****************************
* Barwin domain signatures *
****************************

Barwin [1] is a barley seed protein of 125 residues that binds weakly a chitin
analog. It contains six cysteines involved in disulfide bonds, as shown in the
following schematic representation.

                              +---------------+
                              |    *****      |                ****
    xxxxxxxxxxxxxxxCxxxxxxxxxxCxxxxCxCxxxxxxxxCxxxxxxxxxxxxxxxxxxCx
                   |               | |                           |
                   +---------------+ +---------------------------+

'C': conserved cysteine involved in a disulfide bond.
'*': position of the patterns.

Barwin is closely related to the following proteins:

 - Hevein, a wound-induced protein found in the latex of rubber trees.
 - Win1 and win2, two wound-induced proteins from potato.
 - Pathogenesis-related protein 4 from tobacco.

Hevein and the win1/2 proteins consist  of an N-terminal chitin-binding domain
followed by a barwin-like C-terminal domain.  Barwin  and its related proteins
could be involved in a defense mechanism in plants.  As signature patterns, we
selected two highly conserved regions that contain some of the cysteines.

-Consensus pattern: C-G-[KR]-C-L-x-V-T-N
                    [The two C's are involved in disulfide bonds]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.

-Consensus pattern: V-N-Y-[EQ]-F-V-[DN]-C
                    [C is involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.

-Last update: October 1993 / Patterns and text revised.

[ 1] Svensson B., Svendsen I., Hojrup P., Roepstorff P., Ludvigsen S.,
     Poulsen F.M.
     Biochemistry 31:8767-8770(1992).