Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q00433 (PHE3_RHDS2) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 89. 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-3 chain, chloroplastic
Gene names
Name:cpeA3
OrganismRhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24))
Taxonomic identifier79257 [NCBI]
Taxonomic lineageEukaryotaCryptophytaPyrenomonadalesPyrenomonadaceaeRhodomonas

Protein attributes

Sequence length128 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.4 Ref.5

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 – 5252Chloroplast
Chain53 – 12876Phycoerythrin alpha-3 chain, chloroplastic
PRO_0000002828

Regions

Region77 – 78215,16-dihydrobiliverdin chromophore binding

Sites

Binding site71115,16-dihydrobiliverdin chromophore (covalent; via 1 link)
Binding site73115,16-dihydrobiliverdin chromophore
Binding site93115,16-dihydrobiliverdin chromophore

Amino acid modifications

Modified residue5615-hydroxylysine Ref.4 Ref.5

Secondary structure

.......... 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00433 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 44B1ECFD62C12732

FASTA12813,175
        10         20         30         40         50         60 
MFAKTLASLA VIGSAAAYVP MMSMDMGRRE VVQAGAAAAA VTPFLSGAPA GAAMDKSAKA 

        70         80         90        100        110        120 
PQITIFDHRG CSRAPKESTG GKAGGQDDEM MVKVASTKVT VSESDAAKKL QEFITFEKGI 


DGPFTSKN 

« Hide

References

[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Jenkins J., Hiller R.G., Speirs J., Godovac-Zimmermann J.
FEBS Lett. 279:361-361(1991) [PubMed] [Europe PMC] [Abstract]
[3]"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], SEQUENCE REVISION TO 62.
[4]"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 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, HYDROXYLATION AT LYS-56.
[5]"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 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, HYDROXYLATION AT LYS-56.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006994 Genomic DNA. Translation: CAA07415.2.
PIRS12900.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QGWX-ray1.63A53-128[»]
1XF6X-ray1.10A53-128[»]
1XG0X-ray0.97A53-128[»]
ProteinModelPortalQ00433.
SMRQ00433. Positions 53-128.
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.
IPR006311. TAT_signal.
[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.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ00433.

Entry information

Entry namePHE3_RHDS2
AccessionPrimary (citable) accession number: Q00433
Secondary accession number(s): O82050
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: October 16, 2013
This is version 89 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