A0A9W5T7X0 · A0A9W5T7X0_BABOV

  • Protein
    Methionine aminopeptidase 2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • 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 site182substrate
Binding site202a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site213a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site213a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site282a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site290substrate
Binding site316a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site411a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site411a 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
      BaOVIS_002890

Organism names

  • Taxonomic identifier
  • Organism
    Babesia ovis
  • Strain
    • Selcuk
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Piroplasmida > Babesiidae > Babesia

Accessions

  • Primary accession
    A0A9W5T7X0

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-34Disordered
Domain119-327Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    47,765
  • Last updated
    2023-11-08 v1
  • Checksum
    177E7DD75FF27C13
MQPPDSQGDAAPSPSKTQKRKKKQQPKKDDTSLDDLLELEALSVVPKNPLLFDTEPGAPLRRINKWTSAIPPNKPVHEQFKGRLFPTGEVWDYSGAGAARVNDAEKRHLEKLSADKYQDLRRAAEVHRQVRRYIQSVIRPDITMIDLVNAIETKSKELIAADGLKCGWAFPTGCSLNDCAAHYTPNYGDKTVLRADDICKIDFGTQVNGHIIDCAFTLAFDEKYDELIRATQEGTNIGIKHAGIDARLCEIGEVIQETIESHEVEINGVTYPVKAIRNLTGHSIGSYHIHSGKAVPIVGNSGCTDIMEEGDLFAIETFASTGKGVVVESMECSHYMKDYDVGYVPLTLKSARDVLKSINTHFGTLAFCRRWLDDVTGSRNLLALRHLVDKGIVNPYPPLCDVRGSYTSQMEHTILLRPTCKEVLSRGEDY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BLIY01000003
EMBL· GenBank· DDBJ
GFE52885.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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