Return to main results Retrieve Phyre Job Id

Job DescriptionP04391
Confidence69.43%DateThu Jan 5 10:58:15 GMT 2012
Rank290Aligned Residues78
% Identity12%Templated1nhpa2
SCOP infoFAD/NAD(P)-binding domain FAD/NAD(P)-binding domain FAD/NAD-linked reductases, N-terminal and central domains
Resolution2.00

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


   134.....140.........150.........160.........170.........180.........190.... .....200.........
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Query Sequence  HPTQLLADLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWP. . . . EAALVTECRALAQQN
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Template Sequence  YLMRGRQWAIKLKQKTV. . DPEVNNVVVIG. . SGYIGIEAAEAFAKAGKKVTVIDILDRPLGVYLDKEFTDVLTEEMEAN
Template Known Secondary structure 


T..
TT


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STT
SSSSTTTTT

TT
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   129130.........140..... ....150...... ...160.........170.........180.........190.........200....
 
   210.....
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Query Sequence  GGNITL
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Template Conservation 

    
Template Sequence  NITIAT
Template Known Secondary structure  T
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   205....210
 
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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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