRING; 426368.MmarC7_0648; -.
DR   EnsemblBacteria; ABR65715; ABR65715; MmarC7_0648.
DR   GeneID; 5738159; -.
DR   KEGG; mmz:MmarC7_0648; -.
DR   eggNOG; arCOG04098; Archaea.
DR   HOGENOM; CLU_083987_0_2_2; -.
DR   OMA; ANAEYKG; -.
DR   OrthoDB; 103467at2157; -.
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; IPR018260; Ribosomal_L22/L17_CS.
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.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..153
FT                   /note="50S ribosomal protein L22"
FT                   /id="PRO_0000354543"
SQ   SEQUENCE   153 AA;  17471 MW;  C8639AF8153978F9 CRC64;
     MAKLKYKVEA DPKNTARAMG RTLRISRKHA IELCRELSGM KLDAAVAYLN RVIALETPVP
     FKVHNKDLPH RKGKIGTHSG RFPQKASLEI LQVLDNAKKN AEQKGLNTEK LRIKHISSNR
     GFTIKRYMPR AFGRASPKNQ ETIHIQVILE EFY