| Analysis | rpsblast_cdd | Start | 98 |
| End | 170 | Strand | + |
| Length | 73 | Note | Gaps:3 |
| Hit Coverage | 80.00 | Hit Length | 95 |
| Hit Pident | 31.58 | E Val | 6e-07 |
| Hit Description | cd05808 CBM20_alpha_amylase Alpha-amylase C-terminal CBM20 (carbohydrate-binding module family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have in addition to the C-terminal CBM20 domain an N-terminal catalytic domain belonging to glycosyl hydrolase family 13 which hydrolyzes internal alpha-1 4-glucosidic bonds in starch and related saccharides yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase beta-amylase glucoamylase and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.. | Hit Pcons | 21.05 |
| Name | Qrob_P0255590.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0255590.2 | Quercus robur | 100.0 | egn | (M=4) 2.7.9.5 - Phosphoglucan, water dikinase. | EC:2.7.9.5 | validated |
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