CAZyme Information: EPrPIT00000022339-p1

Basic Information

• Species: Globisporangium irregulare
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
• CAZyme ID: EPrPIT00000022339-p1
• CAZy Family: GH6
• CAZyme Description: Dolichyl-phosphate beta-glucosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
994		110418.03	6.5932

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486	13869	1223557	65	13804

• Gene Location: location=PirrDAOMBR486_SC0918:403-5368(+)

Full Sequence      

SDGTTFEDRNAWRKYEFETNYTFRNTQKQTLAKAPGKIGGQPFDLSDLDDCEVLLLDQCD
QVQVDNLTNCRVFIGPCSESVFVRNCTNCVFTVACKQLRTRDSSQCSFYLYSLTDPIIET
SQQMRFAPFNGAYNGIERHFAEARLEPTNNHWSQVYDFNDPDKSGENWTILTPQEEAAPW
VVNLDGLVPDSAALGACVNPVSRDSGFIKYTESSSSSSSGMASFSFKTSQKEAEKVMENQ
TESPPVPQQEVAPPAAVSPPVTVTAPPLPVPAPFAVPPPPVAVFSGTATVVHLPPPAPTS
PTVATAASFVENQKVAVIEAVEHLALPLSQAVEPQGVLTKTLPPLERVVSPVVKDEGSDR
PFRKTKARKKKEKKMAPPPRNLASASKRRWFARCWWLGLHVYVYVVLVYSGSLSPQVLST
GGFVFAIAVAVANMSSYVILQTSSPGYVERAEQQADLEAGNTVEDSEHVSDSDSLVPNHD
DQHNKSGDVSGSAGLHFCELCQLTQPLRAKHCKDCEKCVRQYDHHCDCAGTCVGEQNRRK
FVVYLFVQAVEGLVMISVAADAFTLQDNVDEWFKANWLYLIAWFSVFCVLLIAIPLFIYQ
AFLISTNQTSWEHARRSAITYLRSLPDDHSPFDRGCFTNWRVFFCSGDADKWVHILQLQH
MTLCTDSSTLHKKLLNHDEQIMTSADGDAITAESQQLLLLRAAALLVLAPLGVGLALLLH
AFGSLGDERATCTLSVIMPAYNEEDRILVTLKDTVAYLDERRAKDPSFSYEIIVVDDCSQ
DKTVEVVLGEVKKHTVERIRLLRLQKNHGKGGAIRKGVMRARGAKILFADADNATEIRDL
SKLETAIAGNQLQKEGVVVCGSRAHLEEEAIAKRNPIRNLLMHGFHLIVSTLCVRNVRDT
QCGFKLFDRTAARVVFTPMHIERWAFDVELLYIAATRKLSVKEVAVQWREIPGSKLSVVS
ATITMLREIILIRFCYTFGIWKLDDGGFRLAKRQ

Enzyme Prediction     

No EC number prediction in EPrPIT00000022339-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	735	910	2.6e-25	0.9588235294117647

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
240336	PTZ00260	2.26e-112	734	985	72	325	dolichyl-phosphate beta-glucosyltransferase; Provisional
133031	DPG_synthase	1.32e-100	736	955	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	2.99e-53	736	934	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.
400374	TBCC	1.18e-48	40	158	1	119	Tubulin binding cofactor C. Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.
396215	DHHC	4.61e-29	494	615	4	130	DHHC palmitoyltransferase. This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA14548.1|GT2	4.92e-108	722	986	86	351
AAH44127.1|GT2	3.20e-79	722	987	56	321
AHH37954.1|GT2	4.31e-79	722	984	55	317
UJR09417.1|GT2	4.79e-79	727	984	56	312
AFK94129.1|GT2	4.53e-78	728	984	62	321

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BX6_A	3.34e-14	20	171	39	189	Crystal Structure of the human Retinitis Pigmentosa protein 2 (RP2) [Homo sapiens]
3BH6_B	3.40e-14	20	171	41	191	Chain B, Protein XRP2 [Homo sapiens],3BH7_B Crystal structure of the RP2-Arl3 complex bound to GDP-AlF4 [Homo sapiens]
5EKE_A	1.24e-06	727	915	21	192	Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa]
5EKP_A	1.24e-06	727	915	21	192	Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9VLQ1|ALG5_DROME	4.25e-78	727	983	61	318	Dolichyl-phosphate beta-glucosyltransferase OS=Drosophila melanogaster OX=7227 GN=wol PE=1 SV=1
sp|Q54J42|ALG5_DICDI	4.30e-77	720	985	59	327	Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
sp|Q9Y673|ALG5_HUMAN	5.43e-77	728	985	61	319	Dolichyl-phosphate beta-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG5 PE=1 SV=1
sp|Q9DB25|ALG5_MOUSE	2.54e-73	728	985	61	319	Dolichyl-phosphate beta-glucosyltransferase OS=Mus musculus OX=10090 GN=Alg5 PE=1 SV=1
sp|P40350|ALG5_YEAST	3.73e-56	734	982	75	329	Dolichyl-phosphate beta-glucosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000041	0.000000

TMHMM  Annotations     

Start	End
391	413
418	440
541	563
578	600
697	719