Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00433

- PHE3_RHDS2

UniProt

Q00433 - PHE3_RHDS2

Protein

Phycoerythrin alpha-3 chain, chloroplastic

Gene

cpeA3

Organism
Rhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 71115,16-dihydrobiliverdin chromophore (covalent; via 1 link)2 Publications
    Binding sitei73 – 73115,16-dihydrobiliverdin chromophore2 Publications
    Binding sitei93 – 93115,16-dihydrobiliverdin chromophore2 Publications

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW
    2. photosynthesis Source: UniProtKB-KW
    3. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Photosynthesis, Transport

    Keywords - Ligandi

    Bile pigment, Chromophore

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phycoerythrin alpha-3 chain, chloroplastic
    Gene namesi
    Name:cpeA3
    OrganismiRhodomonas sp. (strain CS 24) (Chroomonas sp. (strain CS24))
    Taxonomic identifieri79257 [NCBI]
    Taxonomic lineageiEukaryotaCryptophytaPyrenomonadalesPyrenomonadaceaeRhodomonas

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
    2. phycobilisome Source: InterPro

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Thylakoid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252ChloroplastAdd
    BLAST
    Chaini53 – 12876Phycoerythrin alpha-3 chain, chloroplasticPRO_0000002828Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei56 – 5615-hydroxylysine2 Publications

    Post-translational modificationi

    Contains one covalently linked 15,16-dihydrobiliverdin chromophore.

    Keywords - PTMi

    Hydroxylation

    Interactioni

    Subunit structurei

    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.2 Publications

    Structurei

    Secondary structure

    1
    128
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi59 – 679
    Helixi86 – 894
    Beta strandi90 – 989
    Helixi103 – 11311
    Beta strandi120 – 1223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QGWX-ray1.63A53-128[»]
    1XF6X-ray1.10A53-128[»]
    1XG0X-ray0.97A53-128[»]
    ProteinModelPortaliQ00433.
    SMRiQ00433. Positions 53-128.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00433.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni77 – 78215,16-dihydrobiliverdin chromophore binding

    Sequence similaritiesi

    Belongs to the phycoerythrin family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di3.90.510.10. 1 hit.
    InterProiIPR011070. Globular_prot_asu/bsu.
    IPR004228. Phycoerythr_a_core.
    IPR006311. TAT_signal.
    [Graphical view]
    PfamiPF02972. Phycoerythr_ab. 1 hit.
    [Graphical view]
    ProDomiPD019398. Phycoerythr_a/b_core. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF56568. SSF56568. 1 hit.
    PROSITEiPS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q00433-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFAKTLASLA VIGSAAAYVP MMSMDMGRRE VVQAGAAAAA VTPFLSGAPA    50
    GAAMDKSAKA PQITIFDHRG CSRAPKESTG GKAGGQDDEM MVKVASTKVT 100
    VSESDAAKKL QEFITFEKGI DGPFTSKN 128
    Length:128
    Mass (Da):13,175
    Last modified:May 27, 2002 - v2
    Checksum:i44B1ECFD62C12732
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006994 Genomic DNA. Translation: CAA07415.2.
    PIRiS12900.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ006994 Genomic DNA. Translation: CAA07415.2 .
    PIRi S12900.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q00433.
    SMRi Q00433. Positions 53-128.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q00433.

    Family and domain databases

    Gene3Di 3.90.510.10. 1 hit.
    InterProi IPR011070. Globular_prot_asu/bsu.
    IPR004228. Phycoerythr_a_core.
    IPR006311. TAT_signal.
    [Graphical view ]
    Pfami PF02972. Phycoerythr_ab. 1 hit.
    [Graphical view ]
    ProDomi PD019398. Phycoerythr_a/b_core. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF56568. SSF56568. 1 hit.
    PROSITEi PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    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 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, HYDROXYLATION AT LYS-56.
    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 53-128 IN COMPLEX WITH CPEA2; CPEB AND 15,16-DIHYDROBILIVERDIN, SUBUNIT, HYDROXYLATION AT LYS-56.

    Entry informationi

    Entry nameiPHE3_RHDS2
    AccessioniPrimary (citable) accession number: Q00433
    Secondary accession number(s): O82050
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: May 27, 2002
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    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.

    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

    External Data

    Dasty 3