ID   RK22_ANTAG              Reviewed;         119 AA.
AC   Q85CH6;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=50S ribosomal protein L22, chloroplastic;
GN   Name=rpl22;
OS   Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC   Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC   Anthoceros.
OX   NCBI_TaxID=48387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=12527781; DOI=10.1093/nar/gkg155;
RA   Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT   "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT   chloroplast genome: insight into the earliest land plants.";
RL   Nucleic Acids Res. 31:716-721(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC   TISSUE=Thallus;
RX   PubMed=12711687; DOI=10.1093/nar/gkg327;
RA   Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT   "RNA editing in hornwort chloroplasts makes more than half the genes
RT   functional.";
RL   Nucleic Acids Res. 31:2417-2423(2003).
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   -!- RNA EDITING: Modified_positions=60 {ECO:0000269|PubMed:12527781,
CC       ECO:0000269|PubMed:12711687};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
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DR   EMBL; AB086179; BAC55389.1; -; Genomic_DNA.
DR   EMBL; AB087472; BAC55488.1; -; mRNA.
DR   RefSeq; NP_777453.1; NC_004543.1.
DR   AlphaFoldDB; Q85CH6; -.
DR   SMR; Q85CH6; -.
DR   GeneID; 2553417; -.
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   2: Evidence at transcript level;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA editing;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..119
FT                   /note="50S ribosomal protein L22, chloroplastic"
FT                   /id="PRO_0000125295"
SQ   SEQUENCE   119 AA;  13412 MW;  1FC4E19B72E522BD CRC64;
     MKTNYSNLET QALAKHIRIS ASKVRRVINE IRGRLYEQAP MILEFMLYRA CYPVSQLLSL
     AAANASHNLG LNKADSVTSE VKVDEGTMLK RFEPRAQGRG YPIHKPTSHI TIVIKKKST