{PDOC00620}
{PS00773; CHITINASE_19_1}
{PS00774; CHITINASE_19_2}
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* Chitinases family 19 signatures *
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Chitinases (EC 3.2.1.14) [1] are enzymes that  catalyze the  hydrolysis of the
beta-1,4-N-acetyl-D-glucosamine  linkages in  chitin polymers.  From  the view
point of sequence similarity  chitinases  belong to either  family 18 or 19 in
the classification  of  glycosyl  hydrolases  [2,E1].  Chitinases of family 19
(also known  as  classes  IA  or  I and IB or II) are enzymes from plants that
function in  the  defense  against  fungal  and insect pathogens by destroying
their chitin-containing  cell wall. Class IA/I and IB/II enzymes differ in the
presence (IA/I)  or absence (IB/II) of a N-terminal chitin-binding domain (see
the relevant entry <PDOC00025>). The catalytic domain of these enzymes consist
of about 220 to 230 amino acid residues.

As signature patterns we selected two highly conserved regions,  the first one
is located in the N-terminal section  and  contains  one  of the six cysteines
which are conserved  in  most, if  not all, of  these  chitinases and which is
probably involved in a disulfide bond.

-Consensus pattern: C-x(4,5)-F-Y-[ST]-x(3)-[FY]-[LIVMF]-x-A-x(3)-[YF]-x(2)-F-
                    [GSA]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: [LIVM]-[GSA]-F-x-[STAG](2)-[LIVMFY]-W-[FY]-W-[LIVM]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Neuhaus J.-M.; jean-marc.neuhaus@bota.unine.ch
           Henrissat B.; bernie@afmb.cnrs-mrs.fr

-Last update: November 1997 / Text revised.

[ 1] Flach J., Pilet P.-E., Jolles P.
     "What's new in chitinase research?"
     Experientia 48:701-716(1992).
     PubMed=1516675
[ 2] Henrissat B.
     "A classification of glycosyl hydrolases based on amino acid sequence
     similarities."
     Biochem. J. 280:309-316(1991).
     PubMed=1747104
[E1] https://www.uniprot.org/docs/glycosid

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