Basic Information | |
---|---|
Species | Fragaria vesca |
Cazyme ID | mrna03872.1-v1.0-hybrid |
Family | CBM57 |
Protein Properties | Length: 603 Molecular Weight: 66979.6 Isoelectric Point: 5.2097 |
Chromosome | Chromosome/Scaffold: 4 Start: 25667326 End: 25671611 |
Description | Di-glucose binding protein with Leucine-rich repeat domain |
View CDS |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CBM57 | 211 | 357 | 1.8e-22 |
NDTDQFSRSWQSDAQFRTIDSESPARVISTTNSISHAGDAPNFFPMRLYQSAVTADGKKNLEYDLTVDAKLDYLLWFHFAEIDPKMNKVGDRVFDIFIND KNVTRIDIYKEVGSFRAYTWHYTVKNLSSTQLNVQLKGVAGTPLISG |
Full Sequence |
---|
Protein Sequence Length: 603 Download |
MSLLFFLLPL LLLFVSAHSY SYYGLSYNID CGSATNSTDG FNTTWLSDRF YTGGSSYYVS 60 EPLQFRHPQE KTLRFFPPSS GKKNCYVVPD LPSGRYYVRT FTVYDNYDGK SHPPSFDASV 120 EGTLVFSWRS PWPEDLTRTG AYSDLFVFVT DGEADICFYS IATDSPVVGS LQIVQVDPAS 180 YDGGFDGRKY ILVNYGRLSC GSGQWGPGFS NDTDQFSRSW QSDAQFRTID SESPARVIST 240 TNSISHAGDA PNFFPMRLYQ SAVTADGKKN LEYDLTVDAK LDYLLWFHFA EIDPKMNKVG 300 DRVFDIFIND KNVTRIDIYK EVGSFRAYTW HYTVKNLSST QLNVQLKGVA GTPLISGLEN 360 YAMVPADVAT LPEQVVAMRA LKESLRVPDR MGWNGDPCAP TNWDAWEGVT CHLNKNETAL 420 VISRIDLGSQ GLKGFISDQI NLLSDLLSLD LSDNQLTGSI PESLTSSNLQ LVLLNDNLLD 480 GRVPEQLYSI GVHGGAIDLY GNKGLCGVPS LPDCPLFWEN GGLSTKGKIA IGISCGVILC 540 LMLLVVYIIY VRRRRNDYDF GFPHDLIPLG AKTNRYHRQK SIAVLEMESQ HAKADLQPLQ 600 GK* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam11721 | Malectin | 8.0e-5 | 26 | 159 | 148 | + Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. | ||
pfam11721 | Malectin | 2.0e-13 | 197 | 358 | 176 | + Di-glucose binding within endoplasmic reticulum. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. It carries a signal peptide from residues 1-26, a C-terminal transmembrane helix from residues 255-274, and a highly conserved central part of approximately 190 residues followed by an acidic, glutamate-rich region. Carbohydrate-binding is mediated by the four aromatic residues, Y67, Y89, Y116, and F117 and the aspartate at D186. NMR-based ligand-screening studies has shown binding of the protein to maltose and related oligosaccharides, on the basis of which the protein has been designated "malectin", and its endogenous ligand is found to be Glc2-high-mannose N-glycan. | ||
pfam12819 | Malectin_like | 1.0e-58 | 29 | 363 | 353 | + Carbohydrate-binding protein of the ER. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. The domain is found on a number of plant receptor kinases. | ||
PLN03150 | PLN03150 | 5.0e-100 | 29 | 544 | 551 | + hypothetical protein; Provisional |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 4hq1_A | 0.001 | 374 | 484 | 324 | 427 | A Chain A, Native Structure Of Beta-Galactosidase From Penicillium Sp. |
PDB | 3rj0_A | 0.002 | 425 | 514 | 658 | 745 | A Chain A, Native Structure Of Beta-Galactosidase From Penicillium Sp. |