Domain annotation: [ InterPro ]
Q94057_CAEEL Unreviewed; 102 AA. Protein T14D7.3, confirmed by transcript evidence; Caenorhabditis elegans.
Protein structure models are computational predictions which may contain errors.
The suitability of a specific model for a particular application is determined by
its accuracy (See also "Outcome of a Workshop on Applications of Protein Models
in Biomedical Research. Structure (2009) 17: 151-159.").
The sequence identity between target protein and template structure is
commonly seen as a first indicator for the expected accuracy of a model,
as confirmed by various studies.
This model is based on target-template sequence alignment of
37% sequence identity (B). Alignment errors in
non-conserved segments of the target protein, structural variation in
templates, and incorrect reconstruction of loops (insertions and deletions)
are frequent sources of model inaccuracies. Careful validation of the
model quality and variability among template structures is advised.
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Target - Template Alignment:
Identity computed with respect to: Model
Colored by: identical residues and amino acid property
id. residues .......Q....V..IM..NV.K..ER..K
MVIEW Color Scheme used: CLUSTAL
Hydrophobic amino acids
Large hydrophobic amino acids
Negatively charged amino acids
Positively charged amino acids
Polar amino acids