PROSITE documentation PDOC51467
HARP domain profile


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.

Last update:

February 2012 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

HARP, PS51467; HARP domain profile  (MATRIX)


1AuthorsGhosal G. Yuan J. Chen J.
TitleThe HARP domain dictates the annealing helicase activity of HARP/SMARCAL1.
SourceEMBO Rep. 12:574-580(2011).
PubMed ID21525954

2AuthorsBetous R. Mason A.C. Rambo R.P. Bansbach C.E. Badu-Nkansah A. Sirbu B.M. Eichman B.F. Cortez D.
TitleSMARCAL1 catalyzes fork regression and Holliday junction migration to maintain genome stability during DNA replication.
SourceGenes Dev. 26:151-162(2012).
PubMed ID22279047

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