{PDOC51467}
{PS51467; HARP}
{BEGIN}
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* HARP domain profile *
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SMARCAL1 (SWI/SNF-related,  matrix-associated,  actin-dependent  regulator  of
chromatin, subfamily  A-like1),  also known as DNA-dependent ATPase A and HARP
(Hep-A-related proteins),  maintains  genome integrity during DNA replication.
SMARCAL1 has   ATP-dependent  annealing  helicase  activity,  which  helps  to
stabilize stalled   replication   forks   and  facilitate  DNA  repair  during
replication. Biochemically, SMARCAL1 can bind to DNA that contains single- and
double-stranded regions  such as forks and DNA hairpins. DNA binding activates
its ATPase  activity, and this activity promotes DNA single-stranded annealing
[1,2].

SMARCAL1 is a multifunctional protein. The ATPase domain, which lies in the C-
terminal half  of the protein, is split into two regions of primary amino acid
sequence by a 115-amino-acid linker sequence (see <PDOC51192>). The N-terminal
half of the protein contains a highly sequence conserved ssDNA-binding protein
replication protein A (RPA)-binding domain, and one or two HARP domain(s). The
evolutionarily conserved   HARP   domain  determines  the  annealing  helicase
activity required for the in vivo and in vitro functions of SMARCAL1 [1,2].

The profile we developed covers the entire HARP domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: February 2012 / First entry.

[ 1] Ghosal G., Yuan J., Chen J.
     "The HARP domain dictates the annealing helicase activity of
     HARP/SMARCAL1."
     EMBO Rep. 12:574-580(2011).
     PubMed=21525954; DOI=10.1038/embor.2011.74
[ 2] Betous R., Mason A.C., Rambo R.P., Bansbach C.E., Badu-Nkansah A.,
     Sirbu B.M., Eichman B.F., Cortez D.
     "SMARCAL1 catalyzes fork regression and Holliday junction migration to
     maintain genome stability during DNA replication."
     Genes Dev. 26:151-162(2012).
     PubMed=22279047; DOI=10.1101/gad.178459.111

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