WORKLIST ENTRIES (1):

MTFUNGIIV View alignment        Fungi-IV metallothionein signature
 Type of fingerprint: COMPOUND with 3  elements
Links:
   PRINTS; PR00858 MTCRUSTACEAN; PR00859 MTPROKARYOTE; PR00860 MTVERTEBRATE
   PRINTS; PR00872 MTDIPTERA; PR00873 MTECHINOIDEA; PR00875 MTMOLLUSC
   PRINTS; PR00876 MTNEMATODE; PR00877 MTPLANTPEC
   INTERPRO; IPR000869
   PROTOMAP; P41927
   PFAM; PF00131 metalthio

 Creation date 26-JUN-1998; UPDATE 21-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.
  
   Fungi-IV (family 11) MTs are proteins of about 55 residues, with 9 conserved
   cysteines. In particular, the consensus pattern C-X-K-C-x-C-x(2)-C-K-C has
   been found to be diagnostic of family 11 MTs. The protein binds to copper 
   ions.
  
   MTFUNGIIV is a 3-element fingerprint that provides a signature for fungi-IV
   (family 11) metallothioneins. The fingerprint was derived from an initial
   alignment of 2 sequences: motif 2 contains 3 metal-binding Cys residues;
   and motif 3 includes 6 Cys residues, and spans the characteristic consensus
   pattern. A single iteration on OWL30.1 was required to reach convergence,
   no further sequences being identified beyond the starting set.
  
   An update on SPTR37_9f identified a true set of 2 sequences.

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

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

True positives..
 MT1_YARLI      MT2_YARLI      


  PROTEIN TITLES
   MT1_YARLI        METALLOTHIONEIN-I - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA)
   MT2_YARLI        METALLOTHIONEIN-II - YARROWIA LIPOLYTICA (CANDIDA LIPOLYTICA

SCAN HISTORY OWL30_1 1 300 NSINGLE SPTR37_9f 1 300 NSINGLE INITIAL MOTIF SETS MTFUNGIIV1 Length of motif = 20 Motif number = 1 Fungi IV metallothionein motif I - 1 PCODE ST INT MEFTTAMFGTSLIFTTSTQS MT1_YARLI 1 1 MEFTSALFGASLVQSKHKTT MT2_YARLI 1 1 MTFUNGIIV2 Length of motif = 18 Motif number = 2 Fungi IV metallothionein motif II - 1 PCODE ST INT KHNLVNNCCCSSSTSESS MT1_YARLI 21 0 KHNLVDSCCCSKPTEKPT MT2_YARLI 22 1 MTFUNGIIV3 Length of motif = 15 Motif number = 3 Fungi IV metallothionein motif III - 1 PCODE ST INT ASCACTKCGCKTCKC MT1_YARLI 41 2 NSCTCSKCACDSCKC MT2_YARLI 40 0 FINAL MOTIF SETS MTFUNGIIV1 Length of motif = 20 Motif number = 1 Fungi IV metallothionein motif I - 1 PCODE ST INT MEFTTAMFGTSLIFTTSTQS MT1_YARLI 1 1 MEFTSALFGASLVQSKHKTT MT2_YARLI 1 1 MTFUNGIIV2 Length of motif = 18 Motif number = 2 Fungi IV metallothionein motif II - 1 PCODE ST INT KHNLVNNCCCSSSTSESS MT1_YARLI 21 0 KHNLVDSCCCSKPTEKPT MT2_YARLI 22 1 MTFUNGIIV3 Length of motif = 15 Motif number = 3 Fungi IV metallothionein motif III - 1 PCODE ST INT ASCACTKCGCKTCKC MT1_YARLI 41 2 NSCTCSKCACDSCKC MT2_YARLI 40 0

User query: Display/Full Code "MTFUNGIIV"