A0AA43QK86 · A0AA43QK86_9LECA

  • Protein
    Methionine aminopeptidase 2
  • Gene
    MAP2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • 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 site188substrate
Binding site208a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site219a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site219a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site288a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site296substrate
Binding site321a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site416a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site416a 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

Gene names

    • Name
      MAP2
    • ORF names
      OHK93_006521

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LIQ254RAFAR
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Lecanoromycetes > OSLEUM clade > Lecanoromycetidae > Lecanorales > Lecanorineae > Ramalinaceae > Ramalina

Accessions

  • Primary accession
    A0AA43QK86

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-84Disordered
Compositional bias8-33Polar residues
Compositional bias50-66Basic residues
Domain119-322Peptidase M24

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    426
  • Mass (Da)
    46,654
  • Last updated
    2024-01-24 v1
  • Checksum
    69633184508FBE6D
MAAQATEDVARLSQSIKNQTKTVDQSTPAINENDDSEDANEEDAGNQNASKKKKKRKPKKKKGGSKTQTSPPRVPVSNLFPNGQYPEGELCDYANDNHFRTTSEEKRHLDRSNNDFLQEYRQGAEVHRQVRQWAQGHIKPGQTLTEIAEGIEDSVRALTGHPGLEEGDNIKGGMGFPTGLSINHCAAHYTPNAGNKVVLQQDDVMKVDFGAHINGRIVDSAFTMAFNPVYDNLLAAAKDATNTGIREAGIDVRVGDIGAAIQEAMESYEVELSGQTYPVKSIKNLNGHDIIQHSIHGGKSIPIVKSSDQTKMEEGEIFAIETFGSTGKGYVRDDLETSHYAKRADAPNVALRVSSARSLLSTITKNFGTLPFCRRYLDRLGHEKYLLGLNNLVQSGIVEAYPPLCDIKGSYTAQFEHVSPVMDQAA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias8-33Polar residues
Compositional bias50-66Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPUFD010000005
EMBL· GenBank· DDBJ
MDI1487252.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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