Q2ULB2
Gene name |
mns1B (manA, msdS, AO090003000476) |
Protein name |
Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B |
Names |
Class I alpha-mannosidase 1B, Man(9)-alpha-mannosidase 1B |
Species |
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
KEGG Pathway |
aor:AO090003000476 |
EC number |
3.2.1.113: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
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 Q2ULB2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2ULB2-F1 | Predicted | AlphaFoldDB |
No variants for Q2ULB2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2ULB2 | |||||
No associated diseases with Q2ULB2
No regional properties for Q2ULB2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q2ULB2 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.2.1.113 | Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasmic vesicle lumen | The volume enclosed by a cytoplasmic vesicle. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | Catalysis of the hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in an oligo-mannose oligosaccharide. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
| ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHFSSLSLPL | TALSLVTPSL | AYPQFKFEQR | VARSNSSESR | ANAVKEAFVH | AWDGYMQYAY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PHDELHPISN | GVGDSRNGWG | ASAVDALSTA | VIMGNETIVN | QILDHIATID | YSKTDDQVSL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FETTIRYLGG | MLSGYDLLKG | PASNLVKDQA | KVKTLLDQSQ | NLADVLKFAF | DTPSGIPYNN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| INITSHGNDG | ATTNGLAVTG | TLVLEWTRLS | DLTGDTEYAQ | LSQKAEDYLL | NPSPKSAEPF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGLVGSHINI | SNGAFADGQV | SWNGGDDSFY | EYLIKMYVYD | PKRFSTYGDR | WVKAAESSIK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HLASHPEKRP | DLTFLASYND | GQYGLSSQHL | TCFDGGSFLL | GGTVLDRDDF | IQFGLDLVKG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| CHETYNQTLT | GIGPESFGWD | PKNVPSDQKE | LYERAGFYIS | SGAYILRPEV | IESFYYAWRI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TGQEIYREWV | WNAFVNINKY | CRTDSGFAGL | TNVNAANGGG | RYDNQESFLF | AEVLKYVYLT |
| 490 | 500 | ||||
| FAPDNEWQVQ | RGKGNKFVYN | TEAHPVRVAA |