A0A4Q4VZL8 · A0A4Q4VZL8_9PEZI
- ProteinChaperone DnaJ C-terminal domain-containing protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids159 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | FAD binding | |
Molecular Function | oxidoreductase activity |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChaperone DnaJ C-terminal domain-containing protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Xylariomycetidae > Xylariales > Xylariales incertae sedis > Monosporascus
Accessions
- Primary accessionA0A4Q4VZL8
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 23-49 | Disordered | ||||
Sequence: PDGDASENLEDRSSTGHDSCHGRGVRD | ||||||
Compositional bias | 27-49 | Basic and acidic residues | ||||
Sequence: ASENLEDRSSTGHDSCHGRGVRD | ||||||
Domain | 49-96 | Flavoprotein pyridine nucleotide cytochrome reductase-like FAD-binding | ||||
Sequence: DGDGTFDLTIETYFPGDKQPGGAMSNILDFLPIGEQVELPGPTGEILY | ||||||
Domain | 107-159 | Oxidoreductase FAD/NAD(P)-binding | ||||
Sequence: QKLRVVDANKSEKDILLRVDVDKFQTKSRGQLSVTHDLSHPGDSWEGFKGHVN |
Sequence similarities
Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length159
- Mass (Da)17,409
- Last updated2019-07-31 v1
- Checksum0F2C333396FA710D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 27-49 | Basic and acidic residues | ||||
Sequence: ASENLEDRSSTGHDSCHGRGVRD |
Keywords
- Technical term