dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: H257_11201-t26_3-p1

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Basic Information help

Species

Aphanomyces astaci

Lineage

Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci

CAZyme ID

H257_11201-t26_3-p1

CAZy Family

GT19

CAZyme Description

hypothetical protein, variant 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
311		34767.31	7.4188

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

Gene Location

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in H257_11201-t26_3-p1.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GT2	52	232	1.6e-24	0.9705882352941176

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
240336	PTZ00260	8.67e-107	50	305	71	325	dolichyl-phosphate beta-glucosyltransferase; Provisional
133031	DPG_synthase	1.56e-98	53	275	1	211	DPG_synthase is involved in protein N-linked glycosylation. UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.
133022	DPM_DPG-synthase_like	2.14e-53	53	254	1	185	DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.
395426	Glycos_transf_2	4.43e-22	52	231	1	163	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
133030	DPM1_like_bac	2.32e-19	53	233	1	160	Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
1.06e-92	27	306	73	351
3.76e-81	37	304	49	312
8.37e-79	40	305	23	289
6.59e-76	43	304	62	323
6.59e-76	43	304	62	323

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2.12e-08	52	167	4	107	Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus]
2.84e-08	52	167	4	107	Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.84e-79	40	305	61	327	Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
1.03e-74	25	305	40	319	Dolichyl-phosphate beta-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG5 PE=1 SV=1
1.23e-73	35	303	52	318	Dolichyl-phosphate beta-glucosyltransferase OS=Drosophila melanogaster OX=7227 GN=wol PE=1 SV=1
3.28e-73	25	305	40	319	Dolichyl-phosphate beta-glucosyltransferase OS=Mus musculus OX=10090 GN=Alg5 PE=1 SV=1
4.12e-55	51	302	64	314	Dolichyl-phosphate beta-glucosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg5 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM Annotations help

There is no transmembrane helices in H257_11201-t26_3-p1.