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An12g05810 uncharacterized protein [ Aspergillus niger ]

Gene ID: 4985931, updated on 17-May-2024

Summary

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Gene symbol
An12g05810
Gene description
uncharacterized protein
Locus tag
An12g05810
See related
FungiDB:An12g05810; VEuPathDB:An12g05810
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Aspergillus niger
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Aspergillus subgen. Circumdati
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Genomic context

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See An12g05810 in Genome Data Viewer
Location:
chromosome: III, map: unlocalized, clone: An12
Exon count:
9

NT_166527.1Genomic Context describing neighboring genes Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

Genomic regions, transcripts, and products

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Genomic Sequence:
NT_166527.1

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Pel HJ, et al. Nat Biotechnol, 2007 Feb. PMID 17259976
  2. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article
  3. TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Tang H, et al. Bioinformatics, 2019 Feb 1. PMID 30032202, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

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Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables copper ion binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
uncharacterized protein
XP_001395646.1
  • Catalytic activity: laccases convert 4 benzenediol + O(2) <=> 4 benzosemiquinone + 2 H(2)O.;
    Function: laccase (urishiol oxidase) is an multi-copper enzyme found in fungi and plants with low specificity on both catechol and p-benzenediol, which oxidizes many different types of phenols and diamines.;
    Function: laccase of C. parasitica is involved in the lignin degradation an detoxification of lignin-derived products.;
    Induction: copper is needed as cofactor.;
    Remark: the A. nidulans homologue of the ORF encodes a dihydrogeodin oxidase, that catalyzes the regio- and stereospecific phenol oxidative coupling reaction to form (+)-geodin from dihydrogeodin.;
    Similarity: shows similarity to several laccases,phenol oxidases of different organisms.;
    Title: strong similarity to laccase - Cryphonectria parasitica;
    See PMID 3032923;
    See PMID 7665560;
    See PMID 1535523

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NT_166527.1 Reference assembly

    Range
    1437880..1440370
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_001395609.1 → XP_001395646.1  uncharacterized protein An12g05810 [Aspergillus niger]

    See identical proteins and their annotated locations for XP_001395646.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A370BNG4, A2QZQ7
    Conserved Domains (4) summary
    cd13854
    Location:111 → 237
    CuRO_1_MaLCC_like; The first cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces
    cd13880
    Location:242 → 399
    CuRO_2_MaLCC_like; The second cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces
    cd13901
    Location:431 → 618
    CuRO_3_MaLCC_like; The third cupredoxin domain of the fungal laccases similar to Ma-LCC from Melanocarpus albomyces
    TIGR03388
    Location:142 → 630
    ascorbase; L-ascorbate oxidase, plant type
Nucleotide Protein
Heading Accession and Version

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