uncharacterized protein Dmel_CG4409 [Drosophila melanogaster]
Ins_allergen_rp domain-containing protein( domain architecture ID 10535966)
Ins_allergen_rp domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Ins_allergen_rp | pfam06757 | Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a ... |
81-264 | 7.11e-49 | ||||
Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a case of novel gene evolution. The case in point is the arms-race between plants and their infective insective herbivores in the area of the glucosinolate-myrosinase system. Brassicas have developed the glucosinolate-myrosinase system as chemical defence mechanism against the insects, and consequently the insects have adapted to produce a detoxifying molecule, nitrile-specifier protein (NSP). NSP is present in the small white butterfly Pieris rapae. NSP is structurally different from and has no amino acid homology to any known detoxifying enzymes, and it appears to have arisen by a process of domain and gene duplication of a sequence of unknown function that is widespread in insect species and referred to as insect-allergen-repeat protein. Thus this family is found either as a single domain or as a multiple repeat-domain. : Pssm-ID: 462003 Cd Length: 173 Bit Score: 159.66 E-value: 7.11e-49
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Name | Accession | Description | Interval | E-value | ||||
Ins_allergen_rp | pfam06757 | Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a ... |
81-264 | 7.11e-49 | ||||
Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a case of novel gene evolution. The case in point is the arms-race between plants and their infective insective herbivores in the area of the glucosinolate-myrosinase system. Brassicas have developed the glucosinolate-myrosinase system as chemical defence mechanism against the insects, and consequently the insects have adapted to produce a detoxifying molecule, nitrile-specifier protein (NSP). NSP is present in the small white butterfly Pieris rapae. NSP is structurally different from and has no amino acid homology to any known detoxifying enzymes, and it appears to have arisen by a process of domain and gene duplication of a sequence of unknown function that is widespread in insect species and referred to as insect-allergen-repeat protein. Thus this family is found either as a single domain or as a multiple repeat-domain. Pssm-ID: 462003 Cd Length: 173 Bit Score: 159.66 E-value: 7.11e-49
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Name | Accession | Description | Interval | E-value | ||||
Ins_allergen_rp | pfam06757 | Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a ... |
81-264 | 7.11e-49 | ||||
Insect allergen related repeat, nitrile-specifier detoxification; This family exemplifies a case of novel gene evolution. The case in point is the arms-race between plants and their infective insective herbivores in the area of the glucosinolate-myrosinase system. Brassicas have developed the glucosinolate-myrosinase system as chemical defence mechanism against the insects, and consequently the insects have adapted to produce a detoxifying molecule, nitrile-specifier protein (NSP). NSP is present in the small white butterfly Pieris rapae. NSP is structurally different from and has no amino acid homology to any known detoxifying enzymes, and it appears to have arisen by a process of domain and gene duplication of a sequence of unknown function that is widespread in insect species and referred to as insect-allergen-repeat protein. Thus this family is found either as a single domain or as a multiple repeat-domain. Pssm-ID: 462003 Cd Length: 173 Bit Score: 159.66 E-value: 7.11e-49
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Blast search parameters | ||||
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