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Job DescriptionP00350
Confidence97.50%DateThu Jan 5 10:56:33 GMT 2012
Rank288Aligned Residues103
% Identity17%Templated1y81a1
SCOP infoNAD(P)-binding Rossmann-fold domains NAD(P)-binding Rossmann-fold domains CoA-binding domain
Resolution1.70

  Insertion relative to template
  Deletion relative to template
  Catalytic residue from the CSA
 
Detailed help on interpreting your alignment


   4.....10. ........20.........30.........40.........50.........60.........70.........
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Query Sequence  QQIGVVGM. . . . AVMGRNLALNIESRGYTVSIFNRSREKTEEVIAENPGKKLVPYYTVKEFVESLETPRRILLMVKAGAG
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Template Sequence  RKIALVGASKNPAKYGNIILKDLLSKGFEVLPVNPN. . . . . . . . . . . . YDEIEGLKCYRSVRELPKDVDVIVFVVP. PKV
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   7..10.........20.........30.........40.. .......50.........60.........70 ...
 
   80.........90.........100.........110.........120....
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Query Sequence  TDAAIDSLKPYLDKGDIIIDGGNTFFQDTIRRNRELSAEGFNFIG
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Template Sequence  GLQVAKEAVEA. GFKKLWFQPGAESE. . . . EIRRFLEKAGVEYSF
Template Known Secondary structure  T.T


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   74.....80.... .....90........ .100.........110...
 
Download:Text version

No model constructed - rank, confidence too low




Phyre is for academic use only

Please cite: Protein structure prediction on the web: a case study using the Phyre server
Kelley LA and Sternberg MJE. Nature Protocols 4, 363 - 371 (2009) [pdf] [Import into BibTeX]
 
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Lawrence Kelley, Benjamin Jefferys 
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