Description

IPR036265 is a HIT-like superfamily.

<p>The histidine triad motif (HIT) consists of the conserved sequence HXHXHXX (where X is a hydrophobic amino acid) at the enzymatic catalytic centre, in which the second histidine is strictly conserved and participates in catalysis with the third histidine [[cite:PUB00097344], [cite:PUB00097347], [cite:PUB00008005]]. Proteins containing HIT domains form a superfamily of nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides [[cite:PUB00008005], [cite:PUB00097344]]. They are highly conserved from archaea to humans and are involved in galactose metabolism, DNA repair, and tumor suppression [[cite:PUB00097349]]. HIT-containing proteins can be divided in five families based on catalytic specificities, sequence compositions, and structural similarities of its members:</p> <ul> <li>Hint family of protein kinase-interacting proteins, the most ancient class in this superfamily. These include adenosine 5'-monophosphoramide hydrolases (e.g. HIT-nucleotide-binding protein, or HINT) [[cite:PUB00097345], [cite:PUB00008005]]. They also have a conserved zinc-binding motif C-X-X-C (where C is a cysteine residue and X is a hydrophobic residue), and a zinc ion is coordinated by these cysteine residues, together with the first histidine residue [[cite:PUB00097349]].</li> <li>Fragile HIT protein, or FINT, whose name is due to its high rate of mutation at its locus on chromosome 3 in many cancers has been characterised as a tumor suppressor and plays a role in the hydrolysis of dinucleotide polyphosphates [[cite:PUB00097347], [cite:PUB00097349]]. HINT and FINT HIT domains have a topology similar to that found in the N-terminal of protein kinases [[cite:PUB00035586]].</li> <li>GalT family. These include specific nucleoside monophosphate transferases (e.g. galactose-1-phosphate uridylyltransferase, diadenosine tetraphosphate phosphorylase, and adenylyl sulphate:phosphate adenylytransferase). These HIT domains are a duplication consisting of 2 HIT-like motifs. This family binds zinc and iron [[cite:PUB00097347], [cite:PUB00097343]].</li> <li>Aprataxin, which hydrolyses both dinucleotide polyphosphates and phophoramidates, and is involved in DNA repair systems [[cite:PUB00097347], [cite:PUB00097349]].</li> <li>mRNA decapping enzyme family. These include enzymes such as DcpS and Dcp2. The HIT-domain is usually C-terminal in these proteins [[cite:PUB00035587], [cite:PUB00097346]].</li> </ul> <p>This superfamily also includes CDP-diacylglycerol pyrophosphatases, CDH, which play a role in phospholipid metabolism and regulates phosphatidylinositol levels [[cite:PUB00097348]], the C-terminal CwfJ domains of CWF19-like protein DRN1 from Saccharomyces cerevisiae ([swissprot:P53255]) which is involved branched RNA metabolism, modulating the turnover of lariat-intron pre-mRNAs by the lariat-debranching enzyme DBR1 and its homologues. This C-terminal Cwfj domains contain evolutionarily conserved cysteine and histidine residues in an arrangement similar to the CCCH-class of zinc fingers [[cite:PUB00090681], [cite:PUB00008533]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: