A0A0M9ERR0 · A0A0M9ERR0_FUSLA

  • Protein
    Methionine aminopeptidase 2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).

Caution

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

Catalytic activity

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    EC:3.4.11.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site194substrate
Binding site214a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site225a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site225a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site294a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site302substrate
Binding site327a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site422a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site422a divalent metal cation 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase 2
  • EC number
  • Short names
    MAP 2
    ; MetAP 2
  • Alternative names
    • Peptidase M

Gene names

    • ORF names
      FLAG1_08890

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Fl201059
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium

Accessions

  • Primary accession
    A0A0M9ERR0

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-97Disordered
Compositional bias74-88Polar residues
Domain126-336Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    441
  • Mass (Da)
    48,348
  • Last updated
    2015-12-09 v1
  • Checksum
    AC4E4916F1234E87
MAAQVPTEALKELNVADGSQKPGANAQSNTDAAGDEHGGDDSEDEADGVAPAEGAAKKKKKRKPKKKKKNPTSQSDPPRVQVSQLFPNKSYPPGEEVEYKDENTYRTTNEEKRHLDNLNADFLADYREAAEIHRQVRQWTQKNVKPGQTLTSIAEGIEDGVRALTGHSGLEEGDSLKAGMGFPCGLSLNHCAAHYTPNAGNKMVLQKEDVMKVDFGVHVNGRIVDSAFTMSFDNKYDNLLQAVKEATNAGIREAGIDARVGEIGGVIQETMESFEVEIDGTTYPVKSIRNLTGHNILPYSIHGTKAVPIVKSNDQTKMEEGDVFAIETFGSTGNGYVRDDMETSHYAKRGDSSHVDLRLSSAKSLLNVINKNFGTLPFCRRYLDRIGQDKYLLGLNNLVNAGIVEAYPPLCDKKGSYTAQFEHTILIRPTVKEVISRGDDY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias74-88Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JXCE01000296
EMBL· GenBank· DDBJ
KPA38270.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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