Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi3g33257.1 |
Family | GH17 |
Protein Properties | Length: 352 Molecular Weight: 39836.2 Isoelectric Point: 5.291 |
Chromosome | Chromosome/Scaffold: 3 Start: 35637788 End: 35639694 |
Description | Glycosyl hydrolase superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH17 | 3 | 205 | 0 |
LTQALKSEGFPSIRVSTPHYLGILAPSDGIPSNATFRASYNTELFPSMLQFHRDTKPPFMVNPYPYFSYNPQTLNYALFRPNARIYDPATKLNYTSMFEA QMDAIYTAMVKLGYGDVEVAIGEAGWPTQAEADQVGVGVKEAQDFNEGMLRVCSSGKGTPLMPNRTFETYLFSLFDENQKPGPVDERHFGLFNPDFTPVY DLR |
Full Sequence |
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Protein Sequence Length: 352 Download |
MRLTQALKSE GFPSIRVSTP HYLGILAPSD GIPSNATFRA SYNTELFPSM LQFHRDTKPP 60 FMVNPYPYFS YNPQTLNYAL FRPNARIYDP ATKLNYTSMF EAQMDAIYTA MVKLGYGDVE 120 VAIGEAGWPT QAEADQVGVG VKEAQDFNEG MLRVCSSGKG TPLMPNRTFE TYLFSLFDEN 180 QKPGPVDERH FGLFNPDFTP VYDLRLLTDG KGIFQHDWLV FSSVKNEVLN SVHTVSFSTV 240 RLWLEKVIEA EKEAARQLVQ QKKRDRALIA LKKKKSQEEL LKQVDTLQMN VEQQMADIEL 300 ARKQKAVLES LKTGNASFES IQSEINIDDV QTLMDDTAEA KAYQDWNLRS L* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03357 | Snf7 | 3.0e-17 | 244 | 345 | 102 | + Snf7. This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localisation, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family. | ||
pfam00332 | Glyco_hydro_17 | 2.0e-50 | 1 | 204 | 210 | + Glycosyl hydrolases family 17. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
GO:0015031 | protein transport |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAX95270.1 | 0 | 2 | 207 | 152 | 357 | glucan endo-1,3-beta-glucosidase precursor (ec 3.2.1.39) ((1-3)-beta-glucan endohydrolase) ((1-3)-beta-glucanase) (beta-1,3-endoglucanase) [Oryza sativa Japonica Group] |
GenBank | AAX95357.1 | 0 | 2 | 207 | 144 | 349 | glucan endo-1,3-beta-glucosidase precursor (ec 3.2.1.39) ((1- |
GenBank | EEC68648.1 | 0 | 2 | 207 | 152 | 357 | hypothetical protein OsI_37085 [Oryza sativa Indica Group] |
GenBank | EEE52578.1 | 0 | 2 | 207 | 152 | 357 | hypothetical protein OsJ_34867 [Oryza sativa Japonica Group] |
Swiss-Prot | P52409 | 0 | 2 | 213 | 142 | 353 | E13B_WHEAT RecName: Full=Glucan endo-1,3-beta-glucosidase; AltName: Full=(1- |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1ghs_B | 9e-33 | 33 | 206 | 139 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 1ghs_A | 9e-33 | 33 | 206 | 139 | 306 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 3ur8_B | 8e-32 | 3 | 206 | 116 | 314 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 3ur8_A | 8e-32 | 3 | 206 | 116 | 314 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
PDB | 3ur7_B | 8e-32 | 3 | 206 | 116 | 314 | A Chain A, Higher-density Crystal Structure Of Potato Endo-1,3-beta-glucanase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GT863077 | 212 | 2 | 213 | 0 |
HX157025 | 212 | 2 | 213 | 0 |
CJ701047 | 212 | 2 | 213 | 0 |
GR338289 | 210 | 2 | 211 | 0 |
CJ699002 | 206 | 2 | 207 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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