Species | Trichosporon asahii | |||||||||||
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Lineage | Basidiomycota; Tremellomycetes; ; Trichosporonaceae; Trichosporon; Trichosporon asahii | |||||||||||
CAZyme ID | EJT46649.1 | |||||||||||
CAZy Family | AA6 | |||||||||||
CAZyme Description | 1,3-beta-glucanosyltransferase [Source:UniProtKB/TrEMBL;Acc:J6EQA2] | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH5 | 116 | 281 | 9.6e-33 | 0.5676567656765676 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
397351 | Glyco_hydro_72 | 5.32e-35 | 299 | 410 | 29 | 127 | Glucanosyltransferase. This is a family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases. The active site residues in the Aspergillus fumigatus example are the two glutamate residues at 160 and 261. |
176512 | GDPD_YPL206cp_fungi | 3.98e-25 | 64 | 114 | 1 | 51 | Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL206cp and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL206cp and uncharacterized hypothetical homologs existing in fungi. The product of S. cerevisiae ORF YPL206c (PGC1), YPL206cp (Pgc1p), displays homology to bacterial and mammalian glycerophosphodiester phosphodiesterases (GP-GDE, EC 3.1.4.46), which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. S. cerevisiae YPL206cp is an integral membrane protein with a single GDPD domain following by a short hydrophobic C-terminal tail that may function as a membrane anchor. This protein plays an essential role in the regulation of the cardiolipin (CL) biosynthetic pathway in yeast by removing the excess phosphatidylglycerol (PG) content of membranes via a phospholipase C-type degradation mechanism. YPL206cp has been characterized as a PG-specific phospholipase C that selectively catalyzes the cleavage of PG, not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate. Members in this family are distantly related to S. cerevisiae YPL110cp, which selectively hydrolyzes glycerophosphocholine (GPC), not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate, and has been characterized as a cytoplasmic GPC-specific phosphodiesterase. |
176499 | GDPD | 1.30e-19 | 64 | 158 | 1 | 108 | Glycerophosphodiester phosphodiesterase domain as found in prokaryota and eukaryota, and similar proteins. The typical glycerophosphodiester phosphodiesterase domain (GDPD) consists of a TIM barrel and a small insertion domain named the GDPD-insertion (GDPD-I) domain, which is specific for GDPD proteins. This family corresponds to both typical GDPD domain and GDPD-like domain which lacks the GDPD-I region. Members in this family mainly consist of a large family of prokaryotic and eukaryotic glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46), and a number of uncharacterized homologs. Sphingomyelinases D (SMases D) (sphingomyelin phosphodiesterase D, EC 3.1.4.41) from spider venom, SMases D-like proteins, and phospholipase D (PLD) from several pathogenic bacteria are also included in this family. GDPD plays an essential role in glycerol metabolism and catalyzes the hydrolysis of glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols are major sources of carbon and phosphate. Its catalytic mechanism is based on the metal ion-dependent acid-base reaction, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). Both, GDPD related proteins and PI-PLCs, belong to the superfamily of PI-PLC-like phosphodiesterases. |
397241 | GDPD | 1.81e-18 | 67 | 156 | 1 | 85 | Glycerophosphoryl diester phosphodiesterase family. E. coli has two sequence related isozymes of glycerophosphoryl diester phosphodiesterase (GDPD) - periplasmic and cytosolic. This family also includes agrocinopine synthase, the similarity to GDPD has been noted. This family appears to have weak but not significant matches to mammalian phospholipase C pfam00388, which suggests that this family may adopt a TIM barrel fold. |
176506 | GDPD_TtGDE_like | 2.43e-18 | 66 | 110 | 5 | 49 | Glycerophosphodiester phosphodiesterase domain of Thermoanaerobacter tengcongensis and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Thermoanaerobacter tengcongensis glycerophosphodiester phosphodiesterase (TtGDE, EC 3.1.4.46) and its uncharacterized homologs. Members in this family show high sequence similarity to Escherichia coli GP-GDE, which catalyzes the degradation of glycerophosphodiesters to produce sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. Despite the fact that most of GDPD family members exist as the monomer, TtGDE can function as a dimeric unit. Its catalytic mechanism is based on the general base-acid catalysis, which is similar to that of phosphoinositide-specific phospholipases C (PI-PLCs, EC 3.1.4.11). A divalent metal cation is required for the enzyme activity of TtGDE. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
2.12e-48 | 116 | 282 | 364 | 535 | |
3.37e-48 | 116 | 282 | 435 | 606 | |
2.23e-47 | 116 | 282 | 422 | 593 | |
2.90e-46 | 116 | 282 | 432 | 603 | |
2.90e-46 | 116 | 282 | 432 | 603 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.33e-19 | 299 | 407 | 53 | 155 | SACCHAROMYCES CEREVISIAE GAS2P (E176Q MUTANT) IN COMPLEX WITH LAMINARITETRAOSE AND LAMINARIPENTAOSE [Saccharomyces cerevisiae] |
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3.33e-19 | 299 | 407 | 53 | 155 | Saccharomyces cerevisiae Gas2p in complex with laminaripentaose [Saccharomyces cerevisiae],2W63_A Saccharomyces Cerevisiae Gas2p In Complex With Laminaritriose And Laminaritetraose [Saccharomyces cerevisiae],5O9O_A Crystal structure of ScGas2 in complex with compound 7. [Saccharomyces cerevisiae S288C],5O9P_A Crystal structure of Gas2 in complex with compound 10 [Saccharomyces cerevisiae S288C],5O9Q_A Crystal structure of ScGas2 in complex with compound 6 [Saccharomyces cerevisiae S288C],5O9R_A Crystal structure of ScGas2 in complex with compound 9 [Saccharomyces cerevisiae S288C],5O9Y_A Crystal structure of ScGas2 in complex with compound 11 [Saccharomyces cerevisiae S288C],5OA2_A Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_B Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_C Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA6_A Crystal structure of ScGas2 in complex with compound 12 [Saccharomyces cerevisiae S288C] |
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3.33e-19 | 299 | 407 | 53 | 155 | Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) [Saccharomyces cerevisiae] |
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6.51e-14 | 125 | 259 | 176 | 305 | Exo-b-(1,3)-glucanase From Candida Albicans [Candida albicans] |
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6.51e-14 | 125 | 259 | 176 | 305 | Exo-b-(1,3)-glucanase From Candida Albicans At 1.85 A Resolution [Candida albicans],1EQC_A Exo-b-(1,3)-glucanase From Candida Albicans In Complex With Castanospermine At 1.85 A [Candida albicans] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
9.70e-24 | 299 | 407 | 56 | 154 | 1,3-beta-glucanosyltransferase gel4 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gel4 PE=3 SV=1 |
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9.70e-24 | 299 | 407 | 56 | 154 | 1,3-beta-glucanosyltransferase gel4 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=gel4 PE=1 SV=1 |
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9.26e-19 | 299 | 407 | 40 | 136 | 1,3-beta-glucanosyltransferase gas1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas1 PE=1 SV=1 |
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1.71e-18 | 299 | 407 | 53 | 155 | 1,3-beta-glucanosyltransferase GAS2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAS2 PE=1 SV=1 |
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3.45e-18 | 125 | 259 | 212 | 342 | Glucan 1,3-beta-glucosidase OS=Pichia angusta OX=870730 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
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1.000045 | 0.000001 |
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