ID B0I2L1_9MAGN Unreviewed; 171 AA.
AC B0I2L1;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 08-NOV-2023, entry version 44.
DE RecName: Full=50S ribosomal protein L22, chloroplastic {ECO:0000256|RuleBase:RU004009};
DE Flags: Fragment;
GN Name=rpl22 {ECO:0000313|EMBL:BAG06523.1};
OS Litsea hypophaea.
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAG06523.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Litsea.
OX NCBI_TaxID=453235 {ECO:0000313|EMBL:BAG06523.1};
RN [1] {ECO:0000313|EMBL:BAG06523.1}
RP NUCLEOTIDE SEQUENCE.
RA Chaw S.-M., Cheng C.-L., Wu C.-L., Wang R.-J., Su T.-M.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAG06523.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18237435; DOI=10.1186/1471-2148-8-36;
RA Wang R.-J., Cheng C.-L., Chang C.-C., Wu C.-L., Su T.-M., Chaw S.-M.;
RT "Dynamics and evolution of the inverted repeat-large single copy junctions
RT in the chloroplast genomes of monocots.";
RL BMC Evol. Biol. 8:36-36(2008).
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:0000256|RuleBase:RU004009}.
CC -!- FUNCTION: This protein binds specifically to 23S rRNA.
CC {ECO:0000256|RuleBase:RU004009}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU004009}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|RuleBase:RU004005}.
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DR EMBL; AB331343; BAG06523.1; -; Genomic_DNA.
DR AlphaFoldDB; B0I2L1; -.
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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR018260; Ribosomal_uL22_CS.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01044; rplV_bact; 1.
DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:BAG06523.1};
KW Plastid {ECO:0000313|EMBL:BAG06523.1};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU004005};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU004005};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730}.
FT NON_TER 171
FT /evidence="ECO:0000313|EMBL:BAG06523.1"
SQ SEQUENCE 171 AA; 20192 MW; AA9B085114E6521B CRC64;
MSKWRKWKKT LKKQKMKRSS STQVQALAQR ICMSAHKARR VIDQIRGHSY EKTLMLLELM
PYRAFYPIFK LVYSAAANAS HNKSFNEADS VISKAEVNGG TIVKKLKPRA RGRSYPIERP
ACHIIIVLKD SSKKKTDQDI FLETKNVWRD PIIERYIEKE REREKKRWVK K
//
