The domain within your query sequence starts at position 292 and ends at position 670; the E-value for the PAD domain shown below is 3.8e-174.

PIFTDTVMFRIAPWIMTPNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYMN
RGDRWIQDEIEFGYIEAPHKGFPVVLDSPRDGNLKDFPIKQLLGPDFGYVTREPLFETVT
SLDSFGNLEVSPPVTVNGKEYPLGRILIGSSFPLSGGRRMTKVVRDFLQAQQVQAPVELY
SDWLTVGHVDEFMTFIPIPGKKEFRLLMASTSACYQLFREKQKAGHGEAVMFKGLGGMSS
KRITINKILSNESLTQENQYFQRCLDWNRDILKRELALTEKDIIDLPALFKMDENHQARA
FFPNMVNMIVLDKDLGIPKPFGPQVEEECCLETHVRGLLEPLGLACTFIDDISAYHKFLG
EVHCGTNVRRKPFTFKWWH

PAD

PAD
PFAM accession number:PF03068
Interpro abstract (IPR013530):

In the presence of calcium ions, Protein-arginine deiminase (PAD) enzymes EC 3.5.3.15 catalyse the post-translational modification reaction responsible for the formation of citrulline residues from protein-bound arginine residues [(PUBMED:10092850)]. Four PAD isotypes of PAD have been identified in mammals, a fifth may also exist. Non-mammalian vertebrates appear to have only a single PAD enzyme. All known natural substrates of PAD are proteins known to have an important structural function, such as keratin (PAD1), intermediate filaments or proteins associated with intermediate filaments. Citrulination may have consequences for the structural integrity and interactions of these proteins. Physiological levels of calcium appear to be too low to activate these enzymes suggesting a role between PAD activation and loss of calcium homeostasis during terminal differentiation and cell death (apoptosis).

GO component:cytoplasm (GO:0005737)
GO function:protein-arginine deiminase activity (GO:0004668), calcium ion binding (GO:0005509)

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