R4WJM5 · R4WJM5_RIPPE

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 site95substrate
Binding site115a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site126a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site126a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site195a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site203substrate
Binding site228a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site323a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site323a 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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Pentatomomorpha > Coreoidea > Alydidae > Riptortus

Accessions

  • Primary accession
    R4WJM5

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain33-238Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    342
  • Mass (Da)
    38,601
  • Last updated
    2013-07-24 v1
  • Checksum
    10BC4D60306DF542
MLYPGDERKAKDRFSNEEMRALDRLHNDIYNEARQAAEAHRQTRKYIQKWVKPGITMIELCEELEKTARTLIKEEGLKAGLAFPTGCSRNHCAAHYTPNAGDTTVLMYDDVTKIDFGTHINGRIIDCAWTLTFNPKYDKLIEAVREATNTGIKEAGIDVPLCEIGAAIQEVMESYEVEIDGKTYPVKSIRNLNGHSIAPYRIHAGKTVPIVKGGEATVMEENEFYAIETFGSTGRGIVHDDMDVSHYMKNFDAGFIPLRIQSSKQLLNVINNNFGTLAFCKRWLDRLGQTRYQMALKDLCDKGVVEAYPPLCDVKGCYTAQFEHTIVLRPTCKEVISKGDDY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK417770
EMBL· GenBank· DDBJ
BAN20985.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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