The domain within your query sequence starts at position 41 and ends at position 295; the E-value for the PNP_UDP_1 domain shown below is 4.9e-56.

QVAVICGSGLGGLTAHLKAAQIFDYNEIPNFPQSTVQGHAGRLVFGLLNGRSCVMMQGRF
HMYEGYSLSEVTFPVRVFHLLGVETLVVTNAAGGLNPNFEVGDIMLIRDHINLPGFCGQN
PLRGPNDERFGVRFPAMSDAYDRDMRQKAFSAWKQMGEQRKLQEGTYVMLAGPNFETVAE
SRLLKMLGADAVGMSTVPEVIVARHCGLRVFGFSLITNMVVMDYENLEKANHKEVLDAGK
AAAQKLERFVSILME

PNP_UDP_1

 PNP_UDP_1
PFAM accession number:PF01048
Interpro abstract (IPR000845):

Phosphorylases with this domain include:

  • Purine nucleoside phosphorylase ( EC 2.4.2.1 ) (PNP) from most bacteria (gene deoD), which catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ (PUBMED:8534998) ].
  • Uridine phosphorylase ( EC 2.4.2.3 ) (UdRPase) from bacteria (gene udp) and mammals, which catalyses the cleavage of uridine into uracil and ribose-1-phosphate, the products of the reaction are used either as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis [ (PUBMED:7744869) ].
  • 5'-methylthioadenosine phosphorylase ( EC 2.4.2.28 ) (MTA phosphorylase) from Sulfolobus solfataricus [ (PUBMED:7929153) ].
  • Purine nucleoside phosphorylase ( EC 2.4.2.1 ) (PNP) from mammals as well as from some bacteria (gene deoD). This enzyme catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [ (PUBMED:2104852) ].
  • 5'-methylthioadenosine phosphorylase ( EC 2.4.2.28 ) (MTA phosphorylase) from eukaryotes [ (PUBMED:8687427) ].
GO process:nucleoside metabolic process (GO:0009116)
GO function:catalytic activity (GO:0003824)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PNP_UDP_1