ID   RK22_MARPO              Reviewed;         119 AA.
AC   P06388;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=50S ribosomal protein L22, chloroplastic;
GN   Name=rpl22;
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3199436; DOI=10.1016/0022-2836(88)90003-4;
RA   Fukuzawa H., Kohchi T., Sano T., Shirai H., Umesono K., Inokuchi H.,
RA   Ozeki H., Ohyama K.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   III. Gene organization of the large single copy region from rbcL to
RT   trnI(CAU).";
RL   J. Mol. Biol. 203:333-351(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA. {ECO:0000250}.
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:0000250}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
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DR   EMBL; X04465; CAA28125.1; -; Genomic_DNA.
DR   PIR; A02812; R5LV22.
DR   RefSeq; NP_039339.1; NC_001319.1.
DR   AlphaFoldDB; P06388; -.
DR   SMR; P06388; -.
DR   GeneID; 2702572; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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_B; Ribosomal_L22_B; 1.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR   InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR   InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR   PANTHER; PTHR13501; PTHR13501; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; SSF54843; 1.
DR   TIGRFAMs; TIGR01044; rplV_bact; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW   rRNA-binding.
FT   CHAIN           1..119
FT                   /note="50S ribosomal protein L22, chloroplastic"
FT                   /id="PRO_0000125309"
SQ   SEQUENCE   119 AA;  13581 MW;  0697D7FAD080532C CRC64;
     MQTNTSNKKI RAVAKHIHMS PHKVRRVVSQ IRGRSYEQAL MILEFMPYRA CNPILQLLSS
     AAANANHNFG LSKTNLFISE IQVNKGTFFK RFQPRAQGRG YPIHKPTCHI TIVLNILPK