CAZyme Information: SDRG_16101-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_16101-t26_1-p1
• CAZy Family: GT41
• CAZyme Description: dolichyl-phosphate beta-glucosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
330		36401.47	7.4184

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SdiclinaVS20	17448	1156394	89	17359

• Gene Location: location=JH767244:28223-29361(-)

Full Sequence      

MLPLPVVAVVVVGAGALLLLPLLRWFFAPVTMAKAYAAAHDATKYRSYTDPTTPGTTLVF
PCLSAPATRCLSLIVPAFNEEERIEPMLDETIAYLEGRAAADASFTYEIIVVDDCSTDKT
VAVVEGHIRRHGVDKLKLLRLESNHGKGGAVRMGVLKASGEIILMADADAATKIDDFSKL
EALWTTKGKGATSGVVVCGSRAHLEGEATAKRHPLRNVLMHGFHWIVATLCVNDIRDTQC
GFKLFDRKAAQLLFPPLHIERWGFDVELLYLAHKLRIPCYEVAVRWQEIPGSKLNVIDAT
FSMLREMLLIPLCYNLGVWRTNDGAYRLQA

Enzyme Prediction     

No EC number prediction in SDRG_16101-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	72	223	7.8e-26	0.8117647058823529

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
240336	PTZ00260	1.15e-112	71	326	72	328	dolichyl-phosphate beta-glucosyltransferase; Provisional
133031	DPG_synthase	1.31e-107	73	293	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	2.92e-58	73	272	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	3.61e-25	72	249	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	1.33e-23	73	253	1	162	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA14548.1|GT2	8.71e-104	22	324	44	351
AFK11342.1|GT2	9.63e-90	60	319	61	320
AFP05192.1|GT2	9.94e-90	60	319	62	321
BAN20766.1|GT2	9.98e-89	32	329	30	335
AAF52633.1|GT2|2.4.1.117	3.22e-87	57	320	54	317

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5TZE_C	7.74e-09	72	169	4	93	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]
5TZ8_A	1.07e-08	72	169	4	93	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]
6YV7_A	1.35e-06	71	201	45	166	Mannosyltransferase PcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6YV7_B	1.35e-06	71	201	44	165	Mannosyltransferase PcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548]
6P61_A	3.13e-06	71	180	15	113	Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9VLQ1|ALG5_DROME	5.73e-88	57	320	54	317	Dolichyl-phosphate beta-glucosyltransferase OS=Drosophila melanogaster OX=7227 GN=wol PE=1 SV=1
sp|Q9Y673|ALG5_HUMAN	3.17e-84	68	320	64	316	Dolichyl-phosphate beta-glucosyltransferase OS=Homo sapiens OX=9606 GN=ALG5 PE=1 SV=1
sp|Q9DB25|ALG5_MOUSE	2.55e-83	68	320	64	316	Dolichyl-phosphate beta-glucosyltransferase OS=Mus musculus OX=10090 GN=Alg5 PE=1 SV=1
sp|Q54J42|ALG5_DICDI	8.98e-82	71	320	76	324	Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1
sp|O60061|ALG5_SCHPO	2.23e-60	71	319	64	313	Dolichyl-phosphate beta-glucosyltransferase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg5 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000034	0.000014

TMHMM  Annotations     

Start	End
5	27