The domain within your query sequence starts at position 1584 and ends at position 1849; the E-value for the Laminin_I domain shown below is 2e-92.

RLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMET
NELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQD
KTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNED
MEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQ
IENTLKEGNDILDEANRLLGEINSVI

Laminin_I

Laminin_I
PFAM accession number:PF06008
Interpro abstract (IPR009254):

Laminins are glycoproteins that are major constituents of the basement membrane of cells. Laminins are trimeric molecules; laminin-1 is an alpha1 beta1 gamma1 trimer. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure [ (PUBMED:3182802) ]. Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organisation of cells into tissues during embryonic development by interacting with other extracellular matrix components.

GO process:regulation of embryonic development (GO:0045995), regulation of cell adhesion (GO:0030155), regulation of cell migration (GO:0030334)
GO function:signaling receptor binding (GO:0005102)

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