Return to main results Retrieve Phyre Job Id

Job DescriptionP23003
Confidence97.89%DateWed Jan 25 15:20:43 GMT 2012
Rank271Aligned Residues57
% Identity19%Templated1u2za_
SCOP infoS-adenosyl-L-methionine-dependent methyltransferases S-adenosyl-L-methionine-dependent methyltransferases Catalytic, N-terminal domain of histone methyltransferase Dot1l
Resolution2.20

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


   198.200.........210..... ....220.........230 .........240.........250....
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Query Sequence  QMLEWALDVTKGSKGDLL. ELYCGNGNFSLALAR. . NFDRVLATEIAKPSVAAAQYNIAA
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Template Sequence  NFLSDVYQQCQLKKGDTFMDLGSGVGNCVVQAALECGCALSFGCEIMDDASDLTILQYEE
Template Known Secondary structure  TT

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   378.380.........390.........400.........410.........420.........430.......
 
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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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