| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma13g31020.3 |
| Family | CBM57 |
| Protein Properties | Length: 626 Molecular Weight: 68794.4 Isoelectric Point: 8.8013 |
| Chromosome | Chromosome/Scaffold: 13 Start: 33490929 End: 33497349 |
| Description | receptor like protein 4 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CBM57 | 227 | 364 | 3.4e-25 |
| WQHTETFGEDSDRPRSVETRIKQASHPPNFYPETLYRSALVSTSSQPELTYTLDVDPNKNYSVWLHFAEIDNSVTAEGQRVFDIMINGDVAFKDVDIVKL SGDRYTALVLNTTVVVNGRTLTIALSPKDGSFAIINAI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 626 Download |
| MPNIATFRFL LLWMLFLCFA CTARAAQRGP FAMRISCGAR QNVQTKPTTT LWYKDFGYTG 60 GIPTNAKTSS YIAPPLKTLR YFPLSEGPSN CYNINRVPKG HYSIRIFFGL VAQARATDEP 120 LFDISIQGTQ IYSLKSGWTT QDDQAFTEAQ VFLMDGSVSI CFHGTGHGDP AILSIEILQI 180 DNKAYYFGSQ WSQGIILRTV KRLSCGFGQS KYGVDYGADP RGGDRFWQHT ETFGEDSDRP 240 RSVETRIKQA SHPPNFYPET LYRSALVSTS SQPELTYTLD VDPNKNYSVW LHFAEIDNSV 300 TAEGQRVFDI MINGDVAFKD VDIVKLSGDR YTALVLNTTV VVNGRTLTIA LSPKDGSFAI 360 INAIEIMEVI MAESKTLSDE VMALQKLKKA LGLPPRFGWN GDPCVPQQHP WTGADCRLDK 420 SSSKWVIDGL GLDNQGLKGF LPNDISRLHN LQILNLSGNS IQGPIPSPLG TIASLQVLDL 480 SYNFFNGSIP ESLGQLTSLQ RLNLNGNFLS GRVPATLGGR LLHGASFNFT DNAGLCGIPG 540 LPTCGPHLSA GAKVGIGLGV SFTLLLLITG SVCWWKRRQN ILRVQQITAR AAPYAKARTQ 600 FSRDIQMTRH NNNNNAENGP ILLSR* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam11721 | Malectin | 0.004 | 33 | 175 | 166 | + 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. | ||
| PLN00113 | PLN00113 | 2.0e-14 | 430 | 519 | 90 | + leucine-rich repeat receptor-like protein kinase; Provisional | ||
| pfam11721 | Malectin | 1.0e-17 | 202 | 364 | 177 | + 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 | 5.0e-65 | 35 | 369 | 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 | 0 | 10 | 624 | 623 | + hypothetical protein; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005515 | protein binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI30598.1 | 0 | 28 | 624 | 22 | 624 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_174156.1 | 0 | 26 | 624 | 22 | 626 | AtRLP4 (Receptor Like Protein 4); protein binding [Arabidopsis thaliana] |
| RefSeq | XP_002279791.1 | 0 | 33 | 624 | 1 | 600 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002305781.1 | 0 | 33 | 624 | 1 | 596 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002509445.1 | 0 | 7 | 624 | 2 | 629 | serine-threonine protein kinase, plant-type, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3rgz_A | 0.0000000000001 | 437 | 551 | 644 | 755 | 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 | 3rgz_A | 0.000000004 | 426 | 517 | 467 | 558 | 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 | 3rgz_A | 0.0000003 | 424 | 517 | 393 | 486 | 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 | 3rgz_A | 0.000003 | 437 | 518 | 454 | 535 | 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 | 3rgz_A | 0.000009 | 437 | 539 | 430 | 531 | A Chain A, Control Of Phosphorylase B Conformation By A Modified Cofactor: Crystallographic Studies On R-State Glycogen Phosphorylase Reconstituted With Pyridoxal 5'-Diphosphate |
