The domain within your query sequence starts at position 28 and ends at position 178; the E-value for the Pribosyltran domain shown below is 2.3e-25.

DISPLLKDPDSFRASIRLLASHLKSTHSGKIDYIAGLDSRGFLFGPSLAQELGVGCVLIR
KQGKLPGPTVSASYSLEYGKAELEIQKDALEPGQRVVIVDDLLATGGTMFAACDLLHQLR
AEVVECVSLVELTSLKGRERLGPIPFFSLLQ

Pribosyltran

Pribosyltran
PFAM accession number:PF00156
Interpro abstract (IPR000836):

This entry refers to the phosphoribosyl transferase (PRT) type I domain. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrpphosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. This domain is found in a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC 2.4.2.7, hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC 2.4.2.8, ribose-phosphate pyrophosphokinase EC 2.7.6.1, amidophosphoribosyltransferase EC 2.4.2.14, orotate phosphoribosyltransferase EC 2.4.2.10, uracil phosphoribosyltransferase EC 2.4.2.9, and xanthine-guanine phosphoribosyltransferase EC 2.4.2.22. In Arabidopsis, at the very N terminus of this domain is the P-Loop NTPase domain [(PUBMED:17143579), (PUBMED:11751055), (PUBMED:18550080), (PUBMED:15689504), (PUBMED:18399692), (PUBMED:12808089), (PUBMED:8894695), (PUBMED:22075667), (PUBMED:15096496), (PUBMED:7030616), (PUBMED:6105839), (PUBMED:21366534), (PUBMED:18535147)].

GO process:nucleoside metabolic process (GO:0009116)

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