A5EWZ7 · A5EWZ7_DICNV

Function

Catalytic activity

  • Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
    EC:3.4.11.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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 Functionaminopeptidase activity
Molecular Functionmetallopeptidase activity
Molecular Functionzinc ion binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Aminopeptidase N
  • EC number

Gene names

    • Ordered locus names
      DNO_0019

Organism names

Accessions

  • Primary accession
    A5EWZ7

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain57-197Aminopeptidase N-like N-terminal
Domain236-442Peptidase M1 membrane alanine aminopeptidase
Domain456-552Peptidase M1 alanyl aminopeptidase Ig-like fold
Domain555-875Peptidase M1 alanyl aminopeptidase C-terminal

Sequence similarities

Belongs to the peptidase M1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    881
  • Mass (Da)
    101,057
  • Last updated
    2007-06-12 v1
  • Checksum
    E99F90D3277EDC32
MSTLTITRLNDYRPLAFTVKHHDMKFDLQTDAVIVTHNQEFARSQPKKDERGFDIEQEKNVVLNGEDLQLLDIAIDGKMLPAGKYRYKNDLLTLFDVPDKFTLTTTVRLDPDNNLQLSGLYRSNGIYCTQCEAEGFRRISFGYDRPDALATYRVSIEADKTANPVLLSNGNLEASGDLNEGRHYATWFDPHPKPSYLFALVAGDLAVNAKRFTTTKGKEVELRIYTEAAFIDQTDYALQSLIDAFNWDETRFNLSYDLDRFNLVAISDFNMGAMENKSLNIFNTKFVLANTETAADSDFRAIQRVIGHEYFHNWTGNRITCRDWFQLTLKEGLTVFRDQEFSSDLNERTIKRIEDVELLRREQFAEDGGPMSHPVQPQEYAAIDNFYTRTVYEKGAELIRMYHTIIGEEKFQKGMALYIERHDGQAVCIQDFAQCMEDASDYPFTKQFFDWYTTSGTPKVKFTASYNKTEGSFTLSAHQNISAVNPKRPLVIPIRFSLISPNGRLYRFEDGSESQLLLLDKERGSWTFTHADADLIPVLMQGFSAPIYYEYDYGDDELIALAQFAPDGFARYEAVQTLLHRMFQLSLKDSRALKDLSEKVSNLMAFLLKNKKISDSEKALLLAVPPLSSFLPTLPAPINMDNVLSAYDRVVRTIALKMRRNWSDFLKAGKPETQAKYSVKDAGIRALYGLAMKIMSTFDDESNRKLFLELYKNADCMTDRMNALEALNAHADRYREEALQDFYQRFADQPLVIDKWFMLQSKDNIAGALERIEALTRLPAFQIRNPNRFRALVFTFMQSNPKLFHRADGSGYHFVIEQIRRIIRDNPQLSARMIRGLEIVTKLDAKRKALAHKELSSLLEMEDISVDAREIIERVSAGLTS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000513
EMBL· GenBank· DDBJ
ABQ13323.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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