| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 329002 |
| Family | CBM43 |
| Protein Properties | Length: 457 Molecular Weight: 49495.4 Isoelectric Point: 7.8232 |
| Chromosome | Chromosome/Scaffold: 7 Start: 6494159 End: 6495931 |
| 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 | 368 | 451 | 9.2e-34 |
| WCVSNGEVAKEKLQEALDYACGEGGADCRPIQPGATCYHPESLEAHASYAFNSYYQKNSRRVGTCYFGGAAHVVTQPPRYGKCE | |||
| GH17 | 26 | 344 | 0 |
| IGVNYGRIANNLPSPEKVVNLLKSQGINRIKIFDTDKNVLTALANSRIKVIVALPNELLSSAASHQSFADNWIKTHIMSYFPATEIEAIAVGNEVFVDPK NTPYLVSAMKNIHTSLVKYNLDKAIKISSPIALSALANSYPPSSGSFKPDLIEPVIKPMLALLQQTSSFLMVNAYPFFAYAANADKISLDYALFKQNAGN IDSGTGLKYNSLFDAQIDAVYAALSAVGFKGVKVMVTETGWPSVGDENEIGASESTAAAYNGGLVKRVLTGKGTPLRPKEPLNVYLFALFNENQKPGPTS ERNYGMFYPNEGKVYDVPF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 457 Download |
| MAVSFLPCLI LIVSLFSAID AHSGMIGVNY GRIANNLPSP EKVVNLLKSQ GINRIKIFDT 60 DKNVLTALAN SRIKVIVALP NELLSSAASH QSFADNWIKT HIMSYFPATE IEAIAVGNEV 120 FVDPKNTPYL VSAMKNIHTS LVKYNLDKAI KISSPIALSA LANSYPPSSG SFKPDLIEPV 180 IKPMLALLQQ TSSFLMVNAY PFFAYAANAD KISLDYALFK QNAGNIDSGT GLKYNSLFDA 240 QIDAVYAALS AVGFKGVKVM VTETGWPSVG DENEIGASES TAAAYNGGLV KRVLTGKGTP 300 LRPKEPLNVY LFALFNENQK PGPTSERNYG MFYPNEGKVY DVPFSRVRST PVNGNRDHVP 360 VTHEGHTWCV SNGEVAKEKL QEALDYACGE GGADCRPIQP GATCYHPESL EAHASYAFNS 420 YYQKNSRRVG TCYFGGAAHV VTQPPRYGKC EFPTGH* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG5309 | COG5309 | 0.002 | 46 | 335 | 298 | + Exo-beta-1,3-glucanase [Carbohydrate transport and metabolism] | ||
| pfam07983 | X8 | 1.0e-24 | 367 | 439 | 78 | + 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 | 2.0e-38 | 367 | 452 | 86 | + 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 | 1.0e-94 | 26 | 344 | 320 | + 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 | AAL77689.1 | 0 | 21 | 456 | 22 | 460 | AT5g55180/MCO15_13 [Arabidopsis thaliana] |
| GenBank | AAM66024.1 | 0 | 21 | 456 | 22 | 460 | beta-1,3-glucanase-like protein [Arabidopsis thaliana] |
| EMBL | CAB36529.1 | 0 | 1 | 446 | 1 | 445 | putative beta-1, 3-glucanase [Arabidopsis thaliana] |
| RefSeq | NP_194413.2 | 0 | 1 | 456 | 1 | 455 | catalytic/ cation binding / hydrolase, hydrolyzing O-glycosyl compounds [Arabidopsis thaliana] |
| RefSeq | NP_568822.1 | 0 | 21 | 456 | 22 | 460 | glycosyl hydrolase family 17 protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1ghs_B | 0 | 26 | 344 | 1 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 1ghs_A | 0 | 26 | 344 | 1 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 2cyg_A | 0 | 26 | 344 | 1 | 312 | 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 | 26 | 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 | 26 | 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 |
