A0A1N6LXF3 · A0A1N6LXF3_BABMR

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).

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 site199substrate
Binding site219a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site230a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site230a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site299a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site307substrate
Binding site333a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site428a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site428a 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
      BmR1_04g05525

Organism names

  • Taxonomic identifier
  • Strain
    • RI
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0A1N6LXF3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region41-65Disordered
Domain135-335Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    447
  • Mass (Da)
    50,303
  • Last updated
    2017-03-15 v1
  • Checksum
    1AAD8215AC766EAC
MGELLDAVNNTETAKNEEIINKDENDIVGELDDKLNLNKNDKTSDVVKKKNKKKKKKKSSTSETNVNAFNPVDQYIRCIKPWTYEVENSDKPVDQQFSKGKYPLGQIIPYTGTGKARMESKEKMVAEKIHEEDYEYLRRAAECHRQVRRYIQSFIRPGLTMIEIAQAVDAKTKHLISANGLDAGWGFPTGCSLNNCAAHYTPNYGDTTILQQNDVCKLDFGTQVKGNIIDCAFTIAFDEKYDPLIMATQEGTNTGLKMAGIDAYMADIAEAIQEAIESHEVEIDGTTYPVRAIRNLTGHNIGKYLIHAGKSVPIVKNSGCNERMEEGEMYAIETFASTGKGFVLEKEDCSHYMKTFDVGFVPLRLRSSKDLLKCIDENFGTLAFCRRWLDDLGQKRHLISLKNLVDNGIVTPYPPLSDIKGCYTSQMEHTILLRPTCKEVLSRGDDY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN871599
EMBL· GenBank· DDBJ
SIO73556.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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