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Protein

Photosystem I reaction center subunit XI, chloroplastic

Gene

PSAL

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Biological processi

  1. photosynthesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Photosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem I reaction center subunit XI, chloroplastic
Short name:
PSI-L
Alternative name(s):
PSI subunit V
Gene namesi
Name:PSAL
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini48 – 13487StromalSequence AnalysisAdd
BLAST
Transmembranei135 – 15521HelicalSequence AnalysisAdd
BLAST
Topological domaini156 – 18833LumenalSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Topological domaini210 – 2167StromalSequence Analysis

GO - Cellular componenti

  1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. photosystem I reaction center Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem I, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4747ChloroplastSequence AnalysisAdd
BLAST
Chaini48 – 216169Photosystem I reaction center subunit XI, chloroplasticPRO_0000029427Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi55 – 584Combined sources
Beta strandi61 – 644Combined sources
Beta strandi66 – 683Combined sources
Turni74 – 763Combined sources
Turni79 – 857Combined sources
Beta strandi87 – 926Combined sources
Helixi97 – 10711Combined sources
Beta strandi110 – 1134Combined sources
Helixi114 – 1185Combined sources
Beta strandi127 – 1293Combined sources
Turni134 – 1385Combined sources
Helixi139 – 1435Combined sources
Turni144 – 1529Combined sources
Turni171 – 1733Combined sources
Helixi181 – 19515Combined sources
Turni197 – 1993Combined sources
Helixi200 – 2045Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O01X-ray3.40L53-216[»]
2WSCX-ray3.30L1-216[»]
2WSEX-ray3.49L1-216[»]
2WSFX-ray3.48L1-216[»]
ProteinModelPortaliQ41385.
SMRiQ41385. Positions 53-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ41385.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsaL family.Curated

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.1240.10. 1 hit.
InterProiIPR003757. PSI_PsaL.
[Graphical view]
PfamiPF02605. PsaL. 1 hit.
[Graphical view]
ProDomiPD005947. PSI_PsaL. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81568. SSF81568. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q41385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATTSPMAS QLKSGFTTKA LVVPKGISGP ALRGFPSPRR HTSFTVRAIK
60 70 80 90 100
TEKPTYQVIQ PLNGDPFIGG LETPVTSSPL IAWYLSNLPA YRTAVNPLLR
110 120 130 140 150
GVEVGLAHGF LLVGPFVKAG PLRNTEYAGA AGSLAAAGLV VILSMCLTMY
160 170 180 190 200
GIASFKEGEP SIAPALTLTG RKKQPDQLQS ADGWAKFTGG FFFGGVSGVT
210
WACFLMYVLD LPYYFK
Length:216
Mass (Da):22,937
Last modified:November 1, 1996 - v1
Checksum:i603DCA983C7C383B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64445 mRNA. Translation: CAA45775.1.
PIRiS35151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64445 mRNA. Translation: CAA45775.1.
PIRiS35151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O01X-ray3.40L53-216[»]
2WSCX-ray3.30L1-216[»]
2WSEX-ray3.49L1-216[»]
2WSFX-ray3.48L1-216[»]
ProteinModelPortaliQ41385.
SMRiQ41385. Positions 53-216.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ41385.

Family and domain databases

Gene3Di1.20.1240.10. 1 hit.
InterProiIPR003757. PSI_PsaL.
[Graphical view]
PfamiPF02605. PsaL. 1 hit.
[Graphical view]
ProDomiPD005947. PSI_PsaL. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81568. SSF81568. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and characterization of cDNA clones encoding a 18.8 kDa polypeptide, the product of the gene psaL, associated with photosystem I reaction center from spinach."
    Flieger K., Oelmueller R., Herrmann R.G.
    Plant Mol. Biol. 22:703-709(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Monatol.
  2. "Two new components of 9 and 14 kDa from spinach photosystem I complex."
    Ikeuchi M., Inoue Y.
    FEBS Lett. 280:332-334(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 158-178.

Entry informationi

Entry nameiPSAL_SPIOL
AccessioniPrimary (citable) accession number: Q41385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 68 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.