The domain within your query sequence starts at position 1 and ends at position 276; the E-value for the Hus1 domain shown below is 1.5e-77.

MRFRARITSKRFIELFIQVSSTVAKLAKVCVLRVCPDRLYFCPMGLLGEAQLWGEMRRDV
FHHFCMEGASQEFNEICLELMSEHLARAVKNAGNASSLKLQLTNKQRPCLTLVVELASCP
GHTRAVVHDLPVRVLPRRRWKDCTEPHVRGSDVSVYLPALKTLKNMVERMANVGSHVLVE
ANLNGRMNLTVETDRVTIKSYFKNLGNPPNAVLCMSQGRDPETMVQVRVDNRKLLQCFDG
HQINPTMALCNILSNTLLHLVLVHEDISLQYFIPAS

Hus1

Hus1
PFAM accession number:PF04005
Interpro abstract (IPR007150):

This entry consists of the human Hus1 protein and budding yeast Mec3. They are components of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes [ (PUBMED:9891048) (PUBMED:9180692) ].

Hus1, Rad1, and Rad9 (which share homology with Mec1, Rad17, Ddc1 in budding yeast) are three evolutionarily conserved proteins required for checkpoint control. These proteins are known to form a stable complex. Structurally, the Ddc1-Mec3-Rad17 complex is similar to the PCNA complex, which forms trimeric ring-shaped clamps. Ddc1-Mec3-Rad17 plays a role in checkpoint activation that permits DNA-repair pathways to prevent cell cycle progression in response to DNA damage and replication stress [ (PUBMED:9311982) (PUBMED:21978893) ].

GO process:DNA damage checkpoint (GO:0000077)
GO component:checkpoint clamp complex (GO:0030896)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Hus1