In molecular biology, the CVNH domain (CyanoVirin-N Homology domain) is a conserved protein domain. It is found in the sugar-binding antiviral protein cyanovirin-N (CVN) as well as proteins from filamentous ascomycetes and in the fern Ceratopteris richardii.(PMID 16003744)
Family alignment:
There are 53
CVNH domains in 51 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CVNH domain is also avaliable.
The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as aprotein module in eukaryotes.
Proteins. 2005; 60: 670-8
Display abstract
A novel protein family homologous to the sugar-binding antiviral proteincyanovirin-N (CVN) is described. CVN, an 11-kDa protein that, by binding to thehigh-mannose moiety of certain viral surface glycoproteins, blocks virus entryinto target cells, has thus far been identified only in the cyanobacterium Nostocellipsosporum. Here we show that CVN belongs to a protein family identified byanalysis of transcript sequences deriving from a gene expression profiling study conducted in the truffle Tuber borchii. Members of this family (namedCyanoVirin-N Homology) are found in filamentous ascomycetes and in the fernCeratopteris richardii. As revealed by 3D structure-based searches, all CVNHproteins have a predicted fold that matches the so far unique fold of thecyanobacterial polypeptide. The CVNH domain is a versatile protein module. Inferns and cyanobacteria it is found in secretory proteins. In filamentousascomycetes it is found in nonsecretory monodomain proteins as well as part ofmultidomain proteins bearing functionally related modules such as thepeptidoglycan and chitin-binding domain LysM. Transcript abundance data furtherindicate that the expression of different CVNH forms is modulated in response to nutrient availability. These findings have implications for the understanding of protein-oligosaccharide interaction in fungi and plants, and provide candidatepolypeptides to be tested and exploited as antiviral agents.
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