The domain within your query sequence starts at position 1 and ends at position 394; the E-value for the CReP_N domain shown below is 1.3e-205.

METGTHRARKRPGPRLGSWFRLPFLRRSHACSSEFPPPSSRQNPGNSALPERRTRYWTKL
LSQLLALLPSLFQKLLLWSQLFGGLIPTRWLDFAASYSALRALRGREESAAPTVQKSLSS
LRLDSSEDLVVSSLDWLEEGLQWQCSSSDLELKLKAQERALDSAAPTFLLEQQLWGVELL
PSSLQAGLVSHRELDSSSSGPLSVQSLGNFKVVSYLLNPSYLDYLPQLGLRCQSSAGGGQ
FVGFRTLTPESCYLSEDGCHPQPLRAEMSATAWRRCPPLSTEGLPEIHHLRMKRLEFLQA
NKGQELPTPDQDNGYHSLEEEHNLLRMDPQHCTDNPAQAVSPAADRPEPTEKKPELVIQE
VSQSPQGSSLFCELPVEKECEEDHTNATDLSDRG

CReP_N

CReP_N
PFAM accession number:PF10472
Interpro abstract (IPR019512):

This entry represents the conserved N-terminal domain of the regulatory subunit (15B) of protein phosphatase 1 (also known as CReP, or the constitutive repressor of eIF2alpha phosphorylation). The CReP catalytic subunit functions in the dephosphorylation of eIF2-alpha under basal conditions in the absence of stress. In response to translation inhibition, there is reduced synthesis of the labile CReP that contributes to elevated levels of eIF2-alpha phosphorylation [ (PUBMED:14638860) ]. The C terminus, family PP1c, is shared with the apoptosis-associated protein Gadd34 and herpes simplex virus [ (PUBMED:15355306) ].

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