A0A497LBN5 · A0A497LBN5_9ARCH

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Protein has several cofactor binding sites:
Fe cation (UniProtKB | Rhea| CHEBI:24875 )

Ni2+ (UniProtKB | Rhea| CHEBI:49786 )

Features

Showing features for binding site.

134750100150200250300
TypeIDPosition(s)Description
Binding site44Mg2+ (UniProtKB | ChEBI)
Binding site63Ni2+ (UniProtKB | ChEBI)
Binding site66Fe cation (UniProtKB | ChEBI)
Binding site66Ni2+ (UniProtKB | ChEBI)
Binding site319Mg2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionferredoxin hydrogenase activity
Molecular FunctionNAD binding
Molecular Functionnickel cation binding
Molecular Functionoxidoreductase activity, acting on NAD(P)H
Molecular Functionquinone binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    NADH-quinone oxidoreductase subunit D domain-containing protein

Gene names

    • ORF names
      DRO25_00085

Organism names

Accessions

  • Primary accession
    A0A497LBN5

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain122-282NADH-quinone oxidoreductase subunit D
Domain288-346NADH-quinone oxidoreductase subunit D

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    347
  • Mass (Da)
    39,371
  • Last updated
    2019-06-05 v1
  • Checksum
    2C6C31F7181549BD
MPEIVQIGPYRPQLVEPERFELLVENGKIIDVNIELGYVHRGIEKLFTTKTYMQNLALAERICGICSGVHTLCYAQTAESVMNVNVPERAKYLRCIYMELERLHSHYLWFGVLAHSLHEHDAFLKIMGEREQVQDLLEYLTGNRMNYLINTIGGVRRDITPQKAEKIRKVLKNMNKLSNYLLSLLGENGTFTKKTRGVGILPKEKALNLGAVGPTLRGSGIKSDVRKDDPYAAYGELDFEIVTEKDGDAWAKSLVRARETLESIKIIEQALDNLPDGEIAVKPGEPLEKEEVERAEAPRGELVYYIRSNGTNIPERVKVRTPSFMNAFTLIEMLRGDTLQNARIIIE

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue347

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QMXS01000001
EMBL· GenBank· DDBJ
RLI12487.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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