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Job DescriptionP0ACC9
Confidence99.83%DateThu Jan 5 11:17:55 GMT 2012
Rank30Aligned Residues99
% Identity25%Templatec2v0hA_
PDB info PDB header:transferaseChain: A: PDB Molecule:bifunctional protein glmu; PDBTitle: characterization of substrate binding and catalysis of the2 potential antibacterial target n-acetylglucosamine-1-3 phosphate uridyltransferase (glmu)
Resolution1.79 Å

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


   60.........70.........80.........90.........100.........110.........120.........130.........
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Query Sequence  IQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITLGNNVTVGAGS
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Template Sequence  EIKKSTVGKGSKVNHLTYV. . . GDSEIGSNCNIGAGVITCNYDGANKFKTIIGDDVFVGSDTQLVAPVKVANGATIGAGT
Template Known Secondary structure  S

TT
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SS

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   349350.........360....... ..370.........380.........390.........400.........410.........420.....
 
   140.........150.........160.
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Query Sequence  VVLDSVPDNALVVGEKARVKVI
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Template Sequence  TITRDVGENELVITRVAQRHIQ
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T
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   426...430.........440.......
 
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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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