Summary: HIT domain
HIT domain Provide feedback
No Pfam abstract.
Lima CD, Klein MG, Weinstein IB, Hendrickson WA , Proc Natl Acad Sci U S A 1996;93:5357-5362.: Three-dimensional structure of human protein kinase C interacting protein 1, a member of the HIT family of proteins. PUBMED:8643579 EPMC:8643579
Internal database links
|Similarity to PfamA using HHSearch:||CwfJ_C_1 DcpS_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry 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].
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This example describes an architecture with one
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Curation and family details
|Seed source:||Prosite & Pfam-B_8474 (Release 8.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||26|
|Number in full:||8213|
|Average length of the domain:||96.10 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||65.13 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||18|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HIT domain has been found. There are 105 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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