RK2_SACHY
ID RK2_SACHY Reviewed; 273 AA.
AC Q6L3B9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=50S ribosomal protein L2, chloroplastic;
GN Name=rpl2-A; OrderedLocusNames=PS009.1;
GN and
GN Name=rpl2-B; OrderedLocusNames=PS077;
OS Saccharum hybrid (Sugarcane).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum;
OC unclassified Saccharum.
OX NCBI_TaxID=15819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC STRAIN=cv. SP-80-3280;
RX PubMed=15526204; DOI=10.1007/s00294-004-0542-4;
RA Calsa T. Jr., Carraro D.M., Benatti M.R., Barbosa A.C., Kitajima J.P.,
RA Carrer H.;
RT "Structural features and transcript-editing analysis of sugarcane
RT (Saccharum officinarum L.) chloroplast genome.";
RL Curr. Genet. 46:366-373(2004).
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:15526204};
CC Note=The initiator methionine is created by RNA editing.;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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DR EMBL; AE009947; AAT44673.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6L3B9; -.
DR SMR; Q6L3B9; -.
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_0000129701"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..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; 30051 MW; 58626A6A98CBA68B CRC64;
MAKHLYKTPI PSTRKGTVDR QVKSNPRNKL IHGRHRCGKG RNARGIITAR HRGGGHKRLY
RKIDFRRNQK DISGRIVTIE YDPNRNAYIC LIHYGDGEKR YILHPRGAII GDTIVSGTKV
PISMGNALPL TDMPLGTAIH NIEITRGRGG QLARAAGAVA KLIAKEGKLA TLRLPSGEVR
LVSQNCLATV GQVGNVGVNQ KSLGRAGSKC WLGKRPVVRG VVMNPVDHPH GGGEGKAPIG
RKKPTTPWGY PALGRRTRKR KKYSDSFILR RRK
