A0A1E3H9U5 · A0A1E3H9U5_9TREE

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 site187substrate
Binding site207a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site218a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site218a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site287a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site295substrate
Binding site330a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site427a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site427a divalent metal cation 1 (UniProtKB | ChEBI)

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
      L202_08331

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 6039
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus

Accessions

  • Primary accession
    A0A1E3H9U5

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-75Disordered
Compositional bias9-25Basic and acidic residues
Compositional bias26-43Acidic residues
Domain124-331Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    446
  • Mass (Da)
    49,154
  • Last updated
    2017-01-18 v1
  • Checksum
    5EBAB34F59094408
MSAELPKVESLKLSEEGKKEEKEPEVVEGEENDDDDDEGENDDGPANGESKKKKKKKKSKKKKTAAATQSEPPRVGLTKIYKNGIFPVGEEVEYKDDNTYRTSSAECRERERLAQGDPSTQYANIRRAGEVHRQVRAYAQKTIKPGMTMTEIANLVEDGTRAVVEENGFESGIGFPTGLSVNEVAAHYTPNPGDKQVLGDKDVMKVDFGVHVNGRIVDSAFTMNFEPTWDRLLEAVKDATNAGISAAGIDVRMCDIGEAVQEVMESYEVEVNGKVYPVKSISNLNGHSITPYTIHGGVGTRPGKSVPIVKQHGSARDEAKMEEGEYFAIETFGSTGRGRVIEQGACSHYALNASAPERYQGHQQSAKSLLASVRRNFGTLPFCRRYLDHVGEKNYLLALNTLVREDFISDYPPLVDPEPGAMTAQFEHTILLRPTCKEVVSRGDDY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-25Basic and acidic residues
Compositional bias26-43Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AWGJ01000014
EMBL· GenBank· DDBJ
ODN72915.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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