y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00049022m |
Family | CBM20 |
Protein Properties | Length: 335 Molecular Weight: 36577.4 Isoelectric Point: 3.8949 |
Chromosome | Chromosome/Scaffold: 071370 Start: 2405 End: 4632 |
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 | 68 | 153 | 4.7e-23 |
VRVRFVLEEQGALDQSVYLVGDDPALGIWDPANAIPLELAESHGWILEKDLPANKLIEFKFLLRDSSGKLNWQNGPNRIFQTGETV |
Full Sequence |
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Protein Sequence Length: 335 Download |
VGAGGLAARG RRRRALVAVA SLHEPLPSRA QEGHVPAAPQ ANEEEVHGMI GSAAAETSSP 60 PVVSGKTVRV RFVLEEQGAL DQSVYLVGDD PALGIWDPAN AIPLELAESH GWILEKDLPA 120 NKLIEFKFLL RDSSGKLNWQ NGPNRIFQTG ETVNTLVVYE DWGDVKKQKI AEEVGVASVG 180 IEEVVVTDDS ESRDESVQAV VLEDELQMDD DQVVNEVNED ESFVAEDDEN LAVPTNESVQ 240 EDSLKTNEAN PQEPMMQKEP EIIEDLHEMV DMENGSALCA DENSAEKTEE DDILSEDGVP 300 VENGLTSTYE HDLLWGWRAL QELLMNLGIK MDTT* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02851 | E_set_GO_C | 5.0e-14 | 68 | 162 | 100 | + C-terminal Early set domain associated with the catalytic domain of galactose oxidase. E or "early" set domains are associated with the catalytic domain of galactose oxidase at the C-terminal end. Galactose oxidase is an extracellular monomeric enzyme which catalyzes the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalyzing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. The second redox active center necessary for the reaction was found to be situated at a tyrosine residue. The C-terminal domain of galactose oxidase 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. | ||
cd02853 | E_set_MTHase_like_N | 8.0e-17 | 68 | 162 | 95 | + 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. | ||
smart01065 | CBM_2 | 2.0e-17 | 68 | 151 | 88 | + Starch binding domain. | ||
pfam00686 | CBM_20 | 2.0e-22 | 67 | 158 | 95 | + Starch binding domain. | ||
cd05467 | CBM20 | 4.0e-24 | 69 | 162 | 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 |
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 | ACG39865.1 | 0 | 23 | 334 | 56 | 360 | starch binding domain containing protein [Zea mays] |
GenBank | EEC79312.1 | 0 | 7 | 334 | 39 | 373 | hypothetical protein OsI_20148 [Oryza sativa Indica Group] |
RefSeq | NP_001055691.1 | 0 | 7 | 334 | 39 | 373 | Os05g0446900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001146081.1 | 0 | 23 | 334 | 56 | 361 | hypothetical protein LOC100279613 [Zea mays] |
RefSeq | XP_002441189.1 | 0 | 16 | 334 | 46 | 369 | hypothetical protein SORBIDRAFT_09g021950 [Sorghum bicolor] |
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 | 1uks_B | 0.000000000007 | 35 | 162 | 553 | 684 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
PDB | 1uks_A | 0.000000000007 | 35 | 162 | 553 | 684 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
PDB | 1v3m_B | 0.000000000007 | 35 | 162 | 553 | 684 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
PDB | 1v3m_A | 0.000000000007 | 35 | 162 | 553 | 684 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
PDB | 1v3k_B | 0.000000000007 | 35 | 162 | 553 | 684 | A Chain A, Crystal Structure Of F283y Mutant Cyclodextrin Glycosyltransferase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FL820581 | 236 | 25 | 260 | 0 |
JG950808 | 229 | 107 | 335 | 0 |
JG819818 | 253 | 83 | 335 | 0 |
FE622899 | 218 | 116 | 333 | 0 |
FL820581 | 22 | 257 | 278 | 0.29 |
Sequence Alignments (This image is cropped. Click for full image.) |
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