D8PR70 · MAP2_SCHCM

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

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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site176substrate
Binding site196a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site207a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site207a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site276a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site284substrate
Binding site309a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site404a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site404a 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
      SCHCODRAFT_64644

Organism names

Accessions

  • Primary accession
    D8PR70

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004076671-423Methionine aminopeptidase 2

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-20Basic and acidic residues
Region1-89Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    423
  • Mass (Da)
    46,783
  • Last updated
    2010-10-05 v1
  • Checksum
    3680863E582C4A34
MTDVIDAKPEEAKKVPPEVEDEDSGDESAPEASAAGGEATKKKKKKKKPKKKKKAAEQSEPPRVGLSKLFPNGIYPEGEIQPYKDDNAYRTTSEEKRYLERITCEDPDETYQNIRKGAEVHRQVRQYAQRTIKPGMTMTEIANLIEDGTRALVEENGLEAGIGFPTGLSLNNCAAHYTPNAGDTIVLQQGDVMKVDIGVQVKGRIVDSAFTMTFEPTYDKLLEAVRAATNTGIREAGIDARLGEIAGAIQETMESYEVEVNGKLIPVKPIANLSGHSIDRYTIHAGKSVCLVKNDDQTKMEEGEYFAIETFGSTGRGRVVDGGECSHYARKVDAPHVPLRLTTAKSLLKSINKNFGTIPFCRRYLDRIGESKYLLALNHLVQQGIVEDYPPLYDQQGSMTAQFEHTILLRPTVKEVVSRGDDY

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-20Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GL377302
EMBL· GenBank· DDBJ
EFJ03808.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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