The domain within your query sequence starts at position 29 and ends at position 251; the E-value for the ART domain shown below is 4e-65.

LDMAENAFDDEYLKCKSRMESKYIPQMKREEWANDALLRMVWDNAEIQWEARKAQLFLPR
NFKDTYGIALTAYVNEAQEQTSFYHTFSSAVKMAGLSRRRYIYNFPFKAFHFYLVRALQL
LRRPCEKSYKTVVYSTSPDISFTFGEQNQARLGNFTLAYSAKPETADNQRVLTIQTCFGV
AVGKFLNKEDDSVVLIPLSEVFQVSRKGTSNDLVLQSINSTCS

ART

 ART
PFAM accession number:PF01129
Interpro abstract (IPR000768):

Mono-ADP-ribosylation is a post-translational modification of proteins in which the ADP-ribose moiety of NAD is transferred to proteins. This process is responsible for the toxicity of some bacterial toxins (e.g., cholera and pertussis toxins). Mono (ADP-ribosyl) transferases exist in vertebrates EC 2.4.2.31 that transfer ADP-ribose to arginine [ (PUBMED:8703012) ]. NAD + + L-arginine = nicotinamide + N2-(ADP-D-ribosyl)-L-arginine At least five forms of the enzyme have been characterised to date, some of which are attached to the membrane via glycosylphosphatidylinositol (GPI) anchors, while others appear to be secreted. The enzymes contain ~250-300 residues, which encode putative signal sequences and carbohydrate attachment sites. In addition, the N- and C-termini are predominantly hydrophobic, a characteristic of GPI-anchored proteins [ (PUBMED:7947688) ].

GO process:protein ADP-ribosylation (GO:0006471)
GO function:NAD(P)+-protein-arginine ADP-ribosyltransferase activity (GO:0003956)

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