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P30943 (PHE2_RHDS2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phycoerythrin alpha-2 chain, chloroplastic
Gene names
Name:cpeA2
OrganismRhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24))
Taxonomic identifier79257 [NCBI]
Taxonomic lineageEukaryotaCryptophytaPyrenomonadalesPyrenomonadaceaeRhodomonas

Protein attributes

Sequence length104 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Heterotetramer of 2 different alpha chains and 2 identical beta chains. The subunit composition could comprise of any combination of 2 out of 4 different alpha units with an invariant beta unit. Ref.3 Ref.4

Subcellular location

Plastidchloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side.

Post-translational modification

Contains one covalently linked 15,16-dihydrobiliverdin chromophore.

Miscellaneous

The light-harvesting system in Cryptophytes contains phycobiliprotein complexes. Unusually they are composed of either phycoerythrin (CPE) or phycocyanin (CPC) but never allophycocyanin (APC), with only one type of biliprotein being present in any one species. Unlike cyanobacteria or red algae these proteins are not arranged into higher-order phycobilisome complexes, and they are found in the thylakoid lumen.

Sequence similarities

Belongs to the phycoerythrin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Chloroplast Ref.2
Chain38 – 10467Phycoerythrin alpha-2 chain, chloroplastic
PRO_0000002827

Regions

Region61 – 63315,16-dihydrobiliverdin chromophore

Sites

Binding site56115,16-dihydrobiliverdin chromophore (covalent; via 1 link)
Binding site58115,16-dihydrobiliverdin chromophore
Binding site78115,16-dihydrobiliverdin chromophore

Amino acid modifications

Modified residue4115-hydroxylysine Ref.3

Experimental info

Sequence conflict63 – 7412YTGAK…GKDDE → TSKSGKSGQDDT AA sequence Ref.2

Secondary structure

........ 104
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30943 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 1474D433E8CB4396

FASTA10410,696
        10         20         30         40         50         60 
MSAKIIAFSA VVATASAFAP TAGFVPRLRS GATSVNMAMD KSAKAPVITI FDHRGCSRAP 

        70         80         90        100 
KEYTGAKAGG KDDEMMVKAQ SVKIEVSTGT AEGVLATSLA KMTK 

« Hide

References

[1]"Nuclear-encoded genes of phycoerythrin alpha subunits."
Hiller R.G., Howe C.E.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A genomic clone encoding a cryptophyte phycoerythrin alpha-subunit. Evidence for three alpha-subunits and an N-terminal membrane transit sequence."
Jenkins J., Hiller R.G., Speirs J., Godovac-Zimmermann J.
FEBS Lett. 273:191-194(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-82.
[3]"Evolution of a light-harvesting protein by addition of new subunits and rearrangement of conserved elements: crystal structure of a cryptophyte phycoerythrin at 1.63-A resolution."
Wilk K.E., Harrop S.J., Jankova L., Edler D., Keenan G., Sharples F., Hiller R.G., Curmi P.M.
Proc. Natl. Acad. Sci. U.S.A. 96:8901-8906(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2; CPEA3 AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, HYDROXYLATION AT LYS-41.
[4]"Developing a structure-function model for the cryptophyte phycoerythrin 545 using ultrahigh resolution crystallography and ultrafast laser spectroscopy."
Doust A.B., Marai C.N., Harrop S.J., Wilk K.E., Curmi P.M., Scholes G.D.
J. Mol. Biol. 344:135-153(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 38-104 IN COMPLEX WITH CPEA2; CPEA3 AND 15,16-DIHYDROBILIVERDIN, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006994 Genomic DNA. Translation: CAD20039.1.
PIRT10881.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGWX-ray1.63B38-104[»]
1XF6X-ray1.10B38-104[»]
1XG0X-ray0.97B38-104[»]
ProteinModelPortalP30943.
SMRP30943. Positions 38-104.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.510.10. 1 hit.
InterProIPR011070. Globular_prot_asu/bsu.
IPR004228. Phycoerythr_a_core.
[Graphical view]
PfamPF02972. Phycoerythr_ab. 1 hit.
[Graphical view]
ProDomPD019398. Phycoerythr_a/b_core. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56568. SSF56568. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP30943.

Entry information

Entry namePHE2_RHDS2
AccessionPrimary (citable) accession number: P30943
Secondary accession number(s): Q8VX02
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: May 27, 2002
Last modified: October 16, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references