Return to main results Retrieve Phyre Job Id

Job DescriptionP43340
Confidence99.97%DateThu Jan 5 12:02:20 GMT 2012
Rank18Aligned Residues173
% Identity16%Templated1t0ia_
SCOP infoFlavodoxin-like Flavoproteins NADPH-dependent FMN reductase
Resolution2.00

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


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Query Sequence  RIYLVWAHPRHDSLTAHIADAIHQRAMER. . . . . . KIQVTELDLYRRNFNPVMTPEDE. . PDWKNMDKRYSPEVHQLYSE
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Template Sequence  KVGIIMGSVRAKRVCPEIAAYVKRTIENSEELIDQKLKIQVVDLQQIALPLYEDDDELIPAQIKSVDEYADSKTRSWSRI
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Query Sequence  LLEHDTLVVVFPLWWYSFPAMLKGYIDRVWNNGLAYGDGHKLPFNKVRWVALVGGDKESFVQMGWEKNISDYLKNMCSYL
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Template Sequence  VNALDIIVFVTPQYNWGYPAALKNAIDRL. . . . . . . . . YHEWHGKPALVVSYGGHGGS. . . . . . . . . KCNDQLQEVLHGL
Template Known Secondary structure  T
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   82.......90.........100.........110 .........120.........130 .........140...
 
   157..160...... ...170.........180.........190.....
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Query Sequence  GIEDADVTFL. CNTVVFDGEELHASYYQSLLSQVRDMVDA
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Template Sequence  KMNVIGGVAVKIPVGTIPLPEDIVPQLSVHNEEILQLLAS
Template Known Secondary structure  T


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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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