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RK6_SPIOL
ID   RK6_SPIOL               Reviewed;         220 AA.
AC   P82193; A0A0K9R4N9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=50S ribosomal protein L6, chloroplastic {ECO:0000303|PubMed:10874046};
DE   AltName: Full=Chloroplastic large ribosomal subunit protein uL6c {ECO:0000303|PubMed:28007896};
DE   Flags: Precursor;
GN   Name=RPL6; ORFNames=SOVF_107200;
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 39-68, 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=20224.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874046};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC       {ECO:0000255}.
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DR   EMBL; KQ150353; KNA14466.1; -; Genomic_DNA.
DR   PDB; 4V61; EM; 9.40 A; I=39-68.
DR   PDB; 5H1S; EM; 3.50 A; I=39-220.
DR   PDB; 5MLC; EM; 3.90 A; H=1-220.
DR   PDB; 5MMI; EM; 3.25 A; G=1-220.
DR   PDB; 5MMM; EM; 3.40 A; G=1-220.
DR   PDB; 5X8P; EM; 3.40 A; G=39-220.
DR   PDB; 5X8T; EM; 3.30 A; G=39-220.
DR   PDB; 6ERI; EM; 3.00 A; AG=44-215.
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; P82193; -.
DR   SMR; P82193; -.
DR   IntAct; P82193; 1.
DR   STRING; 3562.P82193; -.
DR   OrthoDB; 1509998at2759; -.
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   Gene3D; 3.90.930.12; -; 2.
DR   HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR   InterPro; IPR000702; Ribosomal_L6.
DR   InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR   InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR   InterPro; IPR019906; Ribosomal_L6_bac-type.
DR   InterPro; IPR002358; Ribosomal_L6_CS.
DR   PANTHER; PTHR11655; PTHR11655; 1.
DR   Pfam; PF00347; Ribosomal_L6; 2.
DR   PRINTS; PR00059; RIBOSOMALL6.
DR   SUPFAM; SSF56053; SSF56053; 2.
DR   TIGRFAMs; TIGR03654; L6_bact; 1.
DR   PROSITE; PS00525; RIBOSOMAL_L6_1; 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..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874046"
FT   CHAIN           39..220
FT                   /note="50S ribosomal protein L6, chloroplastic"
FT                   /id="PRO_0000249859"
FT   CONFLICT        52
FT                   /note="Missing (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           42..45
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          86..96
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           99..120
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          123..131
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          135..139
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          142..151
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          153..156
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          170..176
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           178..190
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            196..198
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          201..206
FT                   /evidence="ECO:0007829|PDB:5MMI"
SQ   SEQUENCE   220 AA;  24474 MW;  2E0BB3403003424E CRC64;
     MSLPLPSHMK SVFLGMKVEI STSVPVTRIG FWRKSVDCKE SRIGKQPITV PANVAIAMEG
     QDLKVKGPLG ELSITYPREV LVEKQESGFL RVRKAVETRR ANQMHGLFRT LTDNMVVGVS
     KGFEKKLQLV GVGYRATVEG KDLILSLGFS HPVRMAIPDE LQVKVEENTK VTVSGRDKSV
     VGQFAATIRS WRPPEPYKGK GVRYVDEVVR RKEGKAGKKK
 
 
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