WORKLIST ENTRIES (1):

XHISDIPTASE View alignment      X-His dipeptidase (M25) signature
 Type of fingerprint: COMPOUND with 9  elements
Links:
   PRINTS; PR00756 ALADIPTASE; PR00791 PEPDIPTASEA; PR00730 THERMOLYSIN
   PRINTS; PR00787 NEUTRALPTASE; PR00782 LSHMANOLYSIN; PR00931 MICOLLPTASE
   PRINTS; PR00997 FRAGILYSIN; PR00786 NEPRILYSIN; PR00765 CRBOXYPTASEA
   PRINTS; PR00932 AMINO1PTASE; PR00789 OSIALOPTASE; PR00933 BLYTICPTASE
   PRINTS; PR00919 THERMOPTASE; PR00998 CRBOXYPTASET; PR00768 DEUTEROLYSIN 
   PRINTS; PR00999 FUNGALYSIN; PR01000 SREBPS2PTASE
   INTERPRO; IPR001160

 Creation date 09-SEP-1998; UPDATE 07-JUN-1999

   1. RAWLINGS, N.D. AND BARRETT, A.J.
   Evolutionary families of metallopeptidases.
   METHODS ENZYMOL. 248 183-228 (1995).

   2. RAWLINGS, N.D. AND BARRETT, A.J.
   MEROPS - Peptidase Database
   http://www.bi.bbsrc.ac.uk/merops/merops.htm

   3. RAWLINGS, N.D. AND BARRETT, A.J.
   Family M25 - Clan MH - X-His dipeptidase
   http://www.bi.bbsrc.ac.uk/merops/famcards/m25.htm

   4. HENRICH B., MONNERJAHN U., PLAPP R.
   Peptidase D gene (pepD) of Escherichia coli K-12: nucleotide sequence,
   transcript mapping, and comparison with othe peptidase genes. 
   J.BACTERIOL. 172 4641-4651 (1990). 

   Metalloproteases are the most diverse of the four main types of protease,
   with more than 30 families identified to date [1]. Of these, around
   half contain the HEXXH motif, which has been shown in crystallographic
   studies to form part of the metal-binding site [1]. The HEXXH motif is 
   relatively common, but can be more stringently defined for metallo-
   proteases as abXHEbbHbc, where a is most often valine or threonine and 
   forms part of the S1' subsite in thermolysin and neprilysin, b is an
   uncharged residue, and c a hydrophobic residue. Proline is never found
   in this site, possibly because it would break the helical structure 
   adopted by this motif in metalloproteases [1].
   
   Metalloproteases can be split into five groups on the basis of their metal-
   binding residues: the first three contain the HEXXH motif, the other two
   do not [1]. In the first group, a glutamic acid completes the active site -
   these are termed HEXXH+E: all families in this group show some sequence
   relationship and have been assigned to clan MA [1]. The second group, which
   have a third histidine as the extra metal-binding residue, are termed
   HEXXH+H and are grouped into clan MB on the basis of their inter-relation-
   ship[1]. In the third group, the additional metal-binding residues are
   unidentified. The fourth group is diverse - the metal-binding residues are
   known but do not form the HEXXH motif. And the fifth group comprises the
   remaining families where the metal-binding residues are as yet unknown [1,2].
  
   X-His dipeptidases are zinc-containing metallopeptidases that belong to the
   M25 protease family, which forms part of the MH clan [1,3]. These cyto-
   plasmic endopeptidases cleave Xaa+His dipeptides (where Xaa is any hydro-
   phobic residue). The zinc ligands of the MH clan are His/Asp, Asp, Glu,
   Asp/Glu and His [1,2].
  
   The amino acid sequence deduced from E.coli reveals that peptidase D is a
   slightly hydrophilic protein of 485 residues that contains no extended 
   domains of marked hydrophobicity [4]. 
  
   XHISDIPTASE is a 9-element fingerprint that provides a signature for X-His
   metallodipeptidases (M25). The fingerprint was derived from an initial 
   alignment of 3 sequences: the motifs were drawn from conserved regions
   spanning virtually the full alignment length. A single iteration on OWL30.2
   was required to reach convergence, no further sequences being identified
   beyond the starting set.
  
   An update on SPTR37_9f identified a true set of 3 sequences.

  SUMMARY INFORMATION
      3 codes involving  9 elements
      0 codes involving  8 elements
      0 codes involving  7 elements
      0 codes involving  6 elements
      0 codes involving  5 elements
      0 codes involving  4 elements
      0 codes involving  3 elements
      0 codes involving  2 elements

   COMPOSITE FINGERPRINT INDEX
  
    9|   3    3    3    3    3    3    3    3    3  
    8|   0    0    0    0    0    0    0    0    0  
    7|   0    0    0    0    0    0    0    0    0  
    6|   0    0    0    0    0    0    0    0    0  
    5|   0    0    0    0    0    0    0    0    0  
    4|   0    0    0    0    0    0    0    0    0  
    3|   0    0    0    0    0    0    0    0    0  
    2|   0    0    0    0    0    0    0    0    0  
   --+----------------------------------------------
     |   1    2    3    4    5    6    7    8    9  

True positives..
 PEPD_ECOLI     PEPD_HAEIN     O51553         


  PROTEIN TITLES
   PEPD_ECOLI       AMINOACYL-HISTIDINE DIPEPTIDASE (EC 3.4.13.3) (XAA-HIS DIPEP
   PEPD_HAEIN       AMINOACYL-HISTIDINE DIPEPTIDASE (EC 3.4.13.3) (XAA-HIS DIPEP
   O51553           AMINOACYL-HISTIDINE DIPEPTIDASE (PEPD) - BORRELIA BURGDORFER

SCAN HISTORY OWL30_2 2 50 NSINGLE SPTR37_9f 2 4 NSINGLE INITIAL MOTIF SETS XHISDIPTASE1 Length of motif = 20 Motif number = 1 X-His metallodipeptidase motif I - 1 PCODE ST INT VPQKNNDTVHDFTKDPIQPY PEPD_ECOLI 79 79 VPQANEGNPHDFTKDPIQPY PEPD_HAEIN 79 79 VCEKNESSLHNFETDPIEIV G70175 71 71 XHISDIPTASE2 Length of motif = 19 Motif number = 2 X-His metallodipeptidase motif II - 1 PCODE ST INT DGEWVKARGTTLGADNGIG PEPD_ECOLI 100 1 DGEWVKARGTTLGSDNGIG PEPD_HAEIN 100 1 EDGYLKAVGTTLGADNGIG G70175 92 1 XHISDIPTASE3 Length of motif = 18 Motif number = 3 X-His metallodipeptidase motif III - 1 PCODE ST INT GPLEVLLTMTEEAGMDGA PEPD_ECOLI 134 15 PPLEVLLTMTEETGMDGA PEPD_HAEIN 134 15 PDLELLFTVDEEIGLIGA G70175 127 16 XHISDIPTASE4 Length of motif = 19 Motif number = 4 X-His metallodipeptidase motif IV - 1 PCODE ST INT WLQADILINTDSEEEGEIY PEPD_ECOLI 158 6 WLQSEILINTDTEEIGEIY PEPD_HAEIN 158 6 LCSGKSLINLDGEEEGYFL G70175 151 6 XHISDIPTASE5 Length of motif = 18 Motif number = 5 X-His metallodipeptidase motif V - 1 PCODE ST INT LTLKGLKGGHSGGEIHVG PEPD_ECOLI 205 28 ITLKGLRGGHSGGDIHTG PEPD_HAEIN 204 27 ILFKGLKGGHSGADIHLD G70175 197 27 XHISDIPTASE6 Length of motif = 20 Motif number = 6 X-His metallodipeptidase motif VI - 1 PCODE ST INT GGTLRNAIPREAFATIAVAA PEPD_ECOLI 250 27 GGSIRNAIPREAAAVLAFNG PEPD_HAEIN 250 28 GGNSSNAIPIEAKALIFIDD G70175 242 27 XHISDIPTASE7 Length of motif = 19 Motif number = 7 X-His metallodipeptidase motif VII - 1 PCODE ST INT LIRSLIDSGKDYVVSMLDS PEPD_ECOLI 362 92 LVRSLIESGKYYVTEMLSS PEPD_HAEIN 361 91 LIRSLLDLDKEYVCNHLQS G70175 354 92 XHISDIPTASE8 Length of motif = 17 Motif number = 8 X-His metallodipeptidase motif VIII - 1 PCODE ST INT IHAGLECGLFKKPYPEM PEPD_ECOLI 427 46 IHAGLECGLLKEHYPNI PEPD_HAEIN 426 46 IHAGLETGIISSRLGGI G70175 419 46 XHISDIPTASE9 Length of motif = 23 Motif number = 9 X-His metallodipeptidase motif IX - 1 PCODE ST INT GPTITGPHSPDEQVHIESVGHYW PEPD_ECOLI 449 5 GPTIRNAHSPDEKVEIATVQTYW PEPD_HAEIN 448 5 GPWIEWPHTTRERVNISSTIRVY G70175 441 5 FINAL MOTIF SETS XHISDIPTASE1 Length of motif = 20 Motif number = 1 X-His metallodipeptidase motif I - 2 PCODE ST INT VPQKNNDTVHDFTKDPIQPY PEPD_ECOLI 79 79 VPQANEGNPHDFTKDPIQPY PEPD_HAEIN 79 79 VCEKNESSLHNFETDPIEIV O51553 71 71 XHISDIPTASE2 Length of motif = 19 Motif number = 2 X-His metallodipeptidase motif II - 2 PCODE ST INT DGEWVKARGTTLGADNGIG PEPD_ECOLI 100 1 DGEWVKARGTTLGSDNGIG PEPD_HAEIN 100 1 EDGYLKAVGTTLGADNGIG O51553 92 1 XHISDIPTASE3 Length of motif = 18 Motif number = 3 X-His metallodipeptidase motif III - 2 PCODE ST INT GPLEVLLTMTEEAGMDGA PEPD_ECOLI 134 15 PPLEVLLTMTEETGMDGA PEPD_HAEIN 134 15 PDLELLFTVDEEIGLIGA O51553 127 16 XHISDIPTASE4 Length of motif = 19 Motif number = 4 X-His metallodipeptidase motif IV - 2 PCODE ST INT WLQADILINTDSEEEGEIY PEPD_ECOLI 158 6 WLQSEILINTDTEEIGEIY PEPD_HAEIN 158 6 LCSGKSLINLDGEEEGYFL O51553 151 6 XHISDIPTASE5 Length of motif = 18 Motif number = 5 X-His metallodipeptidase motif V - 2 PCODE ST INT LTLKGLKGGHSGGEIHVG PEPD_ECOLI 205 28 ITLKGLRGGHSGGDIHTG PEPD_HAEIN 204 27 ILFKGLKGGHSGADIHLD O51553 197 27 XHISDIPTASE6 Length of motif = 20 Motif number = 6 X-His metallodipeptidase motif VI - 2 PCODE ST INT GGTLRNAIPREAFATIAVAA PEPD_ECOLI 250 27 GGSIRNAIPREAAAVLAFNG PEPD_HAEIN 250 28 GGNSSNAIPIEAKALIFIDD O51553 242 27 XHISDIPTASE7 Length of motif = 19 Motif number = 7 X-His metallodipeptidase motif VII - 2 PCODE ST INT LIRSLIDSGKDYVVSMLDS PEPD_ECOLI 362 92 LVRSLIESGKYYVTEMLSS PEPD_HAEIN 361 91 LIRSLLDLDKEYVCNHLQS O51553 354 92 XHISDIPTASE8 Length of motif = 17 Motif number = 8 X-His metallodipeptidase motif VIII - 2 PCODE ST INT IHAGLECGLFKKPYPEM PEPD_ECOLI 427 46 IHAGLECGLLKEHYPNI PEPD_HAEIN 426 46 IHAGLETGIISSRLGGI O51553 419 46 XHISDIPTASE9 Length of motif = 23 Motif number = 9 X-His metallodipeptidase motif IX - 2 PCODE ST INT GPTITGPHSPDEQVHIESVGHYW PEPD_ECOLI 449 5 GPTIRNAHSPDEKVEIATVQTYW PEPD_HAEIN 448 5 GPWIEWPHTTRERVNISSTIRVY O51553 441 5

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