Species | Saprolegnia parasitica | |||||||||||
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Lineage | Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica | |||||||||||
CAZyme ID | SPRG_11756-t26_1-p1 | |||||||||||
CAZy Family | GH6 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CBM47 | 119 | 235 | 1.6e-18 | 0.8984375 |
CBM20 | 4 | 87 | 1.4e-16 | 0.8555555555555555 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
176514 | GDPD_GDE5_like | 3.40e-97 | 597 | 919 | 1 | 293 | Glycerophosphodiester phosphodiesterase domain of mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in mammalian glycerophosphodiester phosphodiesterase GDE5-like proteins. GDE5 is widely expressed in mammalian tissues, with highest expression in spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. |
176549 | GDPD_GDE5 | 2.74e-74 | 597 | 917 | 1 | 288 | Glycerophosphodiester phosphodiesterase domain of putative mammalian glycerophosphodiester phosphodiesterase GDE5 and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in putative mammalian GDE5 and similar proteins. Mammalian GDE5 is widely expressed in mammalian tissues, with highest expression in the spinal chord. Although its biological function remains unclear, mammalian GDE5 shows higher sequence homology to fungal and plant glycerophosphodiester phosphodiesterases (GP-GDEs, EC 3.1.4.46) than to other bacterial and mammalian GP-GDEs. It may also hydrolyze glycerophosphodiesters to sn-glycerol-3-phosphate (G3P) and the corresponding alcohols. In addition to C-terminal GDPD domain, all members in this subfamily have a starch binding domain (CBM20) in the N-terminus, which suggests these proteins may play a distinct role in glycerol metabolism. |
176547 | GDPD_GDE5_like_1_plant | 6.12e-54 | 600 | 919 | 4 | 282 | Glycerophosphodiester phosphodiesterase domain of uncharacterized plant glycerophosphodiester phosphodiesterase-like proteins similar to mammalian GDE5. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in a group of uncharacterized plant glycerophosphodiester phosphodiesterase (GP-PDE)-like proteins. Members in this family show very high sequence homology to mammalian glycerophosphodiester phosphodiesterase GDE5 and are distantly related to plant GP-PDEs. |
176548 | GDPD_YPL110cp_fungi | 2.36e-53 | 599 | 920 | 5 | 278 | Glycerophosphodiester phosphodiesterase domain of Saccharomyces cerevisiae YPL110cp and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in Saccharomyces cerevisiae YPL110cp and other uncharacterized fungal homologs. The product of S. cerevisiae ORF YPL110c (GDE1), YPL110cp (Gde1p), 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 YPL110cp has been characterized as a cytoplasmic glycerophosphocholine (GPC)-specific phosphodiesterase that selectively hydrolyzes GPC, not glycerophosphoinositol (GPI), to generate choline and glycerolphosphate. YPL110cp has multi-domain architecture, including not only C-terminal GDPD, but also an SPX N-terminal domain along with several ankyrin repeats, which implies that YPL110cp may mediate protein-protein interactions in a variety of proteins and play a role in maintaining cellular phosphate levels. Members in this family are distantly related to S. cerevisiae YPL206cp, which selectively catalyzes the cleavage of phosphatidylglycerol (PG), not glycerophosphoinositol (GPI) or glycerophosphocholine (GPC), to diacylglycerol (DAG) and glycerophosphate, and has been characterized as a PG-specific phospholipase C. |
397241 | GDPD | 3.08e-32 | 601 | 920 | 1 | 243 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
1.60e-52 | 516 | 919 | 271 | 628 | |
2.60e-51 | 534 | 919 | 308 | 658 | |
1.24e-49 | 534 | 928 | 322 | 682 | |
4.52e-49 | 534 | 919 | 260 | 617 | |
3.74e-48 | 534 | 928 | 304 | 663 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3.52e-08 | 361 | 462 | 20 | 114 | M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity, cyclic-GMP bound [Mesorhizobium japonicum MAFF 303099],4MUV_B M. loti cyclic-nucleotide binding domain mutant displaying inverted ligand selectivity, cyclic-GMP bound [Mesorhizobium japonicum MAFF 303099] |
|
5.98e-08 | 361 | 462 | 16 | 110 | Chain A, cyclic nucleotide binding domain [Mesorhizobium japonicum MAFF 303099],1U12_B Chain B, cyclic nucleotide binding domain [Mesorhizobium japonicum MAFF 303099] |
|
5.98e-08 | 361 | 462 | 16 | 110 | M.loti ion channel cylic nucleotide binding domain [Mesorhizobium loti],1VP6_C M.loti ion channel cylic nucleotide binding domain [Mesorhizobium loti] |
|
6.24e-08 | 361 | 462 | 18 | 112 | M. loti cyclic-nucleotide binding domain, cyclic-GMP bound [unidentified],3CL1_B M. loti cyclic-nucleotide binding domain, cyclic-GMP bound [unidentified] |
|
6.52e-08 | 361 | 462 | 20 | 114 | Chain A, Mll3241 protein [unidentified],2KXL_A Solution structure of a bacterial cyclic nucleotide-activated K+ channel binding domain in the unliganded state [Mesorhizobium loti] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4.04e-46 | 534 | 921 | 252 | 613 | Glycerophosphocholine phosphodiesterase GPCPD1 OS=Rattus norvegicus OX=10116 GN=Gpcpd1 PE=1 SV=1 |
|
4.19e-46 | 534 | 921 | 255 | 616 | Glycerophosphocholine phosphodiesterase GPCPD1 OS=Mus musculus OX=10090 GN=Gpcpd1 PE=1 SV=1 |
|
5.27e-45 | 537 | 921 | 279 | 649 | Putative glycerophosphocholine phosphodiesterase GPCPD1 homolog 1 OS=Caenorhabditis elegans OX=6239 GN=gpcp-1 PE=3 SV=2 |
|
5.78e-45 | 534 | 921 | 252 | 613 | Glycerophosphocholine phosphodiesterase GPCPD1 OS=Homo sapiens OX=9606 GN=GPCPD1 PE=1 SV=2 |
|
2.45e-43 | 534 | 921 | 337 | 706 | Putative glycerophosphocholine phosphodiesterase GPCPD1 homolog 2 OS=Caenorhabditis elegans OX=6239 GN=gpcp-2 PE=3 SV=1 |
Other | SP_Sec_SPI | CS Position |
---|---|---|
0.998738 | 0.001298 |
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