{PDOC00360}
{PS00347; ZF_PARP_1}
{PS50064; ZF_PARP_2}
{BEGIN}
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* Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature and profile *
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Poly(ADP-ribose) polymerase (EC 2.4.2.30) (PARP) [1,2] is a  eukaryotic enzyme
that catalyzes  the  covalent  attachment  of ADP-ribose  units from NAD(+) to
various nuclear  acceptor  proteins.  This  post-translational modification of
nuclear  proteins  is  dependent  on  DNA.  It  appears  to be involved in the
regulation of various  important  cellular  processes such as differentiation,
proliferation and  tumor  transformation  as  well as in the regulation of the
molecular events involved in the recovery of the cell from DNA damage.

Structurally, PARP,  about  1000  amino-acids residues long, consists of three
distinct domains:  an  N-terminal zinc-dependent DNA-binding domain, a central
automodification domain and a C-terminal NAD-binding domain.

The DNA-binding region  contains a pair of zinc finger domains which have been
shown to  bind DNA in a zinc-dependent manner. The zinc finger domains of PARP
seem to bind specifically to single-stranded DNA.

DNA ligase  III  [3]  contains,  in its N-terminal section, a single copy of a
zinc finger highly similar to those of PARP.

-Consensus pattern: C-[KR]-x-C-x(3)-I-x-[KAL]-x(3)-[RG]-x(16,18)-W-[FYH]-H-
                    x(2)-C
                    [The 3 C's and the H are zinc ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Kappus S.; stephanie.kappus@genebio.com

-Last update: September 2022 / Text revised.

[ 1] Althaus F.R., Richter C.R.
     "ADP-ribosylation of proteins. Enzymology and biological
     significance."
     Mol. Biol. Biochem. Biophys. 37:1-237(1987).
     PubMed=3118181
[ 2] de Murcia G., Menissier de Murcia J.
     Trends Biochem. Sci. 19:172-176(1994).
[ 3] Wei Y.-F., Robins P., Carter K., Caldecott K., Pappin D.J.C.,
     Yu G.-L., Wang R.-P., Shell B.K., Nash R.A., Schar P., Barnes D.E.,
     Haseltine W.A., Lindahl T.
     "Molecular cloning and expression of human cDNAs encoding a novel DNA
     ligase IV and DNA ligase III, an enzyme active in DNA repair and
     recombination."
     Mol. Cell. Biol. 15:3206-3216(1995).
     PubMed=7760816

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