The domain within your query sequence starts at position 167 and ends at position 262; the E-value for the HIT domain shown below is 9.2e-17.



PFAM accession number:PF01230
Interpro abstract (IPR001310):

The Histidine Triad (HIT) motif, His-x-His-x-His-x-x (x, a hydrophobic amino acid) was identified as being highly conserved in a variety of organisms [(PUBMED:1472710)]. Crystal structure of rabbit Hint, purified as an adenosine and AMP-binding protein, showed that proteins in the HIT superfamily are conserved as nucleotide-binding proteins and that Hint homologues, which are found in all forms of life, are structurally related to Fhit homologues and GalT-related enzymes, which have more restricted phylogenetic profiles [(PUBMED:9164465)]. Hint homologues including rabbit Hint and yeast Hnt1 hydrolyse adenosine 5' monophosphoramide substrates such as AMP-NH2 and AMP-lysine to AMP plus the amine product and function as positive regulators of Cdk7/Kin28 in vivo [(PUBMED:11805111)]. Fhit homologues are diadenosine polyphosphate hydrolases [(PUBMED:8794732)] and function as tumour suppressors in human and mouse [(PUBMED:10758156)] though the tumour suppressing function of Fhit does not depend on ApppA hydrolysis [(PUBMED:9576908)]. The third branch of the HIT superfamily, which includes GalT homologues, contains a related His-X-His-X-Gln motif and transfers nucleoside monophosphate moieties to phosphorylated second substrates rather than hydrolysing them [(PUBMED:12119013)].

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