NEUZ |
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| SMART accession number: | SM00588
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| Description: |
domain in neuralized proteins |
| Interpro abstract (IPR006573): |
NEUZ is a domain of unknown function found in neuralized proteins, i.e. proteins involved in the specification of the neuroblast during cellular differentiation.
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| Family alignment: |
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There are 454
NEUZ domains in 162 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Doerks T, Copley RR, Schultz J, Ponting CP, Bork P
- Systematic identification of novel protein domain families associated with nuclear functions.
- Genome Res. 2002; 12: 47-56
- Display abstract
A systematic computational analysis of protein sequences containing known nuclear domains led to the identification of 28 novel domain families. This represents a 26% increase in the starting set of 107 known nuclear domain families used for the analysis. Most of the novel domains are present in all major eukaryotic lineages, but 3 are species specific. For about 500 of the 1200 proteins that contain these new domains, nuclear localization could be inferred, and for 700, additional features could be predicted. For example, we identified a new domain, likely to have a role downstream of the unfolded protein response; a nematode-specific signalling domain; and a widespread domain, likely to be a noncatalytic homolog of ubiquitin-conjugating enzymes.
- Ponting CP, Mott R, Bork P, Copley RR
- Novel protein domains and repeats in Drosophila melanogaster: insights into structure, function, and evolution.
- Genome Res. 2001; 11: 1996-2008
- Display abstract
Sequence database searching methods such as BLAST, are invaluable for predicting molecular function on the basis of sequence similarities among single regions of proteins. Searches of whole databases however, are not optimized to detect multiple homologous regions within a single polypeptide. Here we have used the prospero algorithm to perform self-comparisons of all predicted Drosophila melanogaster gene products. Predicted repeats, and their homologs from all species, were analyzed further to detect hitherto unappreciated evolutionary relationships. Results included the identification of novel tandem repeats in the human X-linked retinitis pigmentosa type-2 gene product, repeated segments in cystinosin, associated with a defect in cystine transport, and 'nested' homologous domains in dysferlin, whose gene is mutated in limb girdle muscular dystrophy. Novel signaling domain families were found that may regulate the microtubule-based cytoskeleton and ubiquitin-mediated proteolysis, respectively. Two families of glycosyl hydrolases were shown to contain internal repetitions that hint at their evolution via a piecemeal, modular approach. In addition, three examples of fruit fly genes were detected with tandem exons that appear to have arisen via internal duplication. These findings demonstrate how completely sequenced genomes can be exploited to further understand the relationships between molecular structure, function, and evolution.
- Structure (3D structures containing this domain)
3D Structures of NEUZ domains in PDB
| PDB code | Main view | Title | | 2e63 |  | Solution structure of the neuz domain in kiaa1787 protein |
| 2yue |  | Solution structure of the neuz (nhr) domain in neuralized from drosophila melanogaster |
- Links (links to other resources describing this domain)
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