Phycoerythrin alpha-3 chain, chloroplastic precursor

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Q00433 (PHE3_RHDS2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phycoerythrin alpha-3 chain, chloroplastic

Gene names

Name:

cpeA3

Organism

Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24))

Taxonomic identifier

79257 [NCBI]

Taxonomic lineage

Eukaryota › Cryptophyta › Pyrenomonadales › Pyrenomonadaceae › Rhodomonas

Protein attributes

Sequence length	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast 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.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Plastid Thylakoid
Domain	Transit peptide
Ligand	Bile pigment Chromophore
PTM	Hydroxylation
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell phycobilisome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 52

Chloroplast

Chain

53 – 128

Phycoerythrin alpha-3 chain, chloroplastic

PRO_0000002828

Regions

Region

77 – 78

15,16-dihydrobiliverdin chromophore binding

Sites

Binding site

15,16-dihydrobiliverdin chromophore (covalent; via 1 link)

Binding site

15,16-dihydrobiliverdin chromophore

Binding site

15,16-dihydrobiliverdin chromophore

Amino acid modifications

Modified residue

5-hydroxylysine Ref.4 Ref.5

Secondary structure

128

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q00433 [UniParc].

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

FASTA

128

13,175

        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.

PIR

S12900.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QGW	X-ray	1.63	A	53-128	[»]
1XF6	X-ray	1.10	A	53-128	[»]
1XG0	X-ray	0.97	A	53-128	[»]

ProteinModelPortal

Q00433.

SMR

Q00433. Positions 53-128.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.90.510.10. 1 hit.

InterPro

IPR011070. Globular_prot_asu/bsu.
IPR004228. Phycoerythr_a/b_core.
IPR006311. TAT_signal.
[Graphical view]

Pfam

PF02972. Phycoerythr_ab. 1 hit.
[Graphical view]

ProDom

PD019398. Phycoerythr_a/b_core. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF56568. AlphaBeta_subunt. 1 hit.

PROSITE

PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q00433.

Entry information

Entry name

PHE3_RHDS2

Accession

Primary (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:	April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents