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Exact(7)

Multiple alignments showed that maize ZmNF-Y family proteins had conserved regions and relatively variable N-terminal or C-terminal domains.

All the sequences from each of the cluster when subjected to multiple alignments showed that the strains were fairly similar over a large region.

Multiple alignments showed that the two sequences are well conserved compared to those of the monofunctional enzymes, particularly in the regions of the active and substrate-binding sites (Fig. 2).

The multiple alignments showed diversity of the strictly conserved areas that were consistent throughout the protein sequences of all GDSL candidates, along with the less conserved regions with gaps.

The multiple alignments showed 11 different alleles for hspA (designated H1a,b,c,d; H2a,b,c,d; H3a,b,c) and six different alleles for glmM (designated G1; G2a,b; G3a,b; G4).

PSI-BLAST searches of the PDB database and the corresponding multiple alignments showed that the domain architecture of LapA and HslU is conserved, including the spacing between the Walker A and B motifs (184 and 186 residues, respectively) (data not shown).

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Similar(53)

Multiple alignments show that EHEC Int188 share the highest sequence identity with three other proteins (EPEC, H. alvei, and C. freundii) (Figure 2).

But, multiple alignments show that the fourth motif MPDM is divided into two segments.

Multiple alignments show presence of different conserved domains and motifs in CBL genes.

Domains were defined by inspection of the raw clustal files and of the graphical multiple alignments shown in Figures S1-S3.

Analysis of both the domain architecture and boundaries in the multiple alignments shows a high percentage of sequence conservation among all the AGPase SS along with their structural homologue.

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