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Protein

Phycoerythrocyanin alpha chain

Gene

pccA

Organism
Mastigocladus laminosus (Fischerella sp.)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

Absorptioni

Abs(max)=~550 nm

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Phycoviolobilin chromophore (covalent; via 1 link)

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Phycoerythrocyanin alpha chain
Gene namesi
Name:pccA
OrganismiMastigocladus laminosus (Fischerella sp.)
Taxonomic identifieri83541 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaStigonematalesMastigocladus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Phycobilisome, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Phycoerythrocyanin alpha chainPRO_0000199169Add
BLAST

Post-translational modificationi

Contains one covalently linked bilin chromophore.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1512Combined sources
Turni21 – 244Combined sources
Helixi25 – 284Combined sources
Helixi31 – 6232Combined sources
Helixi64 – 663Combined sources
Beta strandi71 – 744Combined sources
Helixi78 – 10124Combined sources
Helixi105 – 1106Combined sources
Turni111 – 1144Combined sources
Helixi115 – 1184Combined sources
Turni119 – 1224Combined sources
Helixi126 – 13813Combined sources
Helixi144 – 16017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7JX-ray3.00A1-162[»]
2C7KX-ray3.20A1-162[»]
2C7LX-ray2.85A1-162[»]
2J96X-ray2.25A/B1-162[»]
ProteinModelPortaliP00309.
SMRiP00309. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00309.

Family & Domainsi

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.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

P00309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPLTEAIA AADLRGSYLS NTELQAVFGR FNRARAGLEA ARAFANNGKK
60 70 80 90 100
WAEAAANHVY QKFPYTTQMQ GPQYASTPEG KAKCVRDIDH YLRTISYCCV
110 120 130 140 150
VGGTGPLDDY VVAGLKEFNS ALGLSPSWYI AALEFVRDNH GLTGDVAGEA
160
NTYINYAINA LS
Length:162
Mass (Da):17,564
Last modified:July 21, 1986 - v1
Checksum:iC069332836F2BD2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34254 Genomic DNA. Translation: AAC64654.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34254 Genomic DNA. Translation: AAC64654.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7JX-ray3.00A1-162[»]
2C7KX-ray3.20A1-162[»]
2C7LX-ray2.85A1-162[»]
2J96X-ray2.25A/B1-162[»]
ProteinModelPortaliP00309.
SMRiP00309. Positions 1-162.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00309.

Family and domain databases

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

Publicationsi

  1. "Genes encoding both subunits of phycoerythrocyanin, a light-harvesting biliprotein from the cyanobacterium Mastigocladus laminosus."
    Eberlein M., Kufer W.
    Gene 94:133-136(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete amino-acid sequence of both subunits of phycoerythrocyanin from the thermophilic cyanobacterium Mastigocladus laminosus."
    Fueglistaller P., Suter F., Zuber H.
    Hoppe-Seyler's Z. Physiol. Chem. 364:691-712(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  3. "Chromopeptides from phycoerythrocyanin. Structure and linkage of the three bilin groups."
    Bishop J.E., Rapoport H., Klotz A.V., Chan C.F., Glazer A.N., Fueglistaller P., Zuber H.
    J. Am. Chem. Soc. 109:875-881(1987)
    Cited for: CHROMOPHORE STRUCTURE, CHROMOPHORE BINDING AT CYS-84.
  4. "Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A."
    Duerring M., Huber R., Bode W., Ruembelli R., Zuber H.
    J. Mol. Biol. 211:633-644(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. "Structural basis for the photochemistry of alpha-phycoerythrocyanin."
    Schmidt M., Patel A., Zhao Y., Reuter W.
    Biochemistry 46:416-423(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-162, CHROMOPHORE BINDING AT CYS-84.

Entry informationi

Entry nameiPHEA_MASLA
AccessioniPrimary (citable) accession number: P00309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 14, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.