The domain within your query sequence starts at position 98 and ends at position 316; the E-value for the PNP_UDP_1 domain shown below is 7.1e-26.

KFVCVGGSPNRMKAFAQFMHKELRLEGDGEDIEDICAGTDRYCMFKTGPVLSVSHGMGIP
SISIMLHELIKLLHHAHCCDVTIIRIGTSGGIGIAPGSVVITDTAVDSFFKPRFEQVILD
NVVTRSTELDKELANDLFNCSREIPNVPTLIGHTMCTYDFYEGQGRLDGALCSFSREKKL
DYLKRAYRAGVRNIEMESTVFAAMCGLCGLRVVPMSANS

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