The domain within your query sequence starts at position 27 and ends at position 149; the E-value for the RnaseA domain shown below is 1.9e-29.



PFAM accession number:PF00074
Interpro abstract (IPR023412):

Pancreatic ribonucleases (RNaseA) are pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles [ (PUBMED:3940901) ]. Specifically, the enzymes are involved in endonucleolytic cleavage of 3'-phosphomononucleotides and 3'-phosphooligonucleotides ending in C-P or U-P with 2',3'-cyclic phosphate intermediates. Ribonuclease can unwind the DNA helix by complexing with single-stranded DNA; the complex arises by an extended multi-site cation-anion interaction between lysine and arginine residues of the enzyme and phosphate groups of the nucleotides. Other proteins belonging to the pancreatic RNAse family include: bovine seminal vesicle and brain ribonucleases; kidney non-secretory ribonucleases [ (PUBMED:2734298) ]; liver-type ribonucleases [ (PUBMED:2611266) ]; angiogenin, which induces vascularisation of normal and malignant tissues; eosinophil cationic protein [ (PUBMED:2473157) ], a cytotoxin and helminthotoxin with ribonuclease activity; and frog liver ribonuclease and frog sialic acid-binding lectin. The sequence of pancreatic RNases contains four conserved disulphide bonds and three amino acid residues involved in the catalytic activity.

This entry represents a domain in Ribonuclease A. Its structure is an alpha+beta fold -- long curved beta sheet and three helices.

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