Return to main results Retrieve Phyre Job Id

Job DescriptionP36929
Confidence97.67%DateThu Jan 5 11:53:58 GMT 2012
Rank296Aligned Residues111
% Identity14%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


   238.240.........250.........260.........270.........280.........290.. .......300......
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Query Sequence  CMTWLAPQNGEHILDLCAAPGGKTTHILEVAPEAQVVAVDIDEQRLSRVYDNLKR. . . . . . . . . . . LGMKATVKQGDGRY
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Template Sequence  VYQQCQLKKGDTFMDLGSGVGNCVVQAALECGCALSFGCEIMDDASDLTILQYEELKKRCKLYGMRLNNVEFSLKKSFVD
Template Known Secondary structure  TT

TT
S
TTS

S

TTB



SS
STT
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   383......390.........400.........410.........420.........430.........440.........450.........460..
 
   307.. 310.........320.........330.........340.........350.........360.........370.
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Query Sequence  PSQ. WCGEQQFDRILLDAPCSATGVIRRHPDIKWLRRDRDIPELAQLQSEILDAIWPHLKTGGTLV
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Template Sequence  NNRVAELIPQCDVILVNNFLFDEDLN. . . . . . . . . . . . . . . . . . . . . . . KKVEKILQTAKVGCKII
Template Known Secondary structure 
GGG
S

TT

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TT
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   463......470.........480........ .490.........500.....
 
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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