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Protein

C-phycocyanin alpha chain

Gene

cpcA

Organism
Galdieria sulphuraria (Red alga)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Phycocyanobilin chromophore (covalent; via 1 link)1 Publication
Binding sitei128 – 1281Phycocyanobilin chromophore1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
C-phycocyanin alpha chain
Gene namesi
Name:cpcA
Encoded oniPlastid; Chloroplast
OrganismiGaldieria sulphuraria (Red alga)
Taxonomic identifieri130081 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162C-phycocyanin alpha chainPRO_0000199121Add
BLAST

Post-translational modificationi

Contains one covalently linked phycocyanobilin chromophore.

Interactioni

Subunit structurei

Heterododecamer of 6 alpha and 6 beta chains. The basic functional unit of phycobiliproteins is a ring-shaped hexamer formed from two back-to-back trimers contacting via the alpha chain subunits. The trimers are composed of alpha/beta subunit heterodimers arranged around a three-fold axis of symmetry. The phycoerythrins also contain a gamma subunit which is located in the center of the hexamer.1 Publication

Protein-protein interaction databases

MINTiMINT-94258.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi21 – 4626Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 674Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 10124Combined sources
Helixi105 – 1106Combined sources
Turni111 – 1144Combined sources
Helixi115 – 1217Combined sources
Helixi126 – 13914Combined sources
Helixi144 – 16017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHNX-ray1.65A1-162[»]
3BRPX-ray1.85A1-162[»]
3KVSX-ray1.50A1-162[»]
ProteinModelPortaliP00306.
SMRiP00306. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00306.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 754Phycocyanobilin chromophore-binding
Regioni83 – 875Phycocyanobilin chromophore-binding

Sequence similaritiesi

Belongs to the phycobiliprotein family.Curated

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
IPR006246. Phycocyanin_a.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
TIGRFAMsiTIGR01338. phycocy_alpha. 1 hit.

Sequencei

Sequence statusi: Complete.

P00306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPITEAIA AADNQGRFLS NTELQAVNGR YQRAAASLEA ARSLTSNAER
60 70 80 90 100
LINGAAQAVY SKFPYTSQMP GPQYASSAVG KAKCARDIGY YLRMVTYCLV
110 120 130 140 150
VGGTGPMDEY LIAGLEEINR TFDLSPSWYV EALNYIKANH GLSGQAANEA
160
NTYIDYAINA LS
Length:162
Mass (Da):17,506
Last modified:February 1, 1996 - v3
Checksum:iC941FDE84CDCBD95
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491E → Q in AAB01593 (Ref. 4) Curated
Sequence conflicti61 – 611S → Q AA sequence (Ref. 1) Curated
Sequence conflicti95 – 951V → I AA sequence (Ref. 1) Curated
Sequence conflicti101 – 1011V → A AA sequence (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77125 mRNA. Translation: AAB34028.1.
L13467 Genomic DNA. Translation: AAB01593.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77125 mRNA. Translation: AAB34028.1.
L13467 Genomic DNA. Translation: AAB01593.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHNX-ray1.65A1-162[»]
3BRPX-ray1.85A1-162[»]
3KVSX-ray1.50A1-162[»]
ProteinModelPortaliP00306.
SMRiP00306. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-94258.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00306.

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
IPR006246. Phycocyanin_a.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
TIGRFAMsiTIGR01338. phycocy_alpha. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHCA_GALSU
AccessioniPrimary (citable) accession number: P00306
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The light-harvesting antenna system in red algae and cyanobacteria is formed of phycobilisomes. These are composed of the phycobiliproteins phycoerythrin (CPE), phycocyanin (CPC) and allophycocyanin (APC). Cyanobacteria also contain phycoerythrocyanin (PCC). The phycobiliproteins all share the same subunit composition and organization with variations in the covalently bound open-chain tetrapyrrole chromophores. The phycobiliprotein complexes are arranged sequentially in antenna complexes linked by linker proteins with CPE at the periphery, CPC in the middle and APC at the core feeding to the photosynthetic reaction center.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.