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Protein

Photosystem I reaction center subunit III, chloroplastic

Gene

PSAF

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Probably participates in efficiency of electron transfer from plastocyanin to P700 (or cytochrome c553 in algae and cyanobacteria). This plastocyanin-docking protein contributes to the specific association of plastocyanin to PSI.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem I reaction center subunit III, chloroplastic
Alternative name(s):
Light-harvesting complex I 17 kDa protein
PSI-F
Gene namesi
Name:PSAF
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Photosystem I, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7777Chloroplast1 PublicationAdd
BLAST
Chaini78 – 231154Photosystem I reaction center subunit III, chloroplasticPRO_0000029346Add
BLAST

Proteomic databases

PRIDEiP12355.

Interactioni

Protein-protein interaction databases

IntActiP12355. 1 interaction.
MINTiMINT-8174017.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi85 – 873Combined sources
Helixi89 – 968Combined sources
Helixi99 – 1013Combined sources
Helixi105 – 1073Combined sources
Turni119 – 1224Combined sources
Helixi124 – 1274Combined sources
Helixi130 – 1334Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi151 – 1555Combined sources
Turni158 – 1603Combined sources
Helixi162 – 1709Combined sources
Turni171 – 18414Combined sources
Beta strandi187 – 1893Combined sources
Turni194 – 1963Combined sources
Helixi201 – 2033Combined sources
Helixi207 – 2104Combined sources
Helixi217 – 2204Combined sources
Beta strandi223 – 2264Combined sources
Helixi228 – 2303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O01X-ray3.40F78-231[»]
2WSCX-ray3.30F1-231[»]
2WSEX-ray3.49F1-231[»]
2WSFX-ray3.48F1-231[»]
3LW5X-ray3.30F78-231[»]
ProteinModelPortaliP12355.
SMRiP12355. Positions 78-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12355.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsaF family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.8.110. 1 hit.
InterProiIPR003666. PSI_PsaF.
[Graphical view]
PfamiPF02507. PSI_PsaF. 1 hit.
[Graphical view]
SUPFAMiSSF81536. SSF81536. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P12355-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFTIPTNLY KPLATKPKHL SSSSFAPRSK IVCQQENDQQ QPKKLELAKV
60 70 80 90 100
GANAAAALAL SSVLLSSWSV APDAAMADIA GLTPCKESKQ FAKREKQALK
110 120 130 140 150
KLQASLKLYA DDSAPALAIK ATMEKTKKRF DNYGKYGLLC GSDGLPHLIV
160 170 180 190 200
SGDQRHWGEF ITPGILFLYI AGWIGWVGRS YLIAIRDEKK PTQKEIIIDV
210 220 230
PLASSLLFRG FSWPVAAYRE LLNGELVDNN F
Length:231
Mass (Da):25,412
Last modified:October 1, 1989 - v1
Checksum:i270E1BAC159D79B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13133 mRNA. Translation: CAA31523.1.
PIRiS00451. F1SP3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13133 mRNA. Translation: CAA31523.1.
PIRiS00451. F1SP3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O01X-ray3.40F78-231[»]
2WSCX-ray3.30F1-231[»]
2WSEX-ray3.49F1-231[»]
2WSFX-ray3.48F1-231[»]
3LW5X-ray3.30F78-231[»]
ProteinModelPortaliP12355.
SMRiP12355. Positions 78-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12355. 1 interaction.
MINTiMINT-8174017.

Proteomic databases

PRIDEiP12355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP12355.

Family and domain databases

Gene3Di1.10.8.110. 1 hit.
InterProiIPR003666. PSI_PsaF.
[Graphical view]
PfamiPF02507. PSI_PsaF. 1 hit.
[Graphical view]
SUPFAMiSSF81536. SSF81536. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of cDNA clones encoding the entire precursor polypeptides for subunits IV and V of the photosystem I reaction center from spinach."
    Steppuhn J., Hermans J., Nechushtai R., Ljungberg U., Thuemmler F., Lottspeich F., Herrmann R.G.
    FEBS Lett. 237:218-224(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Identification of the plastocyanin binding subunit of photosystem I."
    Hippler M., Ratajczak R., Haehnel W.
    FEBS Lett. 250:280-284(1989)
    Cited for: PROTEIN SEQUENCE OF 78-91.

Entry informationi

Entry nameiPSAF_SPIOL
AccessioniPrimary (citable) accession number: P12355
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 7, 2015
This is version 77 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.