P34784 · PHEG_AGLNE

Function

function

Critical for the incorporation of phycoerythrin in the phycobilisome complex.

Features

Showing features for binding site.

131720406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site94phycourobilin 1 (UniProtKB | ChEBI); covalent
Binding site133phycourobilin 2 (UniProtKB | ChEBI); covalent
Binding site210(2R,3E)-phycoerythrobilin (UniProtKB | ChEBI); covalent
Binding site297phycourobilin 3 (UniProtKB | ChEBI); covalent

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchloroplast thylakoid membrane
Cellular Componentphycobilisome
Biological Processphotosynthesis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    R-phycoerythrin gamma chain, chloroplastic

Organism names

Accessions

  • Primary accession
    P34784

Subcellular Location

Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein
Note: Forms the periphery of the phycobilisome rod.

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-40Chloroplast
ChainPRO_000000282941-317R-phycoerythrin gamma chain, chloroplastic

Post-translational modification

Contains four covalently linked bilin chromophores.

Interaction

Subunit

Heteromer of 1 alpha, 1 beta and 2 gamma chains.

Structure

Family & Domains

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    317
  • Mass (Da)
    34,641
  • Last updated
    1994-02-01 v1
  • Checksum
    1873254B9094F5E2
MASPAFAVNGMFTPVKLSGSFTASMPVDSKPAASATGVRMVVDPLQRKYQSIGKIGVDYSRPKKLATYVRSGYSVGMEFPNTPSMAGHYSLTDCDKAGGAAKILMKYDEYCAKGMLQVGKRAACRTGVYTTKCTEGTQPQMAFDVRVFNRTQAFRQAQKPVAARLREQYEARKACFVLAHNCSREEAQFKEMPMSCATFLASKMEATGACYRTVRPTSVAEDYMAGSVRAQLYTKLNPKGVYGVGACEDGHAKGDADQRRVIALASEYRAAAQSPSTVTGQQYKSAQLATQLFAHDCHHEQEQIYEYPAVAAAMCRY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L13695
EMBL· GenBank· DDBJ
AAA32635.1
EMBL· GenBank· DDBJ
mRNA

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