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Job DescriptionP37648
Confidence99.85%DateThu Jan 5 11:56:20 GMT 2012
Rank32Aligned Residues191
% Identity6%Templated1ppjb2
SCOP infoLuxS/MPP-like metallohydrolase LuxS/MPP-like metallohydrolase MPP-like
Resolution2.10

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


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Query Sequence  SPLRAEAVSIMTDAVRQDRLSIMWDTPWQPIRESAALLRYWRADLAREA. . . . . . . . LFWHVQQALSASNSKDIGLGFDC
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Template Sequence  KAKYHGGEIREQNGDSLVHAALVAESAAI. . GSAEANAFSVLQHVLGAGPHVKRGSNATSSLYQAVAKGVHQPFDVSAFN
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   236...240.........250.........260.... .....270.........280.........290.........300.........310...
 
   328.330.........340.........350.........360.........370.........380.........390.........400.......
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Query Sequence  RVLYLRAQCAINIESPNDKLNSNLNLVARELAKVRDKGLPEEEFNALVAQKKLELQKLFAAYARADTDILMGQRMRSLQN
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Template Sequence  ASYSDSGLFGFYTISQAASAGDVIKAAYNQVKTIAQGNLSNPDVQAAKNKLKAGYLMSV. . . . . ESSEGFLDEVGSQALA
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   314.....320.........330.........340.........350.........360.........370.. .......380........
 
   408.410.........420.........430.........440.........450.......
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Query Sequence  QVVDIAPEQYQKLRQDFLNSLTVEMLNQDLRQQLSNDMALILLQPKGEPE
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Template Sequence  AGSYTPPSTVLQQ. . . . IDAVADADVINAAKKFVSGRKSMAASGNLGHTP
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   389390.........400. ........410.........420.........430....
 
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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