Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.F04306.1 |
Family | CBM57 |
Protein Properties | Length: 329 Molecular Weight: 36403.1 Isoelectric Point: 6.7398 |
Chromosome | Chromosome/Scaffold: 6 Start: 51560143 End: 51563994 |
Description | Leucine-rich repeat transmembrane protein kinase |
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 |
CBM57 | 76 | 258 | 1.3e-30 |
SVKCGGPQITSSSNIVYEQDNILLGPATYYVTDSERWAVSNVGYFTGSNNPAYSAPSLSQFTNTLDTELFHTARVSASSLRYYGLGLENGNYNVTLQFAE IQIQDTEWKRLGRRLFDIYIQGNLVAKDFDIRKEAGGASFTAVLKLYQAQVTANYLEIHFFWAGKGTCCVPKQATYGPLISAI |
Full Sequence |
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Protein Sequence Length: 329 Download |
MTSFLCHFCR DVSYNNLMGS FPSWVSNELQ LTYLNNLVGN NFTLDDSNTS LLPSGLNCLQ 60 RNFPCTTGNG IYYNFSVKCG GPQITSSSNI VYEQDNILLG PATYYVTDSE RWAVSNVGYF 120 TGSNNPAYSA PSLSQFTNTL DTELFHTARV SASSLRYYGL GLENGNYNVT LQFAEIQIQD 180 TEWKRLGRRL FDIYIQGNLV AKDFDIRKEA GGASFTAVLK LYQAQVTANY LEIHFFWAGK 240 GTCCVPKQAT YGPLISAISA VPDFVPTVSN NPPTLDNPPT LDNSPSRKKD RSGLIVGVAT 300 GVGVVGFMAV LPVLYVVWRR RIARMIEDQ |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam12819 | Malectin_like | 0.0006 | 132 | 258 | 132 | + 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 | 3.0e-5 | 122 | 258 | 143 | + hypothetical protein; Provisional | ||
pfam11721 | Malectin | 7.0e-63 | 73 | 258 | 188 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI20016.1 | 0 | 11 | 273 | 442 | 702 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002267129.1 | 0 | 11 | 273 | 370 | 630 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002267672.1 | 0 | 11 | 273 | 366 | 626 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002513383.1 | 0 | 11 | 274 | 351 | 612 | ATP binding protein, putative [Ricinus communis] |
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 | 2kr2_A | 0.004 | 137 | 214 | 53 | 125 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 2k46_A | 0.004 | 137 | 214 | 53 | 125 | A Chain A, Xenopus Laevis Malectin Complexed With Nigerose (Glcalpha1- 3glc) |
PDB | 2jwp_A | 0.005 | 137 | 214 | 49 | 121 | A Chain A, Malectin |