Q759R3
Gene name |
ALG8 (ADR210C) |
Protein name |
Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase |
Names |
Asparagine-linked glycosylation protein 8, Dol-P-Glc:Glc(1)Man(9)GlcNAc(2)-PP-dolichyl alpha-1,3-glucosyltransferase, Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase |
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_ADR210C |
EC number |
2.4.1.265: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q759R3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q759R3-F1 | Predicted | AlphaFoldDB |
No variants for Q759R3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q759R3 | |||||
No associated diseases with Q759R3
1 regional properties for Q759R3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoglycoside phosphotransferase | 144 - 438 | IPR002575 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.265 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity | Catalysis of the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation; the transfer of glucose from dolichyl phosphate glucose (Dol-P-Glc) on to the lipid-linked oligosaccharide Glc(1)Man(9)GlcNAc(2)-PP-Dol. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| oligosaccharide-lipid intermediate biosynthetic process | The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation. |
| protein N-linked glycosylation | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKRSEKTEG | ANKSGRRRGP | GSDAEGAEDS | GTRRYSLWNF | WVASTALKLL | LMPGYYSTDF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EVHRNWLAVT | HRLPLREWYV | DATSQWTLDY | PPLFAWFEWA | LSQVVPGAVR | RDGCLELVAE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GRYGWPTVVF | QRLTVIASEV | LLYVVLQVYV | NRSAAQERTV | NFVVATSVAL | SPAFLLVDHI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HFQYNGFLFA | VLVASIVAAR | ERRYVLCGAL | FTVALCLKHI | FLYLAPAYFV | FLLRAYVLDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GEFRFRSYRD | LVFAVRWGNL | CRLGGVVLAI | MAVTFAPFAG | VMPQLMARLF | PFSRGLTHAY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| WAPNFWAIYS | FVDKVLTFLM | LRVPYVYKLA | TSLVQPPLIP | ASIDEIRARM | AAGNHGTRGL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VQDVSFVILP | QIQPKLTFLL | TLFYQVLAVL | PVLFDPSFKR | FIGSLSLCGF | SAFLFGWHVH |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EKAIMLVIVP | FSFLVSFDQR | LLTPFRLLTA | SGYVSLFPLL | YSSSSFVIKV | LYTLIWCIVY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HSALKRTVPA | SASVQRRVFF | FDRLAAVYVM | LLLPMVLGVK | YLELLEGKFE | ALEKYQFLGL |
| 550 | 560 | ||||
| MCYSIYCAIG | VCTSWMGLSW | LYNFDEPLWV |