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P12353

- PSAD_SPIOL

UniProt

P12353 - PSAD_SPIOL

Protein

Photosystem I reaction center subunit II, chloroplastic

Gene

psaD

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    PsaD can form complexes with ferredoxin and ferredoxin-oxidoreductase in photosystem I (PS I) reaction center. PSAD may encode the ferredoxin-docking protein.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. photosynthesis Source: UniProtKB-KW

    Keywords - Biological processi

    Photosynthesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Photosystem I reaction center subunit II, chloroplastic
    Alternative name(s):
    Photosystem I 20 kDa subunit
    Short name:
    PSI-D
    Gene namesi
    Name:psaD
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    Plastidchloroplast thylakoid membrane 1 Publication; Peripheral membrane protein 1 Publication; Stromal side 1 Publication

    GO - Cellular componenti

    1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
    2. photosystem I reaction center Source: InterPro

    Keywords - Cellular componenti

    Chloroplast, Membrane, Photosystem I, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5050Chloroplast1 PublicationAdd
    BLAST
    Chaini51 – 212162Photosystem I reaction center subunit II, chloroplasticPRO_0000029377Add
    BLAST

    Expressioni

    Inductioni

    By light.1 Publication

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PETFP002212EBI-864919,EBI-864933

    Protein-protein interaction databases

    IntActiP12353. 1 interaction.

    Structurei

    Secondary structure

    1
    212
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi89 – 913
    Beta strandi97 – 993
    Beta strandi103 – 1053
    Beta strandi109 – 1113
    Turni116 – 1194
    Beta strandi130 – 1323
    Turni136 – 1394
    Turni141 – 1477
    Beta strandi148 – 1503
    Beta strandi155 – 1573
    Turni168 – 1703
    Beta strandi171 – 1733
    Beta strandi175 – 1773
    Beta strandi189 – 1913
    Turni194 – 1974
    Beta strandi206 – 2083

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O01X-ray3.40D75-212[»]
    2WSCX-ray3.30D1-212[»]
    2WSEX-ray3.49D1-212[»]
    2WSFX-ray3.48D1-212[»]
    ProteinModelPortaliP12353.
    SMRiP12353. Positions 75-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12353.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni145 – 1539Ferredoxin and ferredoxin-oxidoreductase bindingSequence Analysis

    Sequence similaritiesi

    Belongs to the PsaD family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.30.1470.10. 1 hit.
    InterProiIPR003685. PSI_PsaD.
    [Graphical view]
    PfamiPF02531. PsaD. 1 hit.
    [Graphical view]
    SUPFAMiSSF64234. SSF64234. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12353-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMATQATLF SPSSLSSAKP IDTRLTTSFK QPSAVTFASK PASRHHSIRA    50
    AAAAEGKAAA ATETKEAPKG FTPPELDPNT PSPIFAGSTG GLLRKAQVEE 100
    FYVITWESPK EQIFEMPTGG AAIMREGPNL LKLARKEQCL ALGTRLRSKY 150
    KIKYQFYRVF PSGEVQYLHP KDGVYPEKVN PGRQGVGLNM RSIGKNVSPI 200
    EVKFTGKQPY DL 212
    Length:212
    Mass (Da):23,103
    Last modified:September 26, 2001 - v2
    Checksum:iBC5FF64D97A6570E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 63ATQ → GTP in CAA54744. (PubMed:7920722)Curated
    Sequence conflicti12 – 121P → R in CAA54744. (PubMed:7920722)Curated
    Sequence conflicti22 – 221D → E in CAA54744. (PubMed:7920722)Curated
    Sequence conflicti35 – 362VT → LS in CAA32182. (PubMed:3066511)Curated
    Sequence conflicti45 – 473HHS → LHT in CAA54744. (PubMed:7920722)Curated
    Sequence conflicti58 – 581A → R in CAA68728. (PubMed:3288500)Curated
    Sequence conflicti60 – 612AA → TP(PubMed:3066511)Curated
    Sequence conflicti60 – 612AA → TP(PubMed:3049567)Curated
    Sequence conflicti68 – 703PKG → TKA in CAA54744. (PubMed:7920722)Curated
    Sequence conflicti91 – 911Missing in CAA54744. (PubMed:7920722)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14017 mRNA. Translation: CAA32182.1.
    Y00759 mRNA. Translation: CAA68728.1.
    X77674 Genomic DNA. Translation: CAA54744.1.
    PIRiS03016. A1SP2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14017 mRNA. Translation: CAA32182.1 .
    Y00759 mRNA. Translation: CAA68728.1 .
    X77674 Genomic DNA. Translation: CAA54744.1 .
    PIRi S03016. A1SP2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O01 X-ray 3.40 D 75-212 [» ]
    2WSC X-ray 3.30 D 1-212 [» ]
    2WSE X-ray 3.49 D 1-212 [» ]
    2WSF X-ray 3.48 D 1-212 [» ]
    ProteinModelPortali P12353.
    SMRi P12353. Positions 75-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P12353. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P12353.

    Family and domain databases

    Gene3Di 3.30.1470.10. 1 hit.
    InterProi IPR003685. PSI_PsaD.
    [Graphical view ]
    Pfami PF02531. PsaD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64234. SSF64234. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of cDNAs encoding the entire precursor polypeptides for subunits II and III of the photosystem I reaction center from spinach."
      Muench S., Ljungberg U., Steppuhn J., Schneiderbauer A., Nechushtai R., Beyreuther K., Herrmann R.G.
      Curr. Genet. 14:511-518(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
      Tissue: Seedling.
    2. "Cloning and sequencing of spinach cDNA clones encoding the 20 kDa PS I polypeptide."
      Lagoutte B.
      FEBS Lett. 232:275-280(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    3. "Promoter and leader sequences of the spinach PsaD and PsaF genes direct an opposite light response in tobacco cotyledons: PsaD sequences downstream of the ATG codon are required for a positive light response."
      Flieger K., Wicke A., Herrmann R.G., Oelmueller R.
      Plant J. 6:359-368(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: cv. Monatol.
      Tissue: Seedling.
    4. Oelmueller R.
      Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    5. "The protein responsible for center A/B in spinach photosystem I: isolation with iron-sulfur cluster(s) and complete sequence analysis."
      Oh-oka H., Takahashi Y., Kuriyama K., Saeki K., Matsubara H.
      J. Biochem. 103:962-968(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 51-63.
    6. "Purification and membrane topology of PSI-D and PSI-E, two subunits of the photosystem I reaction center."
      Lagoutte B., Vallon O.
      Eur. J. Biochem. 205:1175-1185(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPSAD_SPIOL
    AccessioniPrimary (citable) accession number: P12353
    Secondary accession number(s): Q43642, Q9S8Z2, Q9S8Z3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3