SMART: Pfam domain AXH

The domain within your query sequence starts at position 467 and ends at position 580; the E-value for the AXH domain shown below is 3.1e-44.

FMKGAIIQLATGELKRVEDLQTQDFVRSAEVSGGLKIDSSTVVDIQESQWPGFVMLHFVV
GEQQSKVSIEVPPEHPFFVYGQGWSSCSPGRTAQLFSLPCHRLQVGDVCISISL

AXH

PFAM accession number:	PF08517
Interpro abstract (IPR003652):	Spinocerebellar ataxia type 1 is late-onset neurodegenerative diseases caused by the expansion of a CAG triplet repeat in the SCA1 gene. This results in the lengthening of a polyglutamine tract in the gene product ataxin-1 producing a toxic gain of function that results in neuronal death. The crystal structure of the AXH domain of ataxin-1 has been determined as it exhibits significant sequence similarity to the transcription factor HBP1 [ (PUBMED:12965213) ] and has been implicated in RNA binding and self-association. The AXH domain is dimeric and contains an OB-fold, a structural motif found in many oligonucleotide-binding proteins. By comparison to other proteins that contain an OB-fold, the putative RNA-binding region has been identified. In addition, there are a number of well-conserved residues that form a second ligand-binding surface, suggesting that AXH domains interact with a common yet unidentified partner [ (PUBMED:14583607) ].
GO function:	protein binding (GO:0005515), RNA binding (GO:0003723)

PFAM accession number:

PF08517

Interpro abstract (IPR003652):

Spinocerebellar ataxia type 1 is late-onset neurodegenerative diseases caused by the expansion of a CAG triplet repeat in the SCA1 gene. This results in the lengthening of a polyglutamine tract in the gene product ataxin-1 producing a toxic gain of function that results in neuronal death.

The crystal structure of the AXH domain of ataxin-1 has been determined as it exhibits significant sequence similarity to the transcription factor HBP1 [ (PUBMED:12965213) ] and has been implicated in RNA binding and self-association. The AXH domain is dimeric and contains an OB-fold, a structural motif found in many oligonucleotide-binding proteins. By comparison to other proteins that contain an OB-fold, the putative RNA-binding region has been identified. In addition, there are a number of well-conserved residues that form a second ligand-binding surface, suggesting that AXH domains interact with a common yet unidentified partner [ (PUBMED:14583607) ].

GO function:

protein binding (GO:0005515), RNA binding (GO:0003723)

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