SMART: Pfam domain SF1-HH

The domain within your query sequence starts at position 18 and ends at position 130; the E-value for the SF1-HH domain shown below is 1.5e-47.

KRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPE
DRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHTLITEMVALNPDFKPPADYK

SF1-HH

PFAM accession number:	PF16275
Interpro abstract (IPR032570):	This helix-hairpin domain can be found in N-terminal region of mammalian splicing factor 1 (SF1) and fungal branchpoint binding proteins (BBP) [ (PUBMED:9433137) ]. These proteins are required for pre-spliceosome formation, which is the first step of pre-mRNA splicing [ (PUBMED:12374752) (PUBMED:10775271) ]. SF1 forms a complex with U2AF65 through the interaction between this domain and the C-terminal U2AF homology motif domain (UHM) of U2AF65. This domain forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex [ (PUBMED:23175611) ]. This domain contains a highly conserved SPSP motif at its C terminus; the phophorylation of the SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface [ (PUBMED:23273425) ].

PFAM accession number:

PF16275

Interpro abstract (IPR032570):

This helix-hairpin domain can be found in N-terminal region of mammalian splicing factor 1 (SF1) and fungal branchpoint binding proteins (BBP) [ (PUBMED:9433137) ]. These proteins are required for pre-spliceosome formation, which is the first step of pre-mRNA splicing [ (PUBMED:12374752) (PUBMED:10775271) ].

SF1 forms a complex with U2AF65 through the interaction between this domain and the C-terminal U2AF homology motif domain (UHM) of U2AF65. This domain forms a secondary, hydrophobic interface with U2AF65(UHM) to lock the orientation of the two subunits, which is essential for cooperative formation of the ternary SF1-U2AF65-RNA complex [ (PUBMED:23175611) ]. This domain contains a highly conserved SPSP motif at its C terminus; the phophorylation of the SPSP motif induces a disorder-to-order transition within a novel SF1/U2AF65 interface [ (PUBMED:23273425) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry SF1-HH