The domain within your query sequence starts at position 397 and ends at position 682; the E-value for the PP1c_bdg domain shown below is 1.5e-154.

LPVSTRPVCSNKLIDYILGGAPSDLEASSDSESEDWGEEPEDDGFDSDGSLSESDVEQDS
EGLHLWNSFHSVDPYNPQNFTATIQTAARIAPRDPSDSGTSWSGSCGVGSCQEGPLPETP
DHSSGEEDDWEPSADEAENLKLWNSFCHSEDPYNLLNFKAPFQPSGKNWKGRQDSKASSE
ATVAFSGHHTLLSCKAQLLESQEDNCPGCGLGEALAGERYTHIKRKKVTFLEEVTEYYIS
GDEDRKGPWEEFARDGCRFQKRIQETEVAIGYCLAFEHREKMFNRL

PP1c_bdg

PP1c_bdg
PFAM accession number:PF10488
Interpro abstract (IPR019523):

This entry represents the conserved C terminus of the regulatory subunit (15A and 15B) of protein phosphatase 1. This C-terminal domain appears to be a binding region for the catalytic subunit (PP1C) of protein phosphatase-1, which may in some circumstances also be retroviral in origin since it is found in both herpes simplex virus and in mouse and man. This domain is found in Gadd-34 apoptosis-associated proteins as well as the constitutive repressor of eIF2-alpha phosphorylation/protein phosphatase 1, regulatory (inhibitor) subunit 15b, otherwise known as CReP. Diverse stressful conditions are associated with phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 (eIF2-alpha) on serine 51. This signaling event, which is conserved from yeast to mammals, negatively regulates the guanine nucleotide exchange factor, eIF2-B and inhibits the recycling of eIF2 to its active GTP bound form. In mammalian cells eIF2-alpha phosphorylation emerges as an important event in stress signaling that impacts on gene expression at both the translational and transcriptional levels [ (PUBMED:14638860) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PP1c_bdg