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If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01974
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 22 - 66 aligns to "C-x(2,4)-C-x(7,9)-C-x(2)-C-x(9,12)-C-x(3)-C-x(7)-H-x(3)-H" in entry Q01662
    • Subsequence at position 22 - 66 aligns to "C-x(2,4)-C-x(7,9)-C-x(2)-C-x(9,12)-C-x(3)-C-x(7)-H-x(3)-H" in entry Q01662
    • Subsequence at position 203 - 203 aligns to "H" in entry P53582 (individually applies "Substrate")
    • Subsequence at position 301 - 301 aligns to "H" in entry P53582 (individually applies "Substrate")
  • Subsequence at position 220 - 220 aligns to "D" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 231 - 231 aligns to "D" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 231 - 231 aligns to "D" in entry P53582 (applies "Divalent metal cation 2; catalytic") Subsequence at position 294 - 294 aligns to "H" in entry P53582 (applies "Divalent metal cation 2; catalytic; via tele nitrogen") Subsequence at position 327 - 327 aligns to "E" in entry P53582 (applies "Divalent metal cation 2; catalytic") Subsequence at position 358 - 358 aligns to "E" in entry P53582 (applies "Divalent metal cation 1") Subsequence at position 358 - 358 aligns to "E" in entry P53582 (applies "Divalent metal cation 2; catalytic")

... then these annotations are applied i

Subunit structurei

  • Associates with the 60S ribosomal subunit of the 80S translational complex.

Cofactori

  • Co2+, Zn2+, Mn2+, Fe2+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.

Subcellular locationi

Functioni

  • 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).

Sequence similaritiesi

Catalytic activityi

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.

Regioni

  • Zinc finger-like; important for proper ribosome association (to residues corresponding to positions 22 - 66)

Metal bindingi

  • Divalent metal cation 1 (to residues corresponding to position 220)
  • Divalent metal cation 1 (to residues corresponding to position 231)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 231)
  • Divalent metal cation 2; catalytic; via tele nitrogen (to residues corresponding to position 294)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 327)
  • Divalent metal cation 1 (to residues corresponding to position 358)
  • Divalent metal cation 2; catalytic (to residues corresponding to position 358)

Binding sitei

  • Substrate (to residues corresponding to position 203)
  • Substrate (to residues corresponding to position 301)

Keywordsi

GO (Gene Ontology) termsi