| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma13g34066.4 |
| Family | CBM57 |
| Protein Properties | Length: 620 Molecular Weight: 68742.5 Isoelectric Point: 6.8236 |
| Chromosome | Chromosome/Scaffold: 13 Start: 35712812 End: 35719822 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 24 | 200 | 4.4e-33 |
| HINCGGERELSSEGIVYDPDLDPSGAATSKIMGSNWAFSNTGHFLDAQKPVSETYIQQQNKTGLSKLYQTARVSPISLTYYGFCLENGDYTVLLHFAEIM FTDDNTYSSLGRRIFDVYIQGVQVMKDFNIANEAGGVGKNITRSFPAHVRNNSLIIRFYWAGKGTTAIPYGPLISAI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 620 Download |
| MSQNGPIHCL TTTNDCPKTF NSFHINCGGE RELSSEGIVY DPDLDPSGAA TSKIMGSNWA 60 FSNTGHFLDA QKPVSETYIQ QQNKTGLSKL YQTARVSPIS LTYYGFCLEN GDYTVLLHFA 120 EIMFTDDNTY SSLGRRIFDV YIQGVQVMKD FNIANEAGGV GKNITRSFPA HVRNNSLIIR 180 FYWAGKGTTA IPYGPLISAI SVTHVSTTTS GSMSTGVIVG IVVAAIVLVI LIVLGWRIYI 240 GKRNSFGKEL KDLNLRTNLF TMRQIKVATN NFDISNKIGE GGFGPVYKGI LSNGMIIAVK 300 MLSSKSKQGN REFINEIGLI SALQHPCLVK LHGCCVEGDQ LLLVYEYMEN NSLAQALFGN 360 GASQLKLNWP TRHKICIGIA RGLAFLHEES TLKIVHRDIK ATNVLLDKDL NPKISDFGLA 420 KLDEEDNTHI STRVAGTYGY MAPEYAMHGY LTDKADVYSF GVVALEIVSG KSNTIHRSKQ 480 EALHLLDWAH LLKEKGNLME LVDRRLGSDF NENEVMMMIK VALLCTNTTS NLRPTMSSVL 540 SMLEGKTMIP EFVSDPSEIM DEMKLEAMRQ HYFQKENERS ETQEQNHSLS IEGPWTASSS 600 SAADLYPVHV DSSYWEKRN* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 9.0e-50 | 277 | 543 | 286 | + Protein tyrosine kinase. | ||
| cd00180 | PKc | 4.0e-50 | 278 | 467 | 194 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
| smart00221 | STYKc | 1.0e-51 | 274 | 543 | 277 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| pfam11721 | Malectin | 2.0e-52 | 22 | 192 | 173 | + 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. | ||
| smart00219 | TyrKc | 2.0e-52 | 274 | 543 | 277 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004672 | protein kinase activity |
| GO:0005524 | ATP binding |
| GO:0006468 | protein phosphorylation |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAU10526.1 | 0 | 2 | 619 | 384 | 999 | putative receptor-like protein kinase 2 [Glycine max] |
| EMBL | CBI20124.1 | 0 | 5 | 619 | 412 | 1036 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002283596.1 | 0 | 5 | 619 | 412 | 1036 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002524511.1 | 0 | 7 | 618 | 362 | 984 | ATP binding protein, putative [Ricinus communis] |
| RefSeq | XP_002524514.1 | 0 | 7 | 619 | 384 | 1007 | ATP binding protein, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 260 | 545 | 20 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3uim_A | 0 | 260 | 545 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 260 | 545 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 260 | 545 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 260 | 545 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
