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* Sulfatases signatures *
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Sulfatases (EC 3.1.6.-) are enzymes that hydrolyze various sulfate esters. The
sequence of different types of sulfatases are available. These enzymes are:

 - Arylsulfatase A (EC 3.1.6.8)  (ASA), a lysosomal  enzyme  which  hydrolyzes
   cerebroside sulfate.
 - Arylsulfatase B (EC 3.1.6.12) (ASB),  a  lysosomal enzyme  which hydrolyzes
   the sulfate esters group from  N-acetylgalactosamine 4-sulfate  residues of
   dermatan sulfate.
 - Steryl-sulfatase  (EC 3.1.6.2) (STS)  (arylsulfatase C),  a  membrane bound
   microsomal enzyme which hydrolyzes 3-beta-hydroxy steroid sulfates.
 - Iduronate 2-sulfatase precursor (EC 3.1.6.13)  (IDS),  a  lysosomal  enzyme
   that hydrolyzes the 2-sulfate  groups  from  non-reducing-terminal iduronic
   acid residues in dermatan sulfate and heparan sulfate.
 - N-acetylgalactosamine-6-sulfatase  (EC 3.1.6.4),  an enzyme that hydrolyzes
   the 6-sulfate  groups  of  the  N-acetyl-d-galactosamine 6-sulfate units of
   chondroitin sulfate and the D-galactose 6-sulfate units of keratan sulfate.
 - Glucosamine-6-sulfatase   (EC 3.1.6.14)  (G6S),  a  lysosomal  enzyme  that
   hydrolyzes the N-acetyl-D-glucosamine  6-sulfate  units  of heparan sulfate
   and keratan sulfate.

 - Sea urchin embryo arylsulfatase (EC 3.1.6.1).
 - Chlamydomonas reinhardtii arylsulfatase (EC 3.1.6.1), an enzyme which plays
   an important role in the mineralization of sulfates.
 - Escherichia coli arylsulfatase (EC 3.6.1.1) (gene aslA).
 - Klebsiella aerogenes arylsulfatase (EC 3.6.1.1) (gene atsA).
 - Escherichia coli hypothetical protein yidJ.

It has been shown that the mammalian  enzymes and the sea urchin sulfatase are
structurally related  [1,2];    this   similarity can be extended to bacterial
enzymes [3],  but  the  algal  [4]  enzyme does not show any similarity to the
other sulfatases.

As signature patterns for that family of enzymes we have selected the two best
conserved regions. Both regions are located in the N-terminal section of these
enzymes.   The  first  region  contains  a conserved arginine which  could  be
implicated in the catalytic mechanism.

-Consensus pattern: [SAP]-[LIVMS]-[SC]-x-P-[STA]-R-x(2)-[LIVMF](2)-T-G
                    [R is a putative active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.

-Consensus pattern: G-Y-x-[ST]-x(2)-[LIVMA]-G-K-x(0,1)-[FYW]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: NONE.

-Last update: June 1994 / Patterns and text revised.

[ 1] Peters C., Schmidt B., Rommerskirch W., Rupp K., Zuehlsdorf M.,
     Vingron M., Meyer H.E., Pohlmann R., von Figura K.
     J. Biol. Chem. 265:3374-3381(1990).
[ 2] Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J.,
     Clements P.R., Hopwood J.J.
     Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990).
[ 3] de Hostos E.L., Schilling J., Grossman A.R.
     Mol. Gen. Genet. 218:229-239(1989).
[ 4] Murooka Y., Ishibashi K., Yasumoto M., Sasaki M., Sugino H., Azakami H.,
     Yamashita M.
     J. Bacteriol. 172:2131-2140(1990).