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CAZyme Information: SPRG_11756-t26_1-p1

You are here: Home > Sequence: SPRG_11756-t26_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Saprolegnia parasitica
Lineage Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
CAZyme ID SPRG_11756-t26_1-p1
CAZy Family GH6
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
939 KK583260|CGC4 102721.69 8.3094
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65 20435 695850 314 20121
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in SPRG_11756-t26_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM47 119 235 1.6e-18 0.8984375
CBM20 4 87 1.4e-16 0.8555555555555555

CDD Domains      download full data without filtering help

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.

CAZyme Hits      help

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

PDB Hits      download full data without filtering help

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]

Swiss-Prot Hits      download full data without filtering help

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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.998738 0.001298

TMHMM  Annotations      help

There is no transmembrane helices in SPRG_11756-t26_1-p1.