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Protein

R-phycocyanin alpha chain

Gene

rpcA

Organism
Polysiphonia urceolata (Red alga) (Conferva urceolata)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Phycocyanobilin chromophore (covalent; via 1 link)1 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:
R-phycocyanin alpha chain
Gene namesi
Name:rpcA
Encoded oniPlastid; Chloroplast
OrganismiPolysiphonia urceolata (Red alga) (Conferva urceolata)
Taxonomic identifieri65404 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaFlorideophyceaeCeramialesRhodomelaceaePolysiphonia

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 – 162162R-phycocyanin alpha chainPRO_0000199135Add
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

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
Helixi65 – 684Combined sources
Beta strandi74 – 774Combined sources
Helixi78 – 10124Combined sources
Helixi105 – 1106Combined sources
Turni111 – 1144Combined sources
Helixi115 – 1217Combined sources
Helixi126 – 13914Combined sources
Helixi144 – 16118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F99X-ray2.40A/K/M1-162[»]
ProteinModelPortaliP59858.
SMRiP59858. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59858.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 875Phycocyanobilin chromophore-binding
Regioni115 – 12410Phycocyanobilin 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.

P59858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPLTEAIA AADSQGRFLS NTELQVVNGR YNRATSSLEA AKALTANADR
60 70 80 90 100
LISGAANAVY SKFPYTTQMP GPNYSSTAIG KAKCARDIGY YLRMVTYCLV
110 120 130 140 150
VGGTGPMDDY LVAGLEEINR TFELSPSWYI EALKYIKNNH GLSGDVANEA
160
NTYIDYAINT LS
Length:162
Mass (Da):17,570
Last modified:September 26, 2003 - v1
Checksum:i6DC32AE0BB371BA2
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F99X-ray2.40A/K/M1-162[»]
ProteinModelPortaliP59858.
SMRiP59858. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP59858.

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...

Publicationsi

  1. "Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome."
    Jiang T., Zhang J.P., Chang W.R., Liang D.C.
    Biophys. J. 81:1171-1179(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH RPCB AND PHYCOCYANOBILIN, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiPHCA_POLUR
AccessioniPrimary (citable) accession number: P59858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: September 26, 2003
Last modified: October 14, 2015
This is version 61 of the entry and version 1 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

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.