Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Plastocyanin A, chloroplastic

Gene

PETE

Organism
Populus nigra (Lombardy poplar)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi106 – 1061Copper
Metal bindingi153 – 1531Copper
Metal bindingi156 – 1561Copper
Metal bindingi161 – 1611Copper

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. electron carrier activity Source: InterPro

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Plastocyanin A, chloroplastic
Gene namesi
Name:PETE
OrganismiPopulus nigra (Lombardy poplar)
Taxonomic identifieri3691 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Subcellular locationi

Plastidchloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side
Note: Loosely bound to the inner thylakoid membrane surface in chloroplasts.

GO - Cellular componenti

  1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6969Chloroplast1 PublicationAdd
BLAST
Chaini70 – 16899Plastocyanin A, chloroplasticPRO_0000002893Add
BLAST

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi71 – 755Combined sources
Beta strandi83 – 908Combined sources
Beta strandi95 – 1006Combined sources
Helixi112 – 1143Combined sources
Helixi121 – 1233Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi147 – 1526Combined sources
Helixi154 – 1563Combined sources
Turni157 – 1604Combined sources
Beta strandi162 – 1676Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXGX-ray1.60A/B70-168[»]
1PLCX-ray1.33A70-168[»]
1PNCX-ray1.60A70-168[»]
1PNDX-ray1.60A70-168[»]
1TKWNMR-A70-168[»]
2PCYX-ray1.80A70-168[»]
3PCYX-ray1.90A70-168[»]
4DP7X-ray1.08X70-168[»]
4DP8X-ray1.07X70-168[»]
4DP9X-ray1.00X70-168[»]
4DPAX-ray1.05X70-168[»]
4DPBX-ray1.00X70-168[»]
4DPCX-ray1.06X70-168[»]
4PCYX-ray2.15A70-168[»]
5PCYX-ray1.80A70-168[»]
6PCYX-ray1.90A70-168[»]
ProteinModelPortaliP00299.
SMRiP00299. Positions 70-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00299.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 16899Plastocyanin-likeAdd
BLAST

Sequence similaritiesi

Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02656. cyanin_plasto. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVTSAAVS IPSFTGLKAG SASNAKVSAS AKVSASPLPR LSIKASMKDV
60 70 80 90 100
GAAVVATAAS AMIASNAMAI DVLLGADDGS LAFVPSEFSI SPGEKIVFKN
110 120 130 140 150
NAGFPHNIVF DEDSIPSGVD ASKISMSEED LLNAKGETFE VALSNKGEYS
160
FYCSPHQGAG MVGKVTVN
Length:168
Mass (Da):17,020
Last modified:September 30, 1996 - v2
Checksum:i901B21A7573DBF82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50185 mRNA. Translation: CAA90564.1.
PIRiS58209. CUPX.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z50185 mRNA. Translation: CAA90564.1.
PIRiS58209. CUPX.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JXGX-ray1.60A/B70-168[»]
1PLCX-ray1.33A70-168[»]
1PNCX-ray1.60A70-168[»]
1PNDX-ray1.60A70-168[»]
1TKWNMR-A70-168[»]
2PCYX-ray1.80A70-168[»]
3PCYX-ray1.90A70-168[»]
4DP7X-ray1.08X70-168[»]
4DP8X-ray1.07X70-168[»]
4DP9X-ray1.00X70-168[»]
4DPAX-ray1.05X70-168[»]
4DPBX-ray1.00X70-168[»]
4DPCX-ray1.06X70-168[»]
4PCYX-ray2.15A70-168[»]
5PCYX-ray1.80A70-168[»]
6PCYX-ray1.90A70-168[»]
ProteinModelPortaliP00299.
SMRiP00299. Positions 70-168.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00299.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR001235. Copper_blue_Plastocyanin.
IPR008972. Cupredoxin.
IPR002387. Plastocyanin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
PRINTSiPR00156. COPPERBLUE.
PR00157. PLASTOCYANIN.
SUPFAMiSSF49503. SSF49503. 1 hit.
TIGRFAMsiTIGR02656. cyanin_plasto. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Reichert J., Jenzelewski V., Haehnel W.
    Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Italica.
    Tissue: Leaf.
  2. "Elegance in molecular design: the copper site of photosynthetic electron-transfer protein."
    Freeman H.C.
    J. Proc. Royal Soc. N.S. Wales 112:45-62(1978)
    Cited for: PROTEIN SEQUENCE OF 70-168.
    Strain: cv. Italica.
  3. "The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide."
    Garrett T.P.J., Clingeleffer D.J., Guss J.M., Rogers S.J., Freeman H.C.
    J. Biol. Chem. 259:2822-2825(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  4. "Structure of oxidized poplar plastocyanin at 1.6-A resolution."
    Guss J.M., Freeman H.C.
    J. Mol. Biol. 169:521-563(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  5. "X-ray crystal structure analysis of plastocyanin at 2.7-A resolution."
    Colman P.M., Freeman H.C., Guss J.M., Murata M., Norris V.A., Ramshaw J.A.M., Venkatappa M.P.
    Nature 272:319-324(1977)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiPLAS1_POPNI
AccessioniPrimary (citable) accession number: P00299
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: September 30, 1996
Last modified: January 6, 2015
This is version 107 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

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.