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Job DescriptionA1A4S6
Confidence99.98%DateWed May 9 18:01:49 BST 2012
Rank8Aligned Residues193
% Identity34%Templated1xa6a1
SCOP infoGTPase activation domain, GAP GTPase activation domain, GAP BCR-homology GTPase activation domain (BH-domain)
Resolution3.20

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


   380.........390.........400.........410.........420.........430.........440.........450.........
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Query Sequence  AIIPRPEGNAQLDKMGFTIIRKCISAVETRGINDQGLYRVVGVSSKVQRLLSMLMDVKTCNEVDLENSADWEVKTITSAL
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Template Sequence  YCCDLTTLVKAHNTQRPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKAD. . ISANVYPDINIITGAL
Template Known Secondary structure  TTS
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   273......280.........290.........300.........310.........320.........330.... .....340.........350
 
   460.........470.........480.........490.........500.........510.........520.........530.........
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Query Sequence  KQYLRSLPEPLMTYELHGDFIVPAKSGSPESRVNAIHFLVHKLPEKNKEMLDILVKHLTNVSNHSKQNLMTVANLGVVFG
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Template Sequence  KLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVFG
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   351........360.........370.........380.........390.........400.........410.........420.........430
 
   540.........550. ........560.........570....
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Query Sequence  PTLMRPQEETVA. ALMDLKFQNIVVEILIENHEKIF
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Template Sequence  PTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF
Template Known Secondary structure  TTS




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TTGGGGTT
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   431........440.........450.........460......
 
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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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