| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 480794 |
| Family | CBM43 |
| Protein Properties | Length: 453 Molecular Weight: 48878.6 Isoelectric Point: 4.5527 |
| Chromosome | Chromosome/Scaffold: 3 Start: 23178500 End: 23181084 |
| Description | O-Glycosyl hydrolases family 17 protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM43 | 366 | 444 | 1.2e-29 |
| WCVPKEDATQEQLQDSLDWVCGQGIDCGPIMPGGVCFEPNNLVSHTAYAMNLYFQKSPENPMDCDFSKAARITSENPSK | |||
| GH17 | 25 | 342 | 0 |
| IGVNYGLLADNLPPPSETAKLLQSTSIEKVRLYNADPSIIKSLAGTDIGIVIGVANGDLPSIASDFNVASQWINSNVLPFYPASNIILINVGNEVLLSND LNLVNQLLPAMQNVQKALEAVSLGRKIKVSTVHAMTVLGNSEPPSAGSFAPSYQAGLKGILQFLSDTESPFAINPYPFFAYQSDPRPETLAFCLFQPNPG RVDSNTGIKYMNMFDAQVDAVHSALKSMGFEKVEVLVAETGWPSTGDNNEVGPSVENAKAYNGNLIAHLRSMVGTPLMPGKSIDTYIFALFDENLKPGPS FERSFGLFKPDLSMAYDI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 453 Download |
| MALSIFFHLL FILFSVSPSN AQSFIGVNYG LLADNLPPPS ETAKLLQSTS IEKVRLYNAD 60 PSIIKSLAGT DIGIVIGVAN GDLPSIASDF NVASQWINSN VLPFYPASNI ILINVGNEVL 120 LSNDLNLVNQ LLPAMQNVQK ALEAVSLGRK IKVSTVHAMT VLGNSEPPSA GSFAPSYQAG 180 LKGILQFLSD TESPFAINPY PFFAYQSDPR PETLAFCLFQ PNPGRVDSNT GIKYMNMFDA 240 QVDAVHSALK SMGFEKVEVL VAETGWPSTG DNNEVGPSVE NAKAYNGNLI AHLRSMVGTP 300 LMPGKSIDTY IFALFDENLK PGPSFERSFG LFKPDLSMAY DIGLTKTTSS QTSQSPQLGK 360 ATSMGWCVPK EDATQEQLQD SLDWVCGQGI DCGPIMPGGV CFEPNNLVSH TAYAMNLYFQ 420 KSPENPMDCD FSKAARITSE NPSKLFSSSY FI* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG5309 | COG5309 | 6.0e-12 | 17 | 335 | 332 | + Exo-beta-1,3-glucanase [Carbohydrate transport and metabolism] | ||
| pfam07983 | X8 | 7.0e-21 | 366 | 435 | 75 | + X8 domain. The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteristic of GPI-anchored domains. | ||
| smart00768 | X8 | 1.0e-35 | 366 | 443 | 78 | + Possibly involved in carbohydrate binding. The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges. | ||
| pfam00332 | Glyco_hydro_17 | 2.0e-103 | 25 | 342 | 318 | + Glycosyl hydrolases family 17. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAD22313.1 | 0 | 18 | 452 | 18 | 452 | putative beta-1,3-glucanase [Arabidopsis thaliana] |
| GenBank | ABK95837.1 | 0 | 1 | 443 | 1 | 441 | unknown [Populus trichocarpa] |
| RefSeq | NP_179219.4 | 0 | 18 | 443 | 18 | 443 | catalytic/ cation binding / hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| RefSeq | NP_195174.6 | 0 | 1 | 443 | 1 | 441 | catalytic/ cation binding / hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| RefSeq | XP_002509479.1 | 0 | 19 | 443 | 22 | 449 | Glucan endo-1,3-beta-glucosidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2cyg_A | 0 | 25 | 342 | 1 | 310 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
| PDB | 3f55_D | 0 | 25 | 345 | 2 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
| PDB | 3f55_C | 0 | 25 | 345 | 2 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
| PDB | 3f55_B | 0 | 25 | 345 | 2 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
| PDB | 3f55_A | 0 | 25 | 345 | 2 | 316 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
