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P23816

- PH62_CHRSP

UniProt

P23816 - PH62_CHRSP

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Protein

Phycocyanin-645 alpha-2 chain

Gene
N/A
Organism
Chroomonas sp.
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Photosynthetic bile pigment-protein complex with maximum absorption at approximately 697 nanometers.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Phycocyanobilin chromophore (covalent; via 1 link)1 Publication

GO - Biological processi

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

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Phycocyanin-645 alpha-2 chain
Short name:
PC-645
OrganismiChroomonas sp.
Taxonomic identifieri3029 [NCBI]
Taxonomic lineageiEukaryotaCryptophytaPyrenomonadalesChroomonadaceaeChroomonas

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8080Phycocyanin-645 alpha-2 chainPRO_0000199211Add
BLAST

Post-translational modificationi

Contains one covalently linked bilin chromophore.

Interactioni

Subunit structurei

Heterotetramer of one alpha-1, one alpha-2, and two beta chains.

Structurei

3D structure databases

ProteinModelPortaliP23816.

Family & Domainsi

Sequence similaritiesi

Belongs to the phycoerythrin family.

Family and domain databases

Gene3Di3.90.510.10. 1 hit.
InterProiIPR011070. Globular_prot_asu/bsu.
IPR004228. Phycoerythr_a_core.
[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.

Sequencei

Sequence statusi: Complete.

P23816-1 [UniParc]FASTAAdd to Basket

« Hide

KNGDLRAPYV EIFDARGCDA KNSQYTGPKS GDMNDDQCVK VSMAVPKVSE   50
ATAEKKRQEF LGFKETAINV PQIAGKTKKY 80
Length:80
Mass (Da):8,814
Last modified:November 1, 1991 - v1
Checksum:iAFC7529A3E8D6D56
GO

Sequence databases

PIRiS10603.

Cross-referencesi

Sequence databases

PIRi S10603.

3D structure databases

ProteinModelPortali P23816.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.90.510.10. 1 hit.
InterProi IPR011070. Globular_prot_asu/bsu.
IPR004228. Phycoerythr_a_core.
[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.
ProtoNeti Search...

Publicationsi

  1. "The complete amino-acid sequence and the phylogenetic origin of phycocyanin-645 from the cryptophytan alga Chroomonas sp."
    Sidler W., Nutt H., Kumpf B., Frank G., Suter F., Brenzel A., Wehrmeyer W., Zuber H.
    Biol. Chem. Hoppe-Seyler 371:537-547(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Structural studies on cryptomonad biliprotein subunits. Two different alpha-subunits in Chroomonas phycocyanin-645 and Cryptomonas phycoerythrin-545."
    Sidler W., Kumpf B., Suter F., Morisset W., Wehrmeyer W., Zuber H.
    Biol. Chem. Hoppe-Seyler 366:233-244(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-69.

Entry informationi

Entry nameiPH62_CHRSP
AccessioniPrimary (citable) accession number: P23816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 16, 2013
This is version 57 of the entry and version 1 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

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3