RK2_AMBTC
ID RK2_AMBTC Reviewed; 273 AA.
AC P60406;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=50S ribosomal protein L2, chloroplastic;
GN Name=rpl2-A;
GN and
GN Name=rpl2-B;
OS Amborella trichopoda.
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SUGGESTION OF RNA
RP EDITING.
RX PubMed=12832641; DOI=10.1093/molbev/msg159;
RA Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT that Amborella is not a basal angiosperm.";
RL Mol. Biol. Evol. 20:1499-1505(2003).
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000305|PubMed:12832641};
CC Note=The initiator methionine is created by RNA editing.
CC {ECO:0000305|PubMed:12832641};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; AJ506156; CAD47814.1; -; Genomic_DNA.
DR EMBL; AJ506156; CAD47816.1; -; Genomic_DNA.
DR RefSeq; NP_904140.1; NC_005086.1.
DR RefSeq; NP_904163.1; NC_005086.1.
DR AlphaFoldDB; P60406; -.
DR SMR; P60406; -.
DR STRING; 13333.ERN11804; -.
DR GeneID; 2546582; -.
DR GeneID; 2546594; -.
DR KEGG; atr:2546582; -.
DR KEGG; atr:2546594; -.
DR eggNOG; KOG0438; Eukaryota.
DR OrthoDB; 1156335at2759; -.
DR Proteomes; UP000017836; Chloroplast.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
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; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA editing.
FT CHAIN 1..273
FT /note="50S ribosomal protein L2, chloroplastic"
FT /id="PRO_0000129662"
FT REGION 1..23
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 254..273
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 29704 MW; 94860473A5476496 CRC64;
MAIHLYKTST PSTRNGAVDS QVKSNPRKNL IYGQHRCGKG RNARGIITAG HRGGGHKRLY
RKIDFRRNEK DISGRIVTIE YDPNRNAYIC LIHYGDGEKR YILHPRGAII GDTIVSGTEV
PISMGNALPL TDMPLGTAIH NIEITLGKGG QLARAAGAVA KLIAKEGKSA TLRLPSGEVR
LISKNCSATV GQVGNVGVNQ KILGRAGSKC WLGKRPVVRG VVMNPVDHPH GGGEGRAPIG
RKKPTTPWGY PALGRRSRKK KKYSDSFILR RRK