A0A2H5PNV0 · A0A2H5PNV0_CITUN

Function

function

This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. Also, involved in the degradation of oxidized and glycated proteins.

Caution

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

Catalytic activity

  • Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
    EC:3.4.19.1 (UniProtKB | ENZYME | Rhea)

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 Componentcytoplasm
Molecular Functionomega peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acylamino-acid-releasing enzyme
  • EC number
  • Alternative names
    • Acyl-peptide hydrolase
    • Acylaminoacyl-peptidase

Gene names

    • ORF names
      CUMW_153590

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Miyagawa wase
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Sapindales > Rutaceae > Aurantioideae > Citrus

Accessions

  • Primary accession
    A0A2H5PNV0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain21-291Acylamino-acid-releasing enzyme N-terminal
Region175-200Disordered
Compositional bias178-197Polar residues
Domain554-770Peptidase S9 prolyl oligopeptidase catalytic

Sequence similarities

Belongs to the peptidase S9C family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    771
  • Mass (Da)
    83,723
  • Last updated
    2018-02-28 v1
  • MD5 Checksum
    C5A9AE316747D363B536DFA565914BFE
MDASKAAPAKQVSSVLDATAEEEYASLSKLLQDFTNISSIDKAWTFNSGNGNGTQAMFSISQPNLLANKRKKFMLSTVISKENENSVTFQWAPFPVEMTGASAVVPSPSGSKLLVVRNPENESPIQFELWSQSQLEKEFHVPQTVHGSVYADGWFEGISWNSDETLIAYVAEEPSPSKPTFSLGSTKGGSSDKDCNSWKGQGDWEEDWGETYAGKRQPSLFVINIDSGEVQAVKGIPKSLSVGQVVWAPLNEGSHQYLVFVGWSSETRKLGIKYCYNRPCALYAVRVSLYKSEASELELKESSSEDLPVVNLTESISSAFFPRFSPDGKFLVFLSAKSSVDSGAHSATDSLHRIDWPTNGNFSSLEKIVDVIPVVQCAEGDCFPGLYSSSILSNPWLSDGCTMLLSSIWGSSQVIISVNVSSGELLRITPAESNFSWSLLTLDGDNIIAVSSSPVDVPQVKYGYFVDKANKGTWSWLNVSSPISRCPEKVKSLLSSRQFSIMKIPVKGVSANLTKGAQKPFEAIFVSSSHKKDCSCDPLIVVLHGGPHSVSLSSYSKSLAFLSSVGYSLLIVNYRGSLGFGEEALQSLPGKVGSQDVNDVLTAIDHVIDMGLANPSKVTVVGGSHGGFLTTHLIGQAPDKFVAAAARNPLCNLALMVGTTDIPDWCYVESYGSKGKDSFTESPSVEDLTRFHSKSPISHISKVKTPTIFLLGAQDLRVPVSNGLQYARALREKGVETKVIVFPNDVHGIERPQSDFESFLNIGLWFKKYCK

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2H5PNW3A0A2H5PNW3_CITUNCUMW_153590834
A0A2H5PNX6A0A2H5PNX6_CITUNCUMW_153590826

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias178-197Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BDQV01000100
EMBL· GenBank· DDBJ
GAY54044.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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