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Protein

R-phycoerythrin alpha chain

Gene

cpeA

Organism
Polysiphonia urceolata (Red alga) (Conferva urceolata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei47Phycoerythrobilin chromophore 21
Binding sitei81Phycoerythrobilin chromophore 11
Binding sitei82Phycoerythrobilin chromophore 1 (covalent; via 1 link)1
Binding sitei84Phycoerythrobilin chromophore 11
Binding sitei88Phycoerythrobilin chromophore 11
Binding sitei137Phycoerythrobilin chromophore 21
Binding sitei139Phycoerythrobilin chromophore 2 (covalent; via 1 link)1
Binding sitei142Phycoerythrobilin chromophore 21

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
R-phycoerythrin alpha chain
Gene namesi
Name:cpeA
Synonyms:rpeA
Encoded oniPlastid; ChloroplastCurated
OrganismiPolysiphonia urceolata (Red alga) (Conferva urceolata)
Taxonomic identifieri65404 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeCeramialesRhodomelaceaePolysiphonia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002405981 – 164R-phycoerythrin alpha chainAdd BLAST164

Post-translational modificationi

Contains two covalently linked phycoerythrobilin chromophores. In PubMed:8876649 the authors refer to the bilins as phycoerythrobilins. In the PDB entries, the bilins are named as phycocyanobilins although the modeled compounds correspond to phycoerythrobilins.

Interactioni

Subunit structurei

Heterododecamer of 6 alpha and 6 beta chains. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer.1 Publication

Structurei

Secondary structure

1164
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Helixi21 – 46Combined sources26
Helixi48 – 62Combined sources15
Helixi64 – 67Combined sources4
Helixi76 – 99Combined sources24
Helixi103 – 108Combined sources6
Turni109 – 112Combined sources4
Helixi113 – 119Combined sources7
Helixi124 – 137Combined sources14
Turni140 – 143Combined sources4
Helixi146 – 163Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LIAX-ray2.80A/K1-164[»]
3MWNX-ray2.60A32-164[»]
ProteinModelPortaliP84861.
SMRiP84861.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84861.

Family & Domainsi

Sequence similaritiesi

Belongs to the phycobiliprotein family.Sequence analysis

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.

P84861-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSVITTTIS AADAAGRYPS TSDLQSVQGN IQRAAARLEA AEKLGSNHEA
60 70 80 90 100
VVKEAGDACF SKYGYNKNPG EAGENQEKIN KCYRDIDHYM RLINYTLVVG
110 120 130 140 150
GTGPLDEWGI AGAREVYRTL NLPSAAYIAA FVFTRDRLCI PRDMSAQAGV
160
EFCTALDYLI NSLS
Length:164
Mass (Da):17,836
Last modified:June 27, 2006 - v1
Checksum:iCD0F348B0EF7716F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LIAX-ray2.80A/K1-164[»]
3MWNX-ray2.60A32-164[»]
ProteinModelPortaliP84861.
SMRiP84861.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP84861.

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...

Entry informationi

Entry nameiPHEA_POLUR
AccessioniPrimary (citable) accession number: P84861
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 27, 2006
Last modified: November 2, 2016
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The light-harvesting antenna system in red algae and cyanobacteria is formed of phycobilisomes. These are composed of the phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin (PCC). The phycobiliproteins all share the same subunit composition and organization with variations in the covalently bound open-chain tetrapyrrole chromophores. The phycobiliprotein complexes are arranged sequentially in antenna complexes linked by linker proteins with CPE at the periphery, CPC in the middle and APC at the core feeding to the photosynthetic reaction center.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.