y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 440606 |
Family | CBM20 |
Protein Properties | Length: 393 Molecular Weight: 42137.4 Isoelectric Point: 4.1585 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM20 | 85 | 169 | 9.7e-25 |
VTTTFMLQKKCDYGERFAVVGASPLLGAWDPAAGVSMDWSEDHVWKCQIDLPVGEQYEYKFVLTSKKAVPEWQPGPNRIFKTDDA |
Full Sequence |
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Protein Sequence Length: 393 Download |
MEKFAAALGV CHRPLVWQQL VGGAVSGSRD SRQGFLQCSC FERRILRHRK AARVLAPRAA 60 RLVLTTASES DDAAVEESEE VMPMVTTTFM LQKKCDYGER FAVVGASPLL GAWDPAAGVS 120 MDWSEDHVWK CQIDLPVGEQ YEYKFVLTSK KAVPEWQPGP NRIFKTDDAE SPLIVSESWE 180 STEMGPSLET GDAPETLSKL VEDILEESTA SAVVEDVLDA AADTVSKLVN EALDKAGENV 240 PELGKTAGGK GVDGTGIVEK EEAGAAAKVA EESEPEKGSK DEQSTNQGKT KSVVTFDNME 300 EDESPDSESS KDTSSESSEE EEGHSASLAV VTPQPECTSD VPEDSKGFKS FKFEAQPATG 360 TKTDHQAENG QPDGIEDDGS VSVPANKEQE IK* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02853 | E_set_MTHase_like_N | 1.0e-13 | 85 | 179 | 96 | + N-terminal Early set domain associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (also called Glycosyltrehalose trehalohydrolase) and similar proteins. E or "early" set domains are associated with the catalytic domain of Maltooligosyl trehalose trehalohydrolase (MTHase) and similar proteins at the N-terminal end. This subfamily also includes bacterial alpha amylases and 1,4-alpha-glucan branching enzymes which are highly similar to MTHase. Maltooligosyl trehalose synthase (MTSase) and MTHase work together to produce trehalose. MTSase is responsible for converting the alpha-1,4-glucosidic linkage to an alpha,alpha-1,1-glucosidic linkage at the reducing end of the maltooligosaccharide through an intramolecular transglucosylation reaction, while MTHase hydrolyzes the penultimate alpha-1,4 linkage of the reducing end, resulting in the release of trehalose. The N-terminal domain of MTHase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase, among others. | ||
cd02861 | E_set_pullulanase_like | 2.0e-14 | 88 | 170 | 85 | + Early set domain associated with the catalytic domain of pullulanase-like proteins. E or "early" set domains are associated with the catalytic domain of pullulanase at either the N-terminal or C-terminal end, and in a few instances at both ends. Pullulanase (also called dextrinase or alpha-dextrin endo-1,6-alpha glucosidase) is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. The E set domain of pullulanase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase. | ||
smart01065 | CBM_2 | 8.0e-15 | 85 | 168 | 88 | + Starch binding domain. | ||
pfam00686 | CBM_20 | 9.0e-17 | 84 | 166 | 86 | + Starch binding domain. | ||
cd05467 | CBM20 | 2.0e-21 | 88 | 179 | 95 | + The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding 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. |
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 | 1kum_A | 0.000000002 | 85 | 179 | 7 | 107 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1kul_A | 0.000000002 | 85 | 179 | 7 | 107 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 1acz_A | 0.000000002 | 85 | 179 | 7 | 107 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, 5 Structures |
PDB | 1ac0_A | 0.000000002 | 85 | 179 | 7 | 107 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure |
PDB | 2vn7_A | 0.003 | 85 | 164 | 497 | 580 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure |
Sequence Alignments (This image is cropped. Click for full image.) |
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