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RK13_SPIOL
ID   RK13_SPIOL              Reviewed;         250 AA.
AC   P12629; A0A0K9RAG3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=50S ribosomal protein L13, chloroplastic {ECO:0000303|PubMed:10874046};
DE   AltName: Full=CL13;
DE   AltName: Full=Chloroplastic large ribosomal subunit protein uL13c {ECO:0000303|PubMed:28007896};
DE   Flags: Precursor;
GN   Name=RPL13; ORFNames=SOVF_093170;
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 [MRNA].
RX   PubMed=2644249; DOI=10.1016/s0021-9258(18)94129-3;
RA   Phua S.H., Srinivasa B.R., Subramanian A.R.;
RT   "Chloroplast ribosomal protein L13 is encoded in the nucleus and is
RT   considerably larger than its bacterial homologue. Construction,
RT   immunoisolation, and nucleotide sequence (including transit peptide) its
RT   cDNA clone from an angiosperm.";
RL   J. Biol. Chem. 264:1968-1971(1989).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 48-53, 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   [4]
RP   FUNCTION.
RX   PubMed=1879566; DOI=10.1016/0014-5793(91)81005-s;
RA   Giese K., Subramanian A.R.;
RT   "Expression and functional assembly into bacterial ribosomes of a nuclear-
RT   encoded chloroplast ribosomal protein with a long NH2-terminal extension.";
RL   FEBS Lett. 288:72-76(1991).
RN   [5]
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   [6]
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   [7]
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=23365.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10874046};
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC       {ECO:0000305}.
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DR   EMBL; J04461; AAA34040.1; -; mRNA.
DR   EMBL; KQ146763; KNA15999.1; -; Genomic_DNA.
DR   PIR; A32033; A32033.
DR   PDB; 4V61; EM; 9.40 A; BL=1-250.
DR   PDB; 5H1S; EM; 3.50 A; L=60-250.
DR   PDB; 5MLC; EM; 3.90 A; L=1-250.
DR   PDB; 5MMI; EM; 3.25 A; K=1-250.
DR   PDB; 5MMM; EM; 3.40 A; K=1-250.
DR   PDB; 5X8P; EM; 3.40 A; K=54-250.
DR   PDB; 5X8T; EM; 3.30 A; K=54-250.
DR   PDB; 6ERI; EM; 3.00 A; AJ=49-248.
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; P12629; -.
DR   SMR; P12629; -.
DR   IntAct; P12629; 1.
DR   STRING; 3562.P12629; -.
DR   OrthoDB; 1119705at2759; -.
DR   EvolutionaryTrace; P12629; -.
DR   Proteomes; UP000054095; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0005840; C:ribosome; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00392; Ribosomal_L13; 1.
DR   Gene3D; 3.90.1180.10; -; 1.
DR   HAMAP; MF_01366; Ribosomal_L13; 1.
DR   InterPro; IPR005822; Ribosomal_L13.
DR   InterPro; IPR005823; Ribosomal_L13_bac-type.
DR   InterPro; IPR023563; Ribosomal_L13_CS.
DR   InterPro; IPR036899; Ribosomal_L13_sf.
DR   PANTHER; PTHR11545; PTHR11545; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   SUPFAM; SSF52161; SSF52161; 1.
DR   TIGRFAMs; TIGR01066; rplM_bact; 1.
DR   PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Plastid;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..47
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:10874046"
FT   CHAIN           48..250
FT                   /note="50S ribosomal protein L13, chloroplastic"
FT                   /id="PRO_0000030461"
FT   HELIX           53..72
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           104..107
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           124..136
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          152..156
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:5X8T"
FT   HELIX           167..170
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           188..194
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           197..205
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          221..223
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   STRAND          225..227
FT                   /evidence="ECO:0007829|PDB:5MMI"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:5MMI"
SQ   SEQUENCE   250 AA;  28164 MW;  0B8F157B7A948EA7 CRC64;
     MATMACASSL TFPSAQTQKS FFGTNVKQTP VLSFPRPTVA AAVAVSARKS TSASTKCTEE
     WRQLKEAVKK EFAIPHVPLD QRWMFTLEEA TGPDIWNTTW YPKSADHVPT DKKWYVVDAT
     DLILGRMAST IAIHIRGKNL ASYTPSVDMG AFVIVVNADK VAVSGKKRTQ KLYRRHSGRP
     GGLKEETFDQ LQKRIPERII EHAVRGMLPK GRLGRYLFNH LKVYKGAEHP HQAQQPIDLP
     LRDKRIRVEK
 
 
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