y
Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10018226 |
Family | CBM20 |
Protein Properties | Length: 425 Molecular Weight: 48196.1 Isoelectric Point: 4.601 |
Chromosome | Chromosome/Scaffold: 163 Start: 119699 End: 121299 |
Description | Carbohydrate-binding-like fold |
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 |
CBM20 | 96 | 180 | 3.1e-24 |
VRVKFQLQKDCMYGEQFLLVGNHPMIGSRDLKNAVPLSWSDGNIWSVEMDLPVNTTMQYKFIHRGRHGEQIWQPGSDRILKTWEN |
Full Sequence |
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Protein Sequence Length: 425 Download |
MREKIEALTK VSFLPKQCLG KAQLRIPYPS RIAPTDSMFF AVSSPIVQPD ENEINSIRGK 60 DARTFVKSNL THEADVGIEF DTDMPGIQQL WSSEIVRVKF QLQKDCMYGE QFLLVGNHPM 120 IGSRDLKNAV PLSWSDGNIW SVEMDLPVNT TMQYKFIHRG RHGEQIWQPG SDRILKTWEN 180 INMIIVTEDW ENAEEQKIME GKQVLNQLEE LSFQQEITGI ENVMKQSEDW ETGLNPKVQG 240 DQGMNRFEEL TIEQNFALMC ASTASFNQGL VDSPDNRRLE SEDQVQTHKI KGQMKNNSQN 300 EKSITSYQEG SARLDDLFPE KVESTEEAAS QELGSSITDV MIGNDDRTAD FTSDNFSTLA 360 TQTPLGGSNN LCIHTCTCNG IYTLKNVEDE TQIPMIHIEA VTKFHKPSAQ NFPFWITKHY 420 KNLI* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart01065 | CBM_2 | 1.0e-12 | 96 | 179 | 88 | + Starch binding domain. | ||
cd02853 | E_set_MTHase_like_N | 4.0e-13 | 96 | 177 | 82 | + 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. | ||
cd02856 | E_set_GDE_Isoamylase_N | 3.0e-13 | 96 | 190 | 99 | + N-terminal Early set domain associated with the catalytic domain of Glycogen debranching enzyme and bacterial isoamylase (also called glycogen 6-glucanohydrolase). E or "early" set domains are associated with the catalytic domain of the glycogen debranching enzyme at the N-terminal end. Glycogen debranching enzymes have both 4-alpha-glucanotransferase and amylo-1,6-glucosidase activities. As a transferase, it transfers a segment of the 1,4-alpha-D-glucan to a new 4-position in an acceptor, which may be glucose or another 1,4-alpha-D-glucan. As a glucosidase, it catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Bacterial isoamylases are also included in this subfamily. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of glycogen debranching enzyme 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. | ||
pfam00686 | CBM_20 | 2.0e-17 | 96 | 187 | 95 | + Starch binding domain. | ||
cd05467 | CBM20 | 8.0e-20 | 97 | 190 | 97 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0005975 | carbohydrate metabolic process |
GO:2001070 | starch binding |
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 | ACU23169.1 | 2e-36 | 93 | 210 | 90 | 207 | unknown [Glycine max] |
EMBL | CAN60108.1 | 2e-36 | 79 | 207 | 42 | 171 | hypothetical protein [Vitis vinifera] |
EMBL | CBI30404.1 | 4e-36 | 79 | 207 | 66 | 195 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002314109.1 | 8.96831e-44 | 29 | 206 | 22 | 201 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002525630.1 | 3.00004e-41 | 62 | 345 | 509 | 761 | pentatricopeptide repeat-containing protein, putative [Ricinus communis] |
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 | 0.007 | 96 | 173 | 7 | 88 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 1kul_A | 0.007 | 96 | 173 | 7 | 88 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis D172aE217A MUTANT COMPLEXED WITH LACTO-N- Fucopentaose Ii |
PDB | 1acz_A | 0.007 | 96 | 173 | 7 | 88 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, 5 Structures |
PDB | 1ac0_A | 0.007 | 96 | 173 | 7 | 88 | A Chain A, Glucoamylase, Granular Starch-Binding Domain Complex With Cyclodextrin, Nmr, Minimized Average Structure |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FN770891 | 137 | 74 | 210 | 4.99997e-41 |
FS278601 | 108 | 93 | 200 | 8.99998e-41 |
FS272369 | 108 | 93 | 200 | 8.99998e-41 |
FN721082 | 137 | 74 | 210 | 9.99995e-41 |
FN721308 | 137 | 74 | 210 | 9.99995e-41 |
Sequence Alignments (This image is cropped. Click for full image.) |
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