ID   RK2_LEMMI               Reviewed;         273 AA.
AC   A9L9D7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=50S ribosomal protein L2, chloroplastic;
GN   Name=rpl2;
OS   Lemna minor (Common duckweed).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Lemnoideae; Lemna.
OX   NCBI_TaxID=4472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUGGESTION OF RNA
RP   EDITING.
RX   PubMed=18463914; DOI=10.1007/s00239-008-9091-7;
RA   Mardanov A.V., Ravin N.V., Kuznetsov B.B., Samigullin T.H., Antonov A.S.,
RA   Kolganova T.V., Skyabin K.G.;
RT   "Complete sequence of the Duckweed (Lemna minor) chloroplast genome:
RT   structural organization and phylogenetic relationships to other
RT   angiosperms.";
RL   J. Mol. Evol. 66:555-564(2008).
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- RNA EDITING: Modified_positions=1 {ECO:0000305|PubMed:18463914};
CC       Note=The initiator methionine is created by RNA editing.
CC       {ECO:0000305|PubMed:18463914};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ400350; ABD48536.1; -; Genomic_DNA.
DR   RefSeq; YP_001595549.1; NC_010109.1.
DR   AlphaFoldDB; A9L9D7; -.
DR   SMR; A9L9D7; -.
DR   GeneID; 5787593; -.
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:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 4.10.950.10; -; 1.
DR   HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR002171; Ribosomal_L2.
DR   InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR   InterPro; IPR022669; Ribosomal_L2_C.
DR   InterPro; IPR022671; Ribosomal_L2_CS.
DR   InterPro; IPR014726; Ribosomal_L2_dom3.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR13691; PTHR13691; 1.
DR   Pfam; PF00181; Ribosomal_L2; 1.
DR   Pfam; PF03947; Ribosomal_L2_C; 1.
DR   PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR   SMART; SM01383; Ribosomal_L2; 1.
DR   SMART; SM01382; Ribosomal_L2_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR01171; rplB_bact; 1.
DR   PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Plastid; Ribonucleoprotein; Ribosomal protein; RNA editing.
FT   CHAIN           1..273
FT                   /note="50S ribosomal protein L2, chloroplastic"
FT                   /id="PRO_0000342541"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..273
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  29963 MW;  C402A7E96382CF0C CRC64;
     MAIHLYKTST PSTRNGAVDR KVKSNPRNNL IYGQHRCGKG RNARGIITAG HRGGGHKRLY
     RKIDFRRNEK DIYGRIVTIE YDPNRNAYIC LIHYGDGEKR YILHPRGAII GDTIVSGTEV
     PISMGNALPL TDMPLGTAIH NIEITLGKGG QLARAAGAVA KLIAKEGKSA TLRLPSGEVR
     LISKNCLATV GQVGNVGVNQ KSLGRAGSKC WLGKRPVVRG VVMNPVDHPH GGGEGRAPIG
     RKRPMTPWGY PALGKRSRKK KRYSDRFILR RRK