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PSAD_SPIOL
ID   PSAD_SPIOL              Reviewed;         212 AA.
AC   P12353; Q43642; Q9S8Z2; Q9S8Z3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Photosystem I reaction center subunit II, chloroplastic;
DE   AltName: Full=Photosystem I 20 kDa subunit;
DE            Short=PSI-D;
DE   Flags: Precursor;
GN   Name=psaD;
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.
RC   TISSUE=Seedling;
RX   PubMed=3066511; DOI=10.1007/bf00521277;
RA   Muench S., Ljungberg U., Steppuhn J., Schneiderbauer A., Nechushtai R.,
RA   Beyreuther K., Herrmann R.G.;
RT   "Nucleotide sequences of cDNAs encoding the entire precursor polypeptides
RT   for subunits II and III of the photosystem I reaction center from
RT   spinach.";
RL   Curr. Genet. 14:511-518(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RX   PubMed=3288500; DOI=10.1016/0014-5793(88)80752-x;
RA   Lagoutte B.;
RT   "Cloning and sequencing of spinach cDNA clones encoding the 20 kDa PS I
RT   polypeptide.";
RL   FEBS Lett. 232:275-280(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=cv. Monatol; TISSUE=Seedling;
RX   PubMed=7920722; DOI=10.1046/j.1365-313x.1994.06030359.x;
RA   Flieger K., Wicke A., Herrmann R.G., Oelmueller R.;
RT   "Promoter and leader sequences of the spinach PsaD and PsaF genes direct an
RT   opposite light response in tobacco cotyledons: PsaD sequences downstream of
RT   the ATG codon are required for a positive light response.";
RL   Plant J. 6:359-368(1994).
RN   [4]
RP   SEQUENCE REVISION.
RA   Oelmueller R.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 51-63.
RX   PubMed=3049567; DOI=10.1093/oxfordjournals.jbchem.a122394;
RA   Oh-oka H., Takahashi Y., Kuriyama K., Saeki K., Matsubara H.;
RT   "The protein responsible for center A/B in spinach photosystem I: isolation
RT   with iron-sulfur cluster(s) and complete sequence analysis.";
RL   J. Biochem. 103:962-968(1988).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX   PubMed=1374333; DOI=10.1111/j.1432-1033.1992.tb16888.x;
RA   Lagoutte B., Vallon O.;
RT   "Purification and membrane topology of PSI-D and PSI-E, two subunits of the
RT   photosystem I reaction center.";
RL   Eur. J. Biochem. 205:1175-1185(1992).
CC   -!- FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin-
CC       oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode
CC       the ferredoxin-docking protein.
CC   -!- INTERACTION:
CC       P12353; P00221: PETF; NbExp=2; IntAct=EBI-864919, EBI-864933;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:1374333}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:1374333}; Stromal side
CC       {ECO:0000269|PubMed:1374333}.
CC   -!- INDUCTION: By light. {ECO:0000269|PubMed:7920722}.
CC   -!- SIMILARITY: Belongs to the PsaD family. {ECO:0000305}.
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DR   EMBL; X14017; CAA32182.1; -; mRNA.
DR   EMBL; Y00759; CAA68728.1; -; mRNA.
DR   EMBL; X77674; CAA54744.1; -; Genomic_DNA.
DR   PIR; S03016; A1SP2.
DR   PDB; 2O01; X-ray; 3.40 A; D=75-212.
DR   PDB; 2WSC; X-ray; 3.30 A; D=1-212.
DR   PDB; 2WSE; X-ray; 3.49 A; D=1-212.
DR   PDB; 2WSF; X-ray; 3.48 A; D=1-212.
DR   PDBsum; 2O01; -.
DR   PDBsum; 2WSC; -.
DR   PDBsum; 2WSE; -.
DR   PDBsum; 2WSF; -.
DR   AlphaFoldDB; P12353; -.
DR   SMR; P12353; -.
DR   IntAct; P12353; 1.
DR   PRIDE; P12353; -.
DR   OrthoDB; 1477247at2759; -.
DR   EvolutionaryTrace; P12353; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009538; C:photosystem I reaction center; IEA:InterPro.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   InterPro; IPR003685; PsaD.
DR   InterPro; IPR036579; PsaD_sf.
DR   PANTHER; PTHR31982; PTHR31982; 1.
DR   Pfam; PF02531; PsaD; 1.
DR   SUPFAM; SSF64234; SSF64234; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Membrane;
KW   Photosynthesis; Photosystem I; Plastid; Thylakoid; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:3049567"
FT   CHAIN           51..212
FT                   /note="Photosystem I reaction center subunit II,
FT                   chloroplastic"
FT                   /id="PRO_0000029377"
FT   REGION          53..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..153
FT                   /note="Ferredoxin and ferredoxin-oxidoreductase binding"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4..6
FT                   /note="ATQ -> GTP (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        12
FT                   /note="P -> R (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        22
FT                   /note="D -> E (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35..36
FT                   /note="VT -> LS (in Ref. 1; CAA32182)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45..47
FT                   /note="HHS -> LHT (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="A -> R (in Ref. 2; CAA68728)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60..61
FT                   /note="AA -> TP (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68..70
FT                   /note="PKG -> TKA (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="Missing (in Ref. 3; CAA54744)"
FT                   /evidence="ECO:0000305"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:2O01"
FT   TURN            116..119
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            136..139
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            141..147
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:2O01"
FT   STRAND          155..157
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            168..170
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   TURN            194..197
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:2O01"
SQ   SEQUENCE   212 AA;  23103 MW;  BC5FF64D97A6570E CRC64;
     MAMATQATLF SPSSLSSAKP IDTRLTTSFK QPSAVTFASK PASRHHSIRA AAAAEGKAAA
     ATETKEAPKG FTPPELDPNT PSPIFAGSTG GLLRKAQVEE FYVITWESPK EQIFEMPTGG
     AAIMREGPNL LKLARKEQCL ALGTRLRSKY KIKYQFYRVF PSGEVQYLHP KDGVYPEKVN
     PGRQGVGLNM RSIGKNVSPI EVKFTGKQPY DL
 
 
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