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P11392

- PHEA_PORPP

UniProt

P11392 - PHEA_PORPP

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Protein

B-phycoerythrin alpha chain

Gene

cpeA

Organism
Porphyridium purpureum (Red alga) (Porphyridium cruentum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821Phycoerythrobilin chromophore 1 (covalent; via 1 link)
Binding sitei139 – 1391Phycoerythrobilin chromophore 2 (covalent; via 1 link)

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
  2. photosynthesis Source: UniProtKB-KW
  3. protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
B-phycoerythrin alpha chain
Gene namesi
Name:cpeA
Encoded oniPlastid; Chloroplast
OrganismiPorphyridium purpureum (Red alga) (Porphyridium cruentum)
Taxonomic identifieri35688 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaePorphyridialesPorphyridiaceaePorphyridium

Subcellular locationi

Plastidchloroplast thylakoid membrane By similarity; Peripheral membrane protein By similarity; Stromal side By similarity
Note: Forms the periphery of the phycobilisome rod.By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. phycobilisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164B-phycoerythrin alpha chainPRO_0000199176Add
BLAST

Post-translational modificationi

Contains two covalently linked bilin chromophores.

Interactioni

Subunit structurei

Heteropolymer of 6 alpha, 6 beta and one gamma chain.By similarity

Protein-protein interaction databases

IntActiP11392. 1 interaction.
MINTiMINT-8389565.

Structurei

Secondary structure

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512
Helixi21 – 6242
Helixi64 – 674
Helixi76 – 9924
Helixi103 – 1086
Turni109 – 1124
Helixi113 – 1197
Helixi124 – 13714
Turni140 – 1434
Helixi146 – 16217

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V57X-ray1.70A/C1-164[»]
3V58X-ray1.85A/C1-164[»]
ProteinModelPortaliP11392.
SMRiP11392. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phycobiliprotein family.Curated

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

P11392-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKSVITTVVS AADAAGRFPS NSDLESIQGN IQRSAARLEA AEKLAGNHEA
60 70 80 90 100
VVKEAGDACF AKYAYLKNPG EAGENQEKIN KCYRDVDHYM RLVNYDLVVG
110 120 130 140 150
GTGPLDEWGI AGAREVYRTL NLPTSAYVAS IAYTRDRLCV PRDMSAQAGV
160
EFSAYLDYLI NALS
Length:164
Mass (Da):17,817
Last modified:July 1, 1989 - v1
Checksum:iA704CE21D52B8D7E
GO

Sequence databases

PIRiS02817.

Cross-referencesi

Sequence databases

PIRi S02817.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V57 X-ray 1.70 A/C 1-164 [» ]
3V58 X-ray 1.85 A/C 1-164 [» ]
ProteinModelPortali P11392.
SMRi P11392. Positions 1-164.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11392. 1 interaction.
MINTi MINT-8389565.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.490.20. 1 hit.
InterProi IPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view ]
Pfami PF00502. Phycobilisome. 1 hit.
[Graphical view ]
PIRSFi PIRSF000081. Phycocyanin. 1 hit.
SUPFAMi SSF46458. SSF46458. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum."
    Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.
    Biol. Chem. Hoppe-Seyler 370:115-124(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies."
    Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.
    J. Biol. Chem. 259:5472-5480(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 79-84 AND 136-142, CHROMOPHORE BINDING AT CYS-82 AND CYS-139.

Entry informationi

Entry nameiPHEA_PORPP
AccessioniPrimary (citable) accession number: P11392
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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