PROSITE documentation PDOC51467HARP 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.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Ghosal G. Yuan J. Chen J. |
Title | The HARP domain dictates the annealing helicase activity of HARP/SMARCAL1. | |
Source | EMBO Rep. 12:574-580(2011). | |
PubMed ID | 21525954 | |
DOI | 10.1038/embor.2011.74 |
2 | Authors | Betous R. Mason A.C. Rambo R.P. Bansbach C.E. Badu-Nkansah A. Sirbu B.M. Eichman B.F. Cortez D. |
Title | SMARCAL1 catalyzes fork regression and Holliday junction migration to maintain genome stability during DNA replication. | |
Source | Genes Dev. 26:151-162(2012). | |
PubMed ID | 22279047 | |
DOI | 10.1101/gad.178459.111 |
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