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

GO - Cellular componenti

  1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
  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.

Family & Domainsi

Sequence similaritiesi

Belongs to the phycobiliprotein family.

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

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MKSVITTVVS AADAAGRFPS NSDLESIQGN IQRSAARLEA AEKLAGNHEA    50
VVKEAGDACF AKYAYLKNPG EAGENQEKIN KCYRDVDHYM RLVNYDLVVG 100
GTGPLDEWGI AGAREVYRTL NLPTSAYVAS IAYTRDRLCV PRDMSAQAGV 150
EFSAYLDYLI NALS 164
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: January 22, 2014
This is version 74 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

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