| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10022641m |
| Family | CBM43 |
| Protein Properties | Length: 527 Molecular Weight: 56706.6 Isoelectric Point: 4.7488 |
| Chromosome | Chromosome/Scaffold: 11 Start: 3967991 End: 3972326 |
| Description | O-Glycosyl hydrolases family 17 protein |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CBM43 | 383 | 464 | 1.2e-30 |
| WCVPKEDATEEQLQASLDWVCGQGIDCRPIMPGGACFEPNNIASHAAYAMNLNFQKSPENPTDCDFSQTARITSDNPSYNNC | |||
| GH17 | 41 | 358 | 0 |
| IGVNYGLLADNLPPPSDTAKLLQSTSIQKVRLYGADPTIIKSLAGTGVEIVIGVANGDLPSLASDVNVASQWIDVNVLPFYPASKIILINVGNEILLSND LNLVNQLLPAMQNVHKALEAVSLGGKIKVSTVHAMTVLGQSEPPSAGLFAPSYQAGLKGILQFLSDTGSSFVINPYPFFAYLSDPRPETLSFCLFQPNPG RVDSNTGIKYMNMFDAQVDAVHSALKSMGFEKVEVVVAETGWPTSGDINEVGPSVENAKAYNGNLIAHLRSMVGTPLMPGKSVDTYTFALFDENLKPGPS FERSFGLFKPDLSMAYDI | |||
| Full Sequence |
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| Protein Sequence Length: 527 Download |
| MIKSLAMSFL PHSYASMALS IFFFLLLILF SVSSGNAQSY IGVNYGLLAD NLPPPSDTAK 60 LLQSTSIQKV RLYGADPTII KSLAGTGVEI VIGVANGDLP SLASDVNVAS QWIDVNVLPF 120 YPASKIILIN VGNEILLSND LNLVNQLLPA MQNVHKALEA VSLGGKIKVS TVHAMTVLGQ 180 SEPPSAGLFA PSYQAGLKGI LQFLSDTGSS FVINPYPFFA YLSDPRPETL SFCLFQPNPG 240 RVDSNTGIKY MNMFDAQVDA VHSALKSMGF EKVEVVVAET GWPTSGDINE VGPSVENAKA 300 YNGNLIAHLR SMVGTPLMPG KSVDTYTFAL FDENLKPGPS FERSFGLFKP DLSMAYDIGL 360 TKTTSSQASQ SPPLGKETTS TGWCVPKEDA TEEQLQASLD WVCGQGIDCR PIMPGGACFE 420 PNNIASHAAY AMNLNFQKSP ENPTDCDFSQ TARITSDNPS YNNCVYPRAG EVGEVGDGSI 480 KGVMNKYVTS DKAMDQNCSE CSSFLSLPIF IISFSFFFHF HSLRIM* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG5309 | COG5309 | 1.0e-10 | 69 | 351 | 291 | + Exo-beta-1,3-glucanase [Carbohydrate transport and metabolism] | ||
| pfam07983 | X8 | 1.0e-19 | 383 | 452 | 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 | 3.0e-37 | 383 | 466 | 84 | + 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 | 4.0e-100 | 41 | 358 | 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 | 36 | 460 | 20 | 443 | putative beta-1,3-glucanase [Arabidopsis thaliana] |
| GenBank | ABK95331.1 | 0 | 17 | 467 | 1 | 452 | unknown [Populus trichocarpa] |
| RefSeq | NP_179219.4 | 0 | 36 | 526 | 20 | 503 | catalytic/ cation binding / hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| RefSeq | NP_195174.6 | 0 | 17 | 497 | 1 | 478 | catalytic/ cation binding / hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| RefSeq | XP_002509479.1 | 0 | 37 | 467 | 24 | 456 | 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 | 41 | 358 | 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 | 41 | 361 | 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 | 41 | 361 | 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 | 41 | 361 | 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 | 41 | 361 | 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 |
