Q4X162
Gene name |
alg10 (AFUA_2G11080) |
Protein name |
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase |
Names |
Alpha-1,2-glucosyltransferase alg10, Alpha-2-glucosyltransferase alg10, Asparagine-linked glycosylation protein 10, Dolichyl-phosphoglucose-dependent glucosyltransferase alg10 |
Species |
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
KEGG Pathway |
afm:AFUA_2G11080 |
EC number |
2.4.1.256: 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 Q4X162
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q4X162-F1 | Predicted | AlphaFoldDB |
No variants for Q4X162
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q4X162 | |||||
No associated diseases with Q4X162
No regional properties for Q4X162
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q4X162 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.256 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| 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 Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | Catalysis of the addition of the third 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(2)Man(9)GlcNAc(2)-PP-Dol. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dolichol-linked oligosaccharide biosynthetic process | The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P. |
| 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 |
| MSAVRPVSGI | SLAARYAVPF | VLLLIPLWMA | KVNTVVPDPY | LDEVFHVPQA | QAYWDHRWFH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WDPKITTPPG | LYIWSYILCA | AALVLRGSPK | ELNAGALRAT | NVAAAAVFLP | WRLQTLLDAL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RKVRNTRPSG | AWLSHTVLNI | CLFPPLFFFS | GLYYTDIVSL | LAVIEAYNWD | IKRSAGSWSL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKTAVFVATG | LTALVLRQTN | IFWVAIFLGG | LQVVRRLRQS | SKASQASSLL | QIIQSGFNNE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LYDPLVSEAS | FFDYVKTSIS | LVSVGLRNFI | PIIISTVPYL | VILAAFGGFV | LWNDGVVLGH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEFHTAGLHL | SQMLYIWPYF | MFFSWPILIF | PVINLVLPNS | VIPAFFDYGF | TKKQKGLPRI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WTALVIIPIM | LAVVHFNTII | HPFTLADNRH | YIFYVFRILR | SHPAIRYAAV | PTAYFVGGWA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VISAFGFSTT | KPQPQFVPIT | KSNELAAAQK | GQLKEAARKK | EKSERKSKSK | KASQVTASPP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AQDQFSPEVL | ARIQEHLAQR | QKQQQEVPRA | SFVLVWLAAT | ALSLVTAPLV | EPRYFIIPWV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MWRLHLPPQP | VPLVYRQQRP | RDEREALHAD | LATNFSLFME | TYWFLAINAA | TGYIFLYKGF |
| 610 | |||||
| EWPQEPGKVQ | RFMW |