The domain within your query sequence starts at position 39 and ends at position 219; the E-value for the Ribonuclease_T2 domain shown below is 3.1e-46.



PFAM accession number:PF00445
Interpro abstract (IPR001568):

The fungal ribonucleases T2 from Aspergillus oryzae, M from Aspergillus saitoi and Rh from Rhizopus niveus are structurally and functionally related 30 Kd glycoproteins [ (PUBMED:2229029) ] that cleave the 3'-5' internucleotide linkage of RNA via a nucleotide 2',3'-cyclic phosphate intermediate ( EC ). Two histidines residues have been shown [ (PUBMED:2298207) (PUBMED:1633875) ] to be involved in the catalytic mechanism of RNase T2 and Rh. These residues and the region around them are highly conserved in a number of other RNAses that have been found to be evolutionary related to these fungal enzymes.

Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases) [ (PUBMED:12109772) (PUBMED:11582795) (PUBMED:10446375) (PUBMED:12731868) (PUBMED:11158587) ]. Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sissile bond, respectively.

GO function:ribonuclease T2 activity (GO:0033897), RNA binding (GO:0003723)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Ribonuclease_T2