| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre12.g551200.t1.2 |
| Family | CBM20 |
| Protein Properties | Length: 643 Molecular Weight: 65942.4 Isoelectric Point: 6.7684 |
| Chromosome | Chromosome/Scaffold: 12 Start: 8144104 End: 8150601 |
| Description | Carbohydrate-binding-like fold |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM20 | 61 | 145 | 8.8e-26 |
| VRYRFVVPQYVTHYGQELRVVGSLPELGGWNPWTAPRMSWSDGHQWSLENNLPQETFEFKVIAVEGGHVRWESGSNRVVQTDDDG | |||
| Full Sequence |
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| Protein Sequence Length: 643 Download |
| MHNGHIRTIC RDACGQQRSD RLRNARAVPR PSRYSAVKVL AFQTDLAARD AAPLAKKATS 60 VRYRFVVPQY VTHYGQELRV VGSLPELGGW NPWTAPRMSW SDGHQWSLEN NLPQETFEFK 120 VIAVEGGHVR WESGSNRVVQ TDDDGDIPVE VVVWLTCHFD HTADTGMQLA VPRANVQDAF 180 ETGRAHLEML KKRRSRMSLE TEQVANPVER KRAAAELIRL TEAVVEASTS VHQLGHMLGN 240 APGSGSASDG EGAAAGAGTG TGAAAEDENK VLLMAIDSVR LPKAMRRISF ASVVQARGAG 300 GLEAAAGSDA DAAATAAGAV SPFLRGELDA RAEELMSAAG ALLQEMQQQK QQRQQANGRA 360 KPDTAAPASA EWAELAQEAG HVAEALAHLG APADTQLQLQ GLASVGSALA SGNGNGVHLP 420 SHSAALASPP EALEAVGAAA NDADDVADDA DETVASWDDG PAAAPEADAA AAPRKNKGGP 480 LKQLAANLTG ALPFKLPFNF GSSPPPAVAA SVAAAAPGGS NGTGSTSSGG AARHGIFGTL 540 RTGGVALRPA AARSAAPGGG MSRQPSVATA AAAPAAAGGS VVGLTEAPTH SYASEPTAEV 600 ELSADNGPAA AQVAVEQPGR PKTSKGRKVR TYKGVHRSSK ST* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd02861 | E_set_pullulanase_like | 7.0e-14 | 69 | 154 | 90 | + 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 | 8.0e-17 | 72 | 145 | 76 | + 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 | 8.0e-18 | 61 | 143 | 88 | + Starch binding domain. | ||
| pfam00686 | CBM_20 | 3.0e-19 | 60 | 145 | 91 | + Starch binding domain. | ||
| cd05467 | CBM20 | 5.0e-21 | 62 | 152 | 96 | + 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | EEC79312.1 | 0.00000000003 | 47 | 154 | 86 | 194 | hypothetical protein OsI_20148 [Oryza sativa Indica Group] |
| GenBank | EEE63902.1 | 0.00000000004 | 60 | 154 | 99 | 194 | hypothetical protein OsJ_18727 [Oryza sativa Japonica Group] |
| RefSeq | NP_001055691.1 | 0.00000000003 | 47 | 154 | 86 | 194 | Os05g0446900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_001694129.1 | 0 | 98 | 642 | 1 | 545 | predicted protein [Chlamydomonas reinhardtii] |
| RefSeq | XP_001761619.1 | 0.0000000002 | 37 | 141 | 73 | 182 | predicted protein [Physcomitrella patens subsp. patens] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1cyg_A | 0.000002 | 27 | 141 | 545 | 666 | A Chain A, Cyclodextrin Glucanotransferase (E.C.2.4.1.19) (Cgtase) |
| PDB | 1uks_B | 0.00006 | 61 | 151 | 587 | 682 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| PDB | 1uks_A | 0.00006 | 61 | 151 | 587 | 682 | A Chain A, Crystal Structure Of F183lF259L MUTANT CYCLODEXTRIN Glucanotransferase Complexed With A Pseudo-Maltotetraose Derived From Acarbose |
| PDB | 1ukt_B | 0.00007 | 61 | 151 | 587 | 682 | A Chain A, Crystal Structure Of Y100l Mutant Cyclodextrin Glucanotransferase Compexed With An Acarbose |
| PDB | 1ukt_A | 0.00007 | 61 | 151 | 587 | 682 | A Chain A, Crystal Structure Of Y100l Mutant Cyclodextrin Glucanotransferase Compexed With An Acarbose |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| BQ811422 | 90 | 1 | 90 | 8e-33 |
| BQ811421 | 48 | 596 | 643 | 2e-19 |
| BQ811420 | 42 | 602 | 643 | 0.000000000000002 |
| GW227229 | 106 | 66 | 169 | 0.0000000000005 |
| GW227804 | 106 | 66 | 169 | 0.0000000000005 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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