A0A8S1D7F3 · A0A8S1D7F3_9INSE

  • Protein
    Peptidase M20 dimerisation domain-containing protein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

Caution

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

Catalytic activity

  • (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-phenylalanine = H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-phenylalanine
    This reaction proceeds in the forward
    and the backward
    directions.
  • (9Z)-octadecenoate + L-phenylalanine = H2O + N-(9Z-octadecenoyl)-L-phenylalanine
    This reaction proceeds in the forward
    and the backward
    directions.
  • (9Z)-octadecenoate + glycine = H2O + N-(9Z-octadecenoyl)glycine
    This reaction proceeds in the backward direction.
  • H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-L-phenylalanine = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + L-phenylalanine
    This reaction proceeds in the forward direction.
  • H2O + N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycine
    This reaction proceeds in the forward
    and the backward
    directions.
  • H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-L-serine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + L-serine
    This reaction proceeds in the forward
    and the backward
    directions.
  • H2O + N-(9Z-octadecenoyl)-L-asparagine = (9Z)-octadecenoate + L-asparagine
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-glutamine = (9Z)-octadecenoate + L-glutamine
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-leucine = (9Z)-octadecenoate + L-leucine
    This reaction proceeds in the forward
    and the backward
    directions.
  • H2O + N-(9Z-octadecenoyl)-L-lysine = (9Z)-octadecenoate + L-lysine
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-methionine = (9Z)-octadecenoate + L-methionine
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-serine = (9Z)-octadecenoate + L-serine
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-tryptophan = (9Z)-octadecenoate + L-tryptophan
    This reaction proceeds in the forward direction.
  • H2O + N-(9Z-octadecenoyl)-L-tyrosine = (9Z)-octadecenoate + L-tyrosine
    This reaction proceeds in the forward direction.
  • H2O + N-hexadecanoyl-L-phenylalanine = hexadecanoate + L-phenylalanine
    This reaction proceeds in the forward direction.
  • H2O + N-octadecanoyl-L-phenylalanine = L-phenylalanine + octadecanoate
    This reaction proceeds in the forward direction.
  • an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
    This reaction proceeds in the forward
    and the backward
    directions.
    EC:3.5.1.14 (UniProtKB | ENZYME | Rhea)
  • an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate + an aromatic L-alpha-amino acid
    This reaction proceeds in the forward
    and the backward
    directions.
    EC:3.5.1.114 (UniProtKB | ENZYME | Rhea)

Pathway

Lipid metabolism; fatty acid metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site148Zn2+ 2 (UniProtKB | ChEBI)
Active site150
Binding site181Zn2+ 2 (UniProtKB | ChEBI)
Binding site181Zn2+ 1 (UniProtKB | ChEBI)
Active site215Proton acceptor
Binding site216Zn2+ 1 (UniProtKB | ChEBI)
Binding site243Zn2+ 2 (UniProtKB | ChEBI)
Binding site489Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
Molecular Functionmetal ion binding
Molecular Functionmetallocarboxypeptidase activity
Biological Processamide biosynthetic process
Biological Processamide catabolic process
Biological Processamino acid metabolic process
Biological Processcellular lipid metabolic process
Biological Processproteolysis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Peptidase M20 dimerisation domain-containing protein

Gene names

    • ORF names
      CLODIP_2_CD03073

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Palaeoptera > Ephemeroptera > Pisciforma > Baetidae > Cloeon

Accessions

  • Primary accession
    A0A8S1D7F3

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain266-401Peptidase M20 dimerisation

Sequence similarities

Belongs to the peptidase M20A family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    532
  • Mass (Da)
    60,131
  • Last updated
    2022-10-12 v1
  • Checksum
    B3DC6AC54A2CA2E3
MVQSKSPKWQLRWRCGRWWWKVFKLLLKIPLVIGLLLSVVVLYRAFTASTPASTLDILNNAQTAGVDDGLKMERAHRLAGALRISTISYEPGKQETGELLKLHRYLEKEFPAVHNCSFVKREIINVYSLLYTVTGTSPDKLPYMLASHLDVVPADPEHWEVDPFSGKIVNNTYIYGRGTIDDKGGVLGILEALEYLIKKGERPQRSFFIAFGHDEEVSGKQGAQEIARVLLKRGVDRLDFVLDEGYTVTRYIFPGTRKHVALVGVSEKGYLTLELSVNGSPGHSSFPPWESAIGILSEAITKLEKNKLPSMFGTGPERSTFEYLAPHVGFLHRLLYSNMWLFSGFMARIMEKEALSNAYVRTTSAITVFHGGIKENVVPAHAKATINHRVHPSQTISEVIEFDKRTIDDPRVEIKVKASKEAHTVSPYGPDDVQFNLIARSIYQTFDDVVVIPGVLIANTDTRWYLGLSSHLYRFFPTVIYPQDTNRYHGIDERISIDNYQQAVSFYYRVMKNADLIIGHVASTTAHQQREL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CADEPI010000158
EMBL· GenBank· DDBJ
CAB3378126.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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