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Protein

B-phycoerythrin alpha chain

Gene

cpeA

Organism
Porphyridium purpureum (Red alga) (Porphyridium cruentum)
Status
Reviewed-Annotation score: 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

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

GO - Cellular componenti

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 – 1512Combined sources
Helixi21 – 6242Combined sources
Helixi64 – 674Combined sources
Helixi76 – 9924Combined sources
Helixi103 – 1086Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1197Combined sources
Helixi124 – 13714Combined sources
Turni140 – 1434Combined sources
Helixi146 – 16217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

PIRiS02817.

3D structure databases

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

Protein-protein interaction databases

IntActiP11392. 1 interaction.
MINTiMINT-8389565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

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 7, 2015
This is version 78 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

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.