Figure 3

Partial multiple alignment of aminopeptidase O, rat aminopeptidase B and Actinobacteria aminopeptidase sequences. Sequences were aligned with ClustalW using the Blosum62 matrix. Multiple alignment of the central Zn²⁺ chelating region of Ap-O from Rattus norvegicus (RnAp-O; AMPO_RAT), Mus musculus (MmAp-O; AMPO_MOUSE), Homo sapiens (HsAp-O; Q5T9B3), Gallus gallus (GgAp-O; XP_425041.1) and aminopeptidases from Actinobacteria [Streptomyces avermitilis (Q82MI5, Q82JJ1, Q82P16, Q82GE5, Q82KD2, Q93H20, Q82FV0); Streptomyces coelicolor (Q9X7P2, Q9KXW8, O69971); Kitasatospora setae (Q6L8I5); Nocardia farcinica (Q5Z264, Q5Z2X1); Corynebacterium efficiens (Q8FSN0); Corynebacterium glutamicum (Q8NTG8); Corynebacterium diphtheriae (Q6NJN5)] is shown. The corresponding part of the Rattus norvegicus Ap-B sequence (RnAp-B; AMPB_RAT) is indicated, as well as the conserved amino acid residues between Ap-B and Ap-O (above RnAp-B sequence) and between Actinobacteria aminopeptidase sequences (below RnAp-B sequence). Conserved amino acid residues between Ap-O proteins or between Actinobacteria proteins are shown above (Ap-O line) and below (Actino line) the multiple alignment, respectively. In the consensus lines, amino acids invariant in all sequences are indicated by stars (H) and colons (:) indicate similar residues according to the following rule: T:A:S; I:L:V:M; K:R:H; D:E:Q:N; F:Y; G; P; W; C. The location of the GXMEN motif is boxed and the conserved amino acid residues are highlighted in the corresponding Ap-O and Actinobacteria sequences. The HEXXHX₁₈E motif is also highlighted. Dashes typify gaps.