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Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10436655g0010 |
Family | CBM20 |
Protein Properties | Length: 293 Molecular Weight: 31611.1 Isoelectric Point: 4.53 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM20 | 97 | 177 | 8.8e-27 |
VTVKFVLEKKCKFGQQFHVVGDAPQFGSWNPKAAVPLEWSEGDIWTKEVDVPVGKQIEYKFILIGKRGELLWQPGPNRAFE |
Full Sequence |
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Protein Sequence Length: 293 Download |
PNSLADGLDK FGANKNGING RNFINLSKDL RCLPFYVAKH RGSSSRIKVF AQDKTSSEDG 60 REIGIQDDSD KTSSEDGCKI GIHDDLVSLH KDQGPTVTVK FVLEKKCKFG QQFHVVGDAP 120 QFGSWNPKAA VPLEWSEGDI WTKEVDVPVG KQIEYKFILI GKRGELLWQP GPNRAFEASG 180 HVASVVVSSE WELDEILSEA GNEKEVCEAT EMEITGQGIG NENSAATLVE GIFSDVISGL 240 DAVQTGNVIS DPPNGALGSS AKQTEDNTQK KGSVIDLSGP PDAPGLRTER NEE 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd02861 | E_set_pullulanase_like | 3.0e-17 | 99 | 176 | 80 | + 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. | ||
cd02853 | E_set_MTHase_like_N | 9.0e-18 | 97 | 176 | 80 | + 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-20 | 97 | 174 | 82 | + Starch binding domain. | ||
pfam00686 | CBM_20 | 1.0e-21 | 96 | 176 | 84 | + Starch binding domain. | ||
cd05467 | CBM20 | 1.0e-23 | 99 | 177 | 82 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABK25218.1 | 0 | 1 | 293 | 14 | 307 | unknown [Picea sitchensis] |
EMBL | CAN60108.1 | 1e-28 | 91 | 196 | 53 | 158 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_001768545.1 | 2e-29 | 93 | 211 | 99 | 224 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001770618.1 | 1e-29 | 93 | 192 | 107 | 207 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002322974.1 | 6e-29 | 80 | 192 | 81 | 193 | predicted protein [Populus trichocarpa] |
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 | 1ded_B | 0.00000005 | 71 | 192 | 564 | 685 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 1ded_A | 0.00000005 | 71 | 192 | 564 | 685 | X Chain X, Crystal Structure Of The Full-Length Autotransporter Esta From Pseudomonas Aeruginosa |
PDB | 1d7f_B | 0.00000005 | 71 | 192 | 564 | 685 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1d7f_A | 0.00000005 | 71 | 192 | 564 | 685 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
PDB | 1v3l_B | 0.00000005 | 71 | 192 | 564 | 685 | A Chain A, Crystal Structure Of Asparagine 233-Replaced Cyclodextrin Glucanotransferase From Alkalophilic Bacillus Sp. 1011 Determined At 1.9 A Resolution |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EX312391 | 275 | 19 | 293 | 0 |
EX311925 | 263 | 1 | 262 | 0 |
EX408057 | 261 | 1 | 260 | 0 |
EX330963 | 252 | 1 | 252 | 0 |
EX409215 | 253 | 1 | 252 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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