| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_002024m |
| Family | GT64 |
| Protein Properties | Length: 781 Molecular Weight: 87871.7 Isoelectric Point: 9.2729 |
| Chromosome | Chromosome/Scaffold: 07413 Start: 45813 End: 51316 |
| Description | glycosyltransferase family protein 47 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT64 | 534 | 770 | 0 |
| FTLLTMTYDARLWNLKMYVKHYSRCSSVKEIVVVWNKGIPPKLSDLDSAVPVRIRVEKKNSLNNRFRKDELIETRAVLELDDDIMMTCDDIERGFNVWRQ HPERIVGFYPRLISGSPLKYRGEKYARKHKGYNMILTGAAFLDSKLAFEMYWGEGAKAGRELVDKYFNCEDVLLNYLYANASTSGTVEYVRPTWAIDTSK FSGAAISRNTQVHYKIRSNCLQKFSEMYGSLSRRKSE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 781 Download |
| MVVPGAVGAG GVGSGAGGTS SPTVGGSCRD VNLKCLFRWR WEYQQHLLHQ RFLSSELVFF 60 LCCLVLYGSI GMLFGWLMFN KPYVGAGGVV GLSSVGCQED NEGSWSIGLF YGNSPFSLKP 120 IETMNVWKNE SAAWPVANPV ITCASVSDSG FASNFVADPF LYVQGDTLYL FYETKNSITM 180 QGDIGVAKST DNGASWQQLG IALDEEWHLS YPYVFNHLDK IYMMPEGSAK GELRLYRAVN 240 FPLQWTLEKI LIKKPLVDSF IIKHDGEYWL FGSDHSDFGT KKNGQLEIWH SSSPLGPWKP 300 HKKNPIYNVN KSLGARNGGR PFLYKGNLYR VGQDCGETYG RRVRVFKVEI LTKDDYKEVE 360 VSLGFEEPRK GRNAWNGARY HHLDVQQLSS GQWIGVMDGD RVPSGDLVHR FLIGCASLAS 420 VAAIVVVLGL LLGAVKCIIP LNWCAYYSGK RSDTLLVWER SNAFSSKVRR FCGRLNRAAS 480 SLRIKIRLNT WAGRLVLAVI FTVGVVLIFT SVKYIYGGNG AEEPYPLKGS YSQFTLLTMT 540 YDARLWNLKM YVKHYSRCSS VKEIVVVWNK GIPPKLSDLD SAVPVRIRVE KKNSLNNRFR 600 KDELIETRAV LELDDDIMMT CDDIERGFNV WRQHPERIVG FYPRLISGSP LKYRGEKYAR 660 KHKGYNMILT GAAFLDSKLA FEMYWGEGAK AGRELVDKYF NCEDVLLNYL YANASTSGTV 720 EYVRPTWAID TSKFSGAAIS RNTQVHYKIR SNCLQKFSEM YGSLSRRKSE FDGRKDGWDL 780 * 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08994 | GH43_like_2 | 0.0005 | 259 | 344 | 88 | + Glycosyl hydrolase 43-like family consists of hypothetical proteins. This subfamily mostly contains uncharacterized proteins similar to glycosyl hydrolase family 43 (GH43) which includes enzymes with beta-xylosidase (EC 3.2.1.37) and alpha-L-arabinofuranosidase (EC 3.2.1.55) and possibly bifunctional xylosidase/arabinofuranosidase activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
| cd08978 | GH_F | 3.0e-5 | 134 | 318 | 200 | + Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 enzymes, is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. | ||
| pfam09258 | Glyco_transf_64 | 9.0e-73 | 534 | 778 | 247 | + Glycosyl transferase family 64 domain. Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0016758 | transferase activity, transferring hexosyl groups |
| GO:0031227 | intrinsic to endoplasmic reticulum membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAB85556.1 | 0 | 46 | 780 | 22 | 764 | putative protein [Arabidopsis thaliana] |
| RefSeq | NP_196070.2 | 0 | 46 | 780 | 23 | 765 | glycosyltransferase family protein 47 [Arabidopsis thaliana] |
| RefSeq | XP_002262646.1 | 0 | 92 | 780 | 68 | 756 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002315348.1 | 0 | 27 | 780 | 21 | 847 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532924.1 | 0 | 78 | 780 | 1 | 704 | transferase, transferring glycosyl groups, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 1on8_B | 4e-25 | 526 | 769 | 22 | 275 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1on8_A | 4e-25 | 526 | 769 | 22 | 275 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1on6_B | 4e-25 | 526 | 769 | 22 | 275 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1on6_A | 4e-25 | 526 | 769 | 22 | 275 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
| PDB | 1omz_B | 4e-25 | 526 | 769 | 22 | 275 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
