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Job DescriptionQ9W4A9
Confidence100.00%DateWed Feb 13 11:40:50 GMT 2013
Rank3Aligned Residues191
% Identity41%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


   300.........310.........320.........330.........340.........350.........360.........370.........
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Query Sequence  GVFGTDLTTMVQLEPHHQIPFVVRRCVEEVEARGMLQEGIYRVSGFADEIEALKLALDREGEKTDMSETAYGNVNVIAGT
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Template Sequence  KVYCCDLTTLVKAHNTQ. RPMVVDICIREIEARGLKSEGLYRVSGFTEHIEDVKMAFDRDGEKADISANVYPDINIITGA
Template Known Secondary structure 

TTS
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SSTTTTS


SSSS

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   271........280....... ..290.........300.........310.........320.........330.........340.........
 
   380.........390.........400.........410.........420.........430.........440.........450.........
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Query Sequence  LKLYLRLLPVPLITFQAYPSFMAAGRTGKQAEQRQLMAEAVRRLPPAHHSCLQYMLEHLKRVASHYAVNKMNEHNLATVF
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Template Sequence  LKLYFRDLPIPVITYDTYSKFIDAAKISNADERLEAVHEVLMLLPPAHYETLRYLMIHLKKVTMNEKDNFMNAENLGIVF
Template Known Secondary structure 
SS
TT
STTTTTT


TTS
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   350.........360.........370.........380.........390.........400.........410.........420.........
 
   460......... 470.........480.........490.
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Query Sequence  APTLIATPQH. . . . . MTNLTEEIFMLSSLITHCKTIF
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Template Sequence  GPTLMRPPEDSTLTTLHDMRYQKLIVQILIENEDVLF
Template Known Secondary structure  TTTS




S
TTGGGGTT
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   430.........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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