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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Phycoerythrobilin chromophore 2
Binding sitei81 – 811Phycoerythrobilin chromophore 1
Binding sitei82 – 821Phycoerythrobilin chromophore 1 (covalent; via 1 link)
Binding sitei84 – 841Phycoerythrobilin chromophore 1
Binding sitei88 – 881Phycoerythrobilin chromophore 1
Binding sitei137 – 1371Phycoerythrobilin chromophore 2
Binding sitei139 – 1391Phycoerythrobilin chromophore 2 (covalent; via 1 link)
Binding sitei142 – 1421Phycoerythrobilin chromophore 2

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 164164R-phycoerythrin alpha chainPRO_0000240598Add
BLAST

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

1
164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi21 – 4626Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 674Combined sources
Helixi76 – 9924Combined sources
Helixi103 – 1086Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1197Combined sources
Helixi124 – 13714Combined sources
Turni140 – 1434Combined sources
Helixi146 – 16318Combined sources

3D structure databases

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

Publicationsi

  1. "Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 A resolution."
    Chang W.-R., Jiang T., Wan Z.-L., Zhang J.-P., Yang Z.-X., Liang D.-C.
    J. Mol. Biol. 262:721-731(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PHEB AND PHYCOCYANOBILIN, CHROMOPHORE BINDING AT ASN-47; LYS-81; CYS-82; ARG-84; HIS-88; ARG-137; CYS-139 AND ARG-142, SUBUNIT.

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: December 9, 2015
This is version 44 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.