SMART: Pfam domain PRP8

The domain within your query sequence starts at position 1760 and ends at position 1989; the E-value for the PRP8_domainIV domain shown below is 9.8e-134.

EPYLSSQNYGELFSNQIIWFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFL
KIIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPKQIIVTRKGMLDPLEVHLLDF
PNIVIKGSELQLPFQACLKVEKFGDLILKATEPQMVLFNLYDDWLKTISSYTAFSRLILI
LRALHVNNDRAKVILKPDKTTVTEPHHIWPTLTDEEWIKVEVQLKDLILA

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) ].

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