Return to main results Retrieve Phyre Job Id

Job DescriptionP28638
Confidence96.85%DateThu Jan 5 11:45:07 GMT 2012
Rank125Aligned Residues61
% Identity20%Templated1nw3a_
SCOP infoS-adenosyl-L-methionine-dependent methyltransferases S-adenosyl-L-methionine-dependent methyltransferases Catalytic, N-terminal domain of histone methyltransferase Dot1l
Resolution2.50

  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  QKPEALLKRIILAS. SNPGDIVLDPFAGSFTTGA. VAIASGRK. FIGIEINSEYIKMGLRRLDV
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Template Sequence  ETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDRE
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   138.140.........150.........160.........170.........180.........190.........200.
 
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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