WORKLIST ENTRIES (1):

MTECHINOIDEA View alignment View Structure    Echinoidea (sea urchin) metallothionein signature
 Type of fingerprint: COMPOUND with 4  elements
Links:
   PRINTS; PR00858 MTCRUSTACEAN; PR00859 MTPROKARYOTE; PR00860 MTVERTEBRATE
   PRINTS; PR00872 MTDIPTERA; PR00874 MTFUNGIIV; PR00875 MTMOLLUSC
   PRINTS; PR00876 MTNEMATODE; PR00877 MTPLANTPEC
   INTERPRO; IPR001396
   PROTOMAP; P04734
   PFAM; PF00131 metalthio

 Creation date 26-JUN-1998; UPDATE 27-JUN-1999

   1. KAGI, J.H.R.
   Overview of Metallothioneins.
   METHODS ENZYMOL. 205 613-626 (1991).

   2. KAGI, J.H.R. AND KOJIMA, Y.
   Chemistry and biochemistry of metallothionein.
   EXPERIENTIA SUPPL. 52 25-61 (1987).

   3. KAGI, J.H.R. AND SCHAFFER, A.
   Biochemistry of metallothionein.
   BIOCHEMISTRY 27 8509-8515 (1988).

   4. FOWLER, B.A., HILDEBRAND, C.E., KOJIMA, Y. AND WEBB, M.
   Nomenclature of metallothionein.
   EXPERIENTIA SUPPL. 52 21 (1987).

   5. KOJIMA, Y.
   Definitions and nomenclature of metallothioneins.
   METHODS ENZYMOL. 205 8-10 (1991).

   6. BINZ, P.-A. AND KAGI, J.H.R.
   Molecular evolution of the metallothionein. Suggestions for a natural 
   classification system.
   IN FOURTH INTERNATIONAL MEETING ON METALLOTHIONEIN, KANSAS CITY (USA), 1997.

   Metallothioneins (MT) are small proteins that bind heavy metals, such as
   zinc, copper, cadmium, nickel, etc.. They have a high content of cysteine
   residues that bind the metal ions through clusters of thiolate bonds [1-3]
   (http://www.unizh.ch/~mtpage/MT.html). An empirical classification into
   three classes has been proposed by Fowler et al. [4] and Kojima [5]. Members
   of class I are defined to include polypeptides related in the positions of
   their cysteines to equine MT-1B, and include mammalian MTs as well as MTs 
   from crustaceans and molluscs. Class II groups MTs from a variety of 
   species, including sea urchins, fungi, insects and cyanobacteria. Class
   III MTs are atypical polypeptides composed of gamma-glutamylcysteinyl
   units [4]. 
  
   This original classification system has been found to be limited, in the
   sense that it does not allow clear differentiation of patterns of structural
   similarities, either between or within classes. Consequently, all class I
   and class II MTs (the proteinaceous sequences) have now been grouped into
   families of phylogenetically-related and thus alignable sequences [6]
   (http://www.unizh.ch/~mtpage/classif.html). This system subdivides the MT
   superfamily into families, subfamilies, subgroups, and isolated isoforms
   and alleles. 
  
   The metallothionein superfamily comprises all polypeptides that resemble
   equine renal metallothionein in several respects [4]: e.g., low molecular
   weight; high metal content; amino acid composition with high Cys and low
   aromatic residue content; unique sequence with characteristic distribution
   of cysteines, and spectroscopic manifestations indicative of metal thiolate
   clusters. A MT family subsumes MTs that share particular sequence-specific 
   features and are thought to be evolutionarily related. The inclusion of a
   MT within a family presupposes that its amino acid sequence is alignable 
   with that of all members. Fifteen MT families have been characterised, each
   family being identified by its number and its taxonomic range: e.g., Family
   1: vertebrate MTs.
  
   Echinoidea (Sea urchin, family 4) MTs are 64-67 residue proteins, in which
   20 conserved cysteines bind divalent metal ions. The protein is arranged
   into two domains, the N-terminal domain containing 9 Cys residues and the
   C-terminal domain having 11 cysteines. In particular, the consensus pattern 
   P-D-x-K-C-V-C-C-x(5)-C-x-C-x(4)-C-C-x(4)-C-C-x(4,6)-C-C has been found to
   be diagnostic of family 4 MTs. The protein is induced by and binds various
   heavy metal ions.
  
   MTECHINOIDEA is a 4-element fingerprint that provides a signature for
   echinoidea (sea urchin, family 4) metallothioneins. The fingerprint was
   derived from an initial alignment of 6 sequences: motif 1 contains 5 metal-
   binding Cys residues; motifs 2 and 3 each include 4 cysteines; and motif 4
   contains 6 Cys residues. Motifs 1 to 3 fully span the characteristic
   consensus pattern. Two iterations on OWL30.1 were required to reach
   convergence, at which point a true set comprising 7 sequences was 
   identified.
  
   An update on SPTR37_9f identified a true set of 5 sequences.

  SUMMARY INFORMATION
      5 codes involving  4 elements
      0 codes involving  3 elements
      0 codes involving  2 elements

   COMPOSITE FINGERPRINT INDEX
  
    4|   5    5    5    5  
    3|   0    0    0    0  
    2|   0    0    0    0  
   --+---------------------
     |   1    2    3    4  

True positives..
 MT_STENE       MTA_STRPU      MTB_STRPU      O02033         
 MT_PARLI       


  PROTEIN TITLES
   MT_STENE         METALLOTHIONEIN (MT) - STERECHINUS NEUMAYERI (ANTARTIC SEA U
   MTA_STRPU        METALLOTHIONEIN-A (MTA) - STRONGYLOCENTROTUS PURPURATUS (PUR
   MTB_STRPU        METALLOTHIONEIN-B (MTB) - STRONGYLOCENTROTUS PURPURATUS (PUR
   O02033           METALLOTHIONEIN - LYTECHINUS PICTUS (PAINTED SEA URCHIN).
   MT_PARLI         METALLOTHIONEIN (MT) - PARACENTROTUS LIVIDUS (COMMON SEA URC

SCAN HISTORY OWL30_1 2 100 NSINGLE SPTR37_9f 2 50 NSINGLE INITIAL MOTIF SETS MTECHINOIDEA1 Length of motif = 16 Motif number = 1 Sea-urchin metallothionein motif I - 1 PCODE ST INT PDTKCVCCQDGKQCPC MT_PARLI 1 1 PDVKCVCCKEGKECAC MTA_STRPU 2 2 PDVKCVCCKEGNECAC MTB_STRPU 2 2 PDVKCVCCQDGKECPC MTA_SPHGR 3 3 PDVKCVCCQDGEECPC MTB_SPHGR 3 3 PDVKCVCCKEGKECAC MT_STENE 2 2 MTECHINOIDEA2 Length of motif = 14 Motif number = 2 Sea-urchin metallothionein motif II - 1 PCODE ST INT GQECCITGKCCKDG MT_PARLI 18 1 GQDCCKTGECCKDG MTA_STRPU 19 1 GQDCCTIGKCCKDG MTB_STRPU 19 1 GGECCITGSCCKEG MTA_SPHGR 20 1 GGECCITGTCCKEG MTB_SPHGR 20 1 GKECCTTGECCKDG MT_STENE 19 1 MTECHINOIDEA3 Length of motif = 11 Motif number = 3 Sea-urchin metallothionein motif III - 1 PCODE ST INT CCGTCSNAACK MT_PARLI 35 3 CCGICTNAACK MTA_STRPU 34 1 CCGKCSNAACK MTB_STRPU 34 1 CCGKCSNAACK MTA_SPHGR 37 3 CCGKCSNAACK MTB_SPHGR 37 3 CCGKCTNAACK MT_STENE 34 1 MTECHINOIDEA4 Length of motif = 19 Motif number = 4 Sea-urchin metallothionein motif IV - 1 PCODE ST INT CTGGCKCEGGCVCTEGNCT MT_PARLI 46 0 CANGCKCGSGCSCTEGNCA MTA_STRPU 45 0 CADGCTCGSGCSCTEGNCP MTB_STRPU 46 1 CADGCKCGSGCSCTLGNCT MTA_SPHGR 48 0 CADGCKCGSGCSCTLGNCT MTB_SPHGR 48 0 CADGCKCGSGCSCTEGNCA MT_STENE 45 0 FINAL MOTIF SETS MTECHINOIDEA1 Length of motif = 16 Motif number = 1 Sea-urchin metallothionein motif I - 2 PCODE ST INT PDVKCVCCKEGKECAC MT_STENE 2 2 PDVKCVCCKEGKECAC MTA_STRPU 2 2 PDVKCVCCKEGNECAC MTB_STRPU 2 2 PDVKCFCCRDGKECAC O02033 4 4 PDTKCVCCQDGKQCPC MT_PARLI 1 1 MTECHINOIDEA2 Length of motif = 14 Motif number = 2 Sea-urchin metallothionein motif II - 2 PCODE ST INT GKECCTTGECCKDG MT_STENE 19 1 GQDCCKTGECCKDG MTA_STRPU 19 1 GQDCCTIGKCCKDG MTB_STRPU 19 1 GGECCITGKCCKEG O02033 21 1 GQECCITGKCCKDG MT_PARLI 18 1 MTECHINOIDEA3 Length of motif = 11 Motif number = 3 Sea-urchin metallothionein motif III - 2 PCODE ST INT CCGKCTNAACK MT_STENE 34 1 CCGICTNAACK MTA_STRPU 34 1 CCGKCSNAACK MTB_STRPU 34 1 CCGKCSNAACK O02033 38 3 CCGTCSNAACK MT_PARLI 35 3 MTECHINOIDEA4 Length of motif = 19 Motif number = 4 Sea-urchin metallothionein motif IV - 2 PCODE ST INT CADGCKCGSGCSCTEGNCA MT_STENE 45 0 CANGCKCGSGCSCTEGNCA MTA_STRPU 45 0 CADGCTCGSGCSCTEGNCP MTB_STRPU 46 1 CADGCKCEGACACTMGNCT O02033 49 0 CTGGCKCEGGCVCTEGNCT MT_PARLI 46 0

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