The domain within your query sequence starts at position 1760 and ends at position 1990; the E-value for the PRP8_domainIV domain shown below is 1.5e-132.

EPYLSSQNYGELFSNQIIWFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFL
KIIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPKQIIVTRKGMLDPLEVHLLDF
PNIVIKGSELQLPFQACLKVEKFGDLILKATEPQMVLFNLYDDWLKTISSYTAFSRLILI
LRALHVNNDRAKVILKPDKTTVTEPHHIWPTLTDEEWIKVEVQLKDLILAD

PRP8_domainIV

PRP8_domainIV
PFAM accession number:PF12134
Interpro abstract (IPR021983):

This entry represents Prp8 domain IV, which adopts a RNase H like fold within its core structure but with little sequence similarity. Pre-mRNA-splicing factor 8 (Prp8), a spliceosome protein, interacts directly with the splice sites and branch regions of precursor-mRNAs and spliceosomal RNAs associated with catalysis of the two steps of splicing. Catalysis of RNA cleavage by RNase H-like proteins involves a two-metal mechanism in which adjacently-bound divalent magnesium ions promote hydrolysis by activation of a water nucleophile and stabilization of the transition-state. However, the Prp8 domain IV contains only one of the canonical metal-binding sites and the coordinating side chains are spatially conserved with respect to Mg2+-coordinating residues within the RNase H fold [(PUBMED:18836455)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry PRP8_domainIV