Return to main results Retrieve Phyre Job Id

Job DescriptionP0AGE6
Confidence100.00%DateThu Jan 5 11:28:54 GMT 2012
Rank4Aligned Residues172
% Identity47%Templated1rtta_
SCOP infoFlavodoxin-like Flavoproteins NADPH-dependent FMN reductase
Resolution1.28

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


   5....10.........20.........30.........40.........50.........60.........70.........80....
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Query Sequence  LQVVTLLGSLRKGSFNGMVARTLPKIAPASMEVNALPSIADIPLYDADVQQEEGFPATVEALAEQIRQADGVVIVTPEYN
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Template Sequence  IKVLGISGSLRSGSYNSAALQEAIGLVPP. GMSIELADISGIPLYNED. VYALGFPPAVERFREQIRAADALLFATPEYN
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S

STT
TT

T.T



TT




.TT



S

T
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   7..10.........20.........30..... ....40.........50... ......60.........70.........80....
 
   85....90.........100.........110.........120.........130.........140.........150.........160....
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Query Sequence  YSVPGGLKNAIDWLSRLPDQPLAGKPVLIQTSSMGVIGGARCQYHLRQILVFLDAMVMNKPEFMGGVIQNKVDPQTGEVI
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Template Sequence  YSMAGVLKNAIDWASRPPEQPFSGKPAAILGASAGRFGTARAQYHLRQTLVFLDVHPLNKPEVMISSAQNAFDAQ. GRLL
Template Known Secondary structure  T
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SSTTTTT


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SGGGTB
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   85....90.........100.........110.........120.........130.........140.........150......... 160...
 
   165....170.........
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Query Sequence  DQGTLDHLTGQLTAF
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Template Sequence  DDKARELIQQQLQAL
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   164.....170........
 
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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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