RK3_SPIOL
ID RK3_SPIOL Reviewed; 305 AA.
AC P82191; A0A0K9QEC7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=50S ribosomal protein L3, chloroplastic {ECO:0000303|PubMed:10874046};
DE AltName: Full=Chloroplastic large ribosomal subunit protein uL3c {ECO:0000303|PubMed:28007896};
DE Flags: Precursor;
GN Name=RPL3; ORFNames=SOVF_195350;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [2]
RP PROTEIN SEQUENCE OF 85-129, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
RP SPECTROMETRY.
RC STRAIN=cv. Alwaro; TISSUE=Leaf;
RX PubMed=10874046; DOI=10.1074/jbc.m005012200;
RA Yamaguchi K., Subramanian A.R.;
RT "The plastid ribosomal proteins. Identification of all the proteins in the
RT 50S subunit of an organelle ribosome (chloroplast).";
RL J. Biol. Chem. 275:28466-28482(2000).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.4 ANGSTROMS).
RX PubMed=18042701; DOI=10.1073/pnas.0709856104;
RA Sharma M.R., Wilson D.N., Datta P.P., Barat C., Schluenzen F., Fucini P.,
RA Agrawal R.K.;
RT "Cryo-EM study of the spinach chloroplast ribosome reveals the structural
RT and functional roles of plastid-specific ribosomal proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19315-19320(2007).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=27762343; DOI=10.1038/srep35793;
RA Ahmed T., Yin Z., Bhushan S.;
RT "Cryo-EM structure of the large subunit of the spinach chloroplast
RT ribosome.";
RL Sci. Rep. 6:35793-35793(2016).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28007896; DOI=10.15252/embj.201695959;
RA Bieri P., Leibundgut M., Saurer M., Boehringer D., Ban N.;
RT "The complete structure of the chloroplast 70S ribosome in complex with
RT translation factor pY.";
RL EMBO J. 36:475-486(2017).
CC -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus. {ECO:0000305|PubMed:10874046,
CC ECO:0000305|PubMed:28007896}.
CC -!- SUBUNIT: Component of the chloroplast large ribosomal subunit (LSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins. {ECO:0000269|PubMed:10874046,
CC ECO:0000269|PubMed:28007896}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:10874046, ECO:0000269|PubMed:28007896}.
CC -!- MASS SPECTROMETRY: Mass=24129.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10874046};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255}.
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DR EMBL; KQ197093; KNA04906.1; -; Genomic_DNA.
DR PDB; 4V61; EM; 9.40 A; F=88-129.
DR PDB; 5H1S; EM; 3.50 A; F=85-305.
DR PDB; 5MLC; EM; 3.90 A; E=1-305.
DR PDB; 5MMI; EM; 3.25 A; D=1-305.
DR PDB; 5MMM; EM; 3.40 A; D=1-305.
DR PDB; 5X8P; EM; 3.40 A; D=85-305.
DR PDB; 5X8T; EM; 3.30 A; D=85-305.
DR PDB; 6ERI; EM; 3.00 A; AD=85-305.
DR PDBsum; 4V61; -.
DR PDBsum; 5H1S; -.
DR PDBsum; 5MLC; -.
DR PDBsum; 5MMI; -.
DR PDBsum; 5MMM; -.
DR PDBsum; 5X8P; -.
DR PDBsum; 5X8T; -.
DR PDBsum; 6ERI; -.
DR AlphaFoldDB; P82191; -.
DR SMR; P82191; -.
DR IntAct; P82191; 1.
DR STRING; 3562.P82191; -.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding; Transit peptide.
FT TRANSIT 1..84
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:10874046"
FT CHAIN 85..305
FT /note="50S ribosomal protein L3, chloroplastic"
FT /id="PRO_0000249411"
FT REGION 228..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:5H1S"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5MMI"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 257..270
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:5MMI"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5X8T"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5MMI"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:5MMI"
SQ SEQUENCE 305 AA; 32980 MW; 6A4D1456370031F6 CRC64;
MAAILPTFSI KSSSCTYSSS KRSLSSPKAV SLSSSVNGTP KVQSLRLSTS FVCSPNQIIK
LKSVSPSRST QLRRAVGGLE IKMMSVDAGI GVMGTKLGMM SFFEEDGTVV PVTVIGFKEG
NIVTQVKTES TDGYNAVQVG YERLRDRKLT MPERGHLNKA GVIPMRHLQE FRLVSVDDFT
PSQKLLFEEL FKEGDMVDIS GTTIGKGFQG GIKRHNFKRG LMTHGSKSHR ALGSIGAGTT
PGHVYKGKKM PGRMGGTKTK IRKLKIMKID TDLRVVMIKG AVPGKPGNLL RLAPAKIVGK
NIPKN
