Species | Sporothrix schenckii | |||||||||||
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Lineage | Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii | |||||||||||
CAZyme ID | SPSK_02674-t39_1-p1 | |||||||||||
CAZy Family | CE5 | |||||||||||
CAZyme Description | S-formylglutathione hydrolase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
EC | 2.3.1.122:4 | 3.1.1.-:4 | 2.3.1.20:4 |
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Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE1 | 23 | 300 | 5.2e-48 | 0.9823788546255506 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
178061 | PLN02442 | 3.27e-114 | 12 | 303 | 14 | 281 | S-formylglutathione hydrolase |
131868 | fghA_ester_D | 4.91e-112 | 7 | 303 | 4 | 275 | S-formylglutathione hydrolase. This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification] |
223700 | FrmB | 1.20e-78 | 11 | 303 | 15 | 312 | S-formylglutathione hydrolase FrmB [Defense mechanisms]. |
395613 | Esterase | 2.23e-48 | 23 | 298 | 1 | 246 | Putative esterase. This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family. |
184875 | PRK14875 | 8.99e-05 | 138 | 182 | 183 | 230 | acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
4.79e-12 | 39 | 248 | 43 | 233 | |
4.07e-10 | 49 | 285 | 58 | 276 | |
4.23e-10 | 18 | 185 | 50 | 193 | |
7.61e-10 | 32 | 275 | 19 | 276 | |
9.80e-10 | 27 | 285 | 28 | 259 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.15e-84 | 12 | 305 | 12 | 282 | Chain A, S-formylglutathione hydrolase [Homo sapiens],3FCX_B Chain B, S-formylglutathione hydrolase [Homo sapiens] |
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3.85e-71 | 12 | 303 | 12 | 277 | S-formylglutathione hydrolase homolog from a psychrophilic bacterium of Shewanella frigidimarina [Shewanella frigidimarina],6JZL_B S-formylglutathione hydrolase homolog from a psychrophilic bacterium of Shewanella frigidimarina [Shewanella frigidimarina] |
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1.12e-70 | 12 | 305 | 13 | 280 | Bromide soaked structure of an esterase from the oil-degrading bacterium Oleispira antarctica [Oleispira antarctica] |
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1.42e-70 | 13 | 303 | 11 | 296 | Crystal Structure Analysis of Yeast Hypothetical Protein: YJG8_YEAST [Saccharomyces cerevisiae],1PV1_B Crystal Structure Analysis of Yeast Hypothetical Protein: YJG8_YEAST [Saccharomyces cerevisiae],1PV1_C Crystal Structure Analysis of Yeast Hypothetical Protein: YJG8_YEAST [Saccharomyces cerevisiae],1PV1_D Crystal Structure Analysis of Yeast Hypothetical Protein: YJG8_YEAST [Saccharomyces cerevisiae] |
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6.40e-69 | 13 | 303 | 11 | 296 | S-formylglutathione hydrolase Variant H160I [Saccharomyces cerevisiae],4FOL_B S-formylglutathione hydrolase Variant H160I [Saccharomyces cerevisiae],4FOL_C S-formylglutathione hydrolase Variant H160I [Saccharomyces cerevisiae],4FOL_D S-formylglutathione hydrolase Variant H160I [Saccharomyces cerevisiae] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1.31e-82 | 12 | 305 | 12 | 282 | S-formylglutathione hydrolase OS=Sus scrofa OX=9823 GN=ESD PE=2 SV=1 |
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1.85e-82 | 12 | 305 | 12 | 282 | S-formylglutathione hydrolase OS=Homo sapiens OX=9606 GN=ESD PE=1 SV=2 |
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8.50e-81 | 12 | 305 | 12 | 282 | S-formylglutathione hydrolase OS=Mus musculus OX=10090 GN=Esd PE=1 SV=1 |
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8.50e-81 | 12 | 305 | 12 | 282 | S-formylglutathione hydrolase OS=Rattus norvegicus OX=10116 GN=Esd PE=2 SV=1 |
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9.69e-80 | 12 | 305 | 12 | 282 | S-formylglutathione hydrolase OS=Bos taurus OX=9913 GN=ESD PE=2 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000056 | 0.000000 |
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