The domain within your query sequence starts at position 214 and ends at position 268; the E-value for the HARP domain shown below is 8e-29.

FRVKIGYNQELIAVFKSLPSRHYDSFTKTWDFSMSDYRALMKAVERLSTVSLKPL

HARP

HARP
PFAM accession number:PF07443
Interpro abstract (IPR010003):

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 stabilise 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 [(PUBMED:21525954), (PUBMED:22279047)].

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. 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 [(PUBMED:21525954), (PUBMED:22279047), (PUBMED:10857751)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HARP