A0A481SAY5 · A0A481SAY5_9CILI

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 site93substrate
Binding site113a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site124a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site124a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site193a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site201substrate
Binding site226a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site321a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site321a 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

Protein family/group 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 > Sar > Alveolata > Ciliophora > Intramacronucleata > Oligohymenophorea > Scuticociliatia > Philasterida > Philasteridae > Philasterides

Accessions

  • Primary accession
    A0A481SAY5

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain30-236Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    340
  • Mass (Da)
    38,427
  • Last updated
    2019-06-05 v1
  • Checksum
    D627B2C5B184CCE1
MEYTKKECSFRTTDAELREKDKLSEEQLNNMRKAAECHRQVRKRCQQIIRPGKRLIDVCEEIEELNRYLVTENGLQAGIAFPTGCSLNHVAAHYTPNPGDFTTIQYDDVCKIDFGTQVEGRIIDCAFTVAFNPKYDKLLEAVKEATWNGIRSAGIDVRLCDIGADIQEVMESYEVTLDGKTYPVKSVRNLNGHSIDPYKIHAGKSVPIVGGGTQEKMEEGEQYAIETFGSTGKGFVVEDMDCSHYMKDFEVGKVPLRSQRARTLLNHINKNFGTLAFCRRWLDRGDQIGHIIGLKELCNQGIVNAYPPLCDQTGCYVAQYEHTLYLNASHKEILSFGDDY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH444708
EMBL· GenBank· DDBJ
QBH22555.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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