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Protein

C-phycocyanin beta chain

Gene

cpcB

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 sitei35 – 351Phycocyanobilin chromophore 11 Publication
Binding sitei39 – 391Phycocyanobilin chromophore 11 Publication
Binding sitei72 – 721Phycocyanobilin chromophore 21 Publication
Binding sitei77 – 771Phycocyanobilin chromophore 21 Publication
Binding sitei82 – 821Phycocyanobilin chromophore 2 (covalent; via 1 link)1 Publication
Binding sitei153 – 1531Phycocyanobilin chromophore 1 (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:
C-phycocyanin beta chain
Gene namesi
Name:cpcB
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 – 172172C-phycocyanin beta chainPRO_0000199149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721N4-methylasparagine1 Publication

Post-translational modificationi

Contains two covalently linked phycocyanobilin chromophores.

Keywords - PTMi

Methylation

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-94276.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi21 – 3212Combined sources
Helixi34 – 4613Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 663Combined sources
Helixi76 – 9924Combined sources
Helixi103 – 1086Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1208Combined sources
Helixi124 – 14219Combined sources
Helixi154 – 17017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHNX-ray1.65B1-172[»]
3BRPX-ray1.85B1-172[»]
3KVSX-ray1.50B1-172[»]
ProteinModelPortaliP00311.
SMRiP00311. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00311.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 887Phycocyanobilin chromophore 2 binding
Regioni149 – 1513Phycocyanobilin chromophore 1 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.
IPR006247. Phycocyanin_b.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
TIGRFAMsiTIGR01339. phycocy_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P00311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDAFAKVVA QADARGEFLS NTQLDALSKM VSEGNKRLDV VNRITSNASA
60 70 80 90 100
IVTNAARALF SEQPQLIQPG GNAYTNRRMA ACLRDMEIIL RYVSYAIIAG
110 120 130 140 150
DSSILDDRCL NGLRETYQAL GVPGASVAVG IEKMKDSAIA IANDPSGITT
160 170
GDCSALMAEV GTYFDRAATA VQ
Length:172
Mass (Da):18,253
Last modified:July 19, 2004 - v4
Checksum:iF271B4D8CD5963CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721N → I in AAB01592 (PubMed:7716249).Curated
Sequence conflicti72 – 721N → T in AAB34027 (PubMed:7716249).Curated
Sequence conflicti72 – 721N → T no nucleotide entry (PubMed:7028751).Curated
Sequence conflicti104 – 1041I → V in AAB01592 (PubMed:7716249).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77125 mRNA. Translation: AAB34027.2.
L13467 Genomic DNA. Translation: AAB01592.1.
PIRiA00320. CFKKB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S77125 mRNA. Translation: AAB34027.2.
L13467 Genomic DNA. Translation: AAB01592.1.
PIRiA00320. CFKKB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PHNX-ray1.65B1-172[»]
3BRPX-ray1.85B1-172[»]
3KVSX-ray1.50B1-172[»]
ProteinModelPortaliP00311.
SMRiP00311. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-94276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00311.

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
IPR006247. Phycocyanin_b.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
TIGRFAMsiTIGR01339. phycocy_beta. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPHCB_GALSU
AccessioniPrimary (citable) accession number: P00311
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 106 of the entry and version 4 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.