ID   RK22_PEA                Reviewed;         204 AA.
AC   P23408;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=50S ribosomal protein L22, chloroplastic;
DE   AltName: Full=CL22;
DE   Flags: Precursor;
GN   Name=rpl22;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=1915281; DOI=10.1002/j.1460-2075.1991.tb07859.x;
RA   Gantt J.S., Baldauf S.L., Calie P.J., Weeden N.F., Palmer J.D.;
RT   "Transfer of rpl22 to the nucleus greatly preceded its loss from the
RT   chloroplast and involved the gain of an intron.";
RL   EMBO J. 10:3073-3078(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- MISCELLANEOUS: In legumes L22 is not encoded in the chloroplast but by
CC       a nuclear gene.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
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DR   EMBL; M60952; AAA33657.1; -; mRNA.
DR   EMBL; M60951; AAA33656.1; -; Genomic_DNA.
DR   PIR; S17314; S17314.
DR   AlphaFoldDB; P23408; -.
DR   SMR; P23408; -.
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-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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-binding;
KW   rRNA-binding; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT   CHAIN           ?..204
FT                   /note="50S ribosomal protein L22, chloroplastic"
FT                   /id="PRO_0000030486"
SQ   SEQUENCE   204 AA;  22790 MW;  7127131157EA7744 CRC64;
     MALSLAINVP PVRDNLLRPQ PFQSQFRPNL LKFPIPSSAR IRCSSSSSFN DISLKTVTPD
     NKNSFVCRFN ATQLEVQETN QPYAETYAVG RHIRMSADKA RRVVDQIRGR PYEASLMVLE
     LMPYRACEAI IKIVFSAGAN ASHNLGLSKS SLFISKAEVN EGKTLKRVRA RAQGRANQIL
     KRTCHITITV RGLPDESDKE ENSS