Species | Aspergillus fumigatus | |||||||||||
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Lineage | Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus | |||||||||||
CAZyme ID | Afu5g00510-T-p1 | |||||||||||
CAZy Family | GH32 | |||||||||||
CAZyme Description | Ortholog of A. niger CBS 513.88 : An06g02400, Aspergillus brasiliensis : Aspbr1_0031922, Neosartorya fischeri NRRL 181 : NFIA_042000 and Aspergillus fumigatus A1163 : AFUB_048980 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH172 | 102 | 363 | 2e-79 | 0.9957627118644068 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
402651 | DUF2961 | 2.33e-113 | 103 | 363 | 1 | 234 | Protein of unknown function (DUF2961). This family of proteins has no known function. |
240045 | Nudix_Hydrolase_30 | 0.007 | 250 | 300 | 56 | 106 | Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U=I, L or V), which functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.58e-304 | 1 | 454 | 1 | 455 | |
1.00e-291 | 5 | 454 | 3 | 452 | |
1.81e-291 | 5 | 454 | 3 | 452 | |
3.00e-282 | 2 | 455 | 4 | 457 | |
2.15e-278 | 3 | 455 | 6 | 458 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.70e-156 | 9 | 390 | 7 | 387 | Chain A, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1V_B Chain B, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1V_C Chain C, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1V_D Chain D, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1V_E Chain E, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1V_F Chain F, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_A Chain A, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_B Chain B, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_C Chain C, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_D Chain D, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_E Chain E, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1W_F Chain F, Difructose dianhydride I synthase/hydrolase (alphaFFase1) [Bifidobacterium dentium],7V1X_A Chain A, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium],7V1X_B Chain B, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium],7V1X_C Chain C, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium],7V1X_D Chain D, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium],7V1X_E Chain E, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium],7V1X_F Chain F, Difructose dianhydride I synthase/hydrolase [Bifidobacterium dentium] |
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6.60e-51 | 12 | 363 | 11 | 327 | Crystal structure of a DUF2961 family protein (BACUNI_00161) from Bacteroides uniformis ATCC 8492 at 1.62 A resolution [Bacteroides uniformis ATCC 8492],4KQ7_B Crystal structure of a DUF2961 family protein (BACUNI_00161) from Bacteroides uniformis ATCC 8492 at 1.62 A resolution [Bacteroides uniformis ATCC 8492] |
Other | SP_Sec_SPI | CS Position |
---|---|---|
1.000060 | 0.000001 |
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