| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01032751001 |
| Family | GH85 |
| Protein Properties | Length: 643 Molecular Weight: 71966.8 Isoelectric Point: 5.4656 |
| Chromosome | Chromosome/Scaffold: 13 Start: 1027118 End: 1037127 |
| Description | Glycosyl hydrolase family 85 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH85 | 1 | 256 | 0 |
| MDVFVYFSHSLVTLPPPCWTNAAHKHGVKVLGTFITEWDEGRAICNALLSTKESAQMYAERLTELAVALGFDGWLINMEVALAKGQIPNLKEFVSHLTQT MHSSMPGSLVIWYDSVTIDSSLEWQDQLNNKNKPFFDICDGIFINYTWAESYPKISADAAGDRKFDVYMGIDVFGRNTYGGGQWNTNVALDLLKKEEVSA AIFAPGWVYETKQPPDFQTAQNRWWSLIEKSWGIQQKYPRVLPFYSNFDQGHGYHF | |||
| Full Sequence |
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| Protein Sequence Length: 643 Download |
| MDVFVYFSHS LVTLPPPCWT NAAHKHGVKV LGTFITEWDE GRAICNALLS TKESAQMYAE 60 RLTELAVALG FDGWLINMEV ALAKGQIPNL KEFVSHLTQT MHSSMPGSLV IWYDSVTIDS 120 SLEWQDQLNN KNKPFFDICD GIFINYTWAE SYPKISADAA GDRKFDVYMG IDVFGRNTYG 180 GGQWNTNVAL DLLKKEEVSA AIFAPGWVYE TKQPPDFQTA QNRWWSLIEK SWGIQQKYPR 240 VLPFYSNFDQ GHGYHFAIDA VQVSDTPWCN ISCQSFQPFL EFSEDSTNTI QVIVNSKEAS 300 YSGGGNITFK GTLQGNDYFR TRLFLGEILL GNLPVHFTYS LKSDSSSLVG LSLEFSSTLN 360 ERMSVLLAAQ GSTLLTMNQF SSKFSKVIMP HRVVKIEAAP GWVIQESSIA MNGYILTEIH 420 AVCYKSKPDF IDLKLNSGSD HLDNDLARSP SNYYAVLGHL MVKTSDQNPD FLPSSSWLVE 480 VQHIKWASDL QGAKTLSAKI IWKLKDGNYS MSQNYNVYVE KLANEEVGNP GTMLKREQEY 540 LGVAQVEAFY VSDFVVPSGT SSLKFIIQVC GTDGASQKLD DSPYFQLDIE EKELQLAKIL 600 GGYSFQQRMS KLFNKLLLLS LQHLPLMPSW KAATLPEHGG LI* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00598 | GH18_chitinase-like | 0.001 | 20 | 144 | 127 | + The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model. | ||
| COG4724 | COG4724 | 3.0e-33 | 1 | 354 | 390 | + Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism] | ||
| pfam03644 | Glyco_hydro_85 | 9.0e-111 | 1 | 258 | 277 | + Glycosyl hydrolase family 85. Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates. | ||
| cd06547 | GH85_ENGase | 1.0e-119 | 1 | 278 | 298 | + Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005737 | cytoplasm |
| GO:0033925 | mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI25424.1 | 0 | 1 | 642 | 1 | 642 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002273683.1 | 0 | 1 | 590 | 99 | 688 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315137.1 | 0 | 1 | 590 | 103 | 697 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002520781.1 | 0 | 1 | 590 | 104 | 691 | endo beta n-acetylglucosaminidase, putative [Ricinus communis] |
| RefSeq | XP_002520784.1 | 0 | 1 | 590 | 100 | 685 | endo beta n-acetylglucosaminidase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fhq_F | 5e-23 | 2 | 354 | 88 | 465 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
| PDB | 3fhq_D | 5e-23 | 2 | 354 | 88 | 465 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
| PDB | 3fhq_B | 5e-23 | 2 | 354 | 88 | 465 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
| PDB | 3fhq_A | 5e-23 | 2 | 354 | 88 | 465 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
| PDB | 3fha_D | 5e-23 | 2 | 354 | 88 | 465 | A Chain A, Structure Of Endo-Beta-N-Acetylglucosaminidase A |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| JG621224 | 270 | 18 | 286 | 0 |
| GE541456 | 270 | 85 | 353 | 0 |
| EL437937 | 249 | 1 | 249 | 0 |
| EC987223 | 207 | 384 | 590 | 0 |
| DW168655 | 257 | 87 | 342 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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