ID   RK22_CUSEX              Reviewed;         135 AA.
AC   A8W3G0;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=50S ribosomal protein L22, plastid;
GN   Name=rpl22;
OS   Cuscuta exaltata (Tall dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=476139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA   McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT   "Complete plastid genome sequences suggest strong selection for retention
RT   of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL   BMC Plant Biol. 7:57-57(2007).
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.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABW83731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU189132; ABW83731.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001542567.1; NC_009963.1.
DR   AlphaFoldDB; A8W3G0; -.
DR   SMR; A8W3G0; -.
DR   GeneID; 5729609; -.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Plastid; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   CHAIN           1..135
FT                   /note="50S ribosomal protein L22, plastid"
FT                   /id="PRO_0000354567"
SQ   SEQUENCE   135 AA;  15298 MW;  0A78F94982E08785 CRC64;
     MINTKPPEIY ALGQHISMSA DKARRIIDRI RGRSYEETLL ILELMPYRAA YPIFKLVYSA
     ASNASYTLAS NEANLVIIKA EVNEGPAIKK LKPRARGRCY PIKRPTCHIT IVLKDISFYD
     SDSESVELNL LKKAR