| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma13g34066.1 |
| Family | CBM57 |
| Protein Properties | Length: 675 Molecular Weight: 74929.3 Isoelectric Point: 6.7282 |
| Chromosome | Chromosome/Scaffold: 13 Start: 35712812 End: 35719820 |
| 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 | 79 | 255 | 5.2e-33 |
| HINCGGERELSSEGIVYDPDLDPSGAATSKIMGSNWAFSNTGHFLDAQKPVSETYIQQQNKTGLSKLYQTARVSPISLTYYGFCLENGDYTVLLHFAEIM FTDDNTYSSLGRRIFDVYIQGVQVMKDFNIANEAGGVGKNITRSFPAHVRNNSLIIRFYWAGKGTTAIPYGPLISAI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 675 Download |
| YFTGNSFTGP IPNWVGNAKR PIDISYNNFS NEPPQQQSCQ QIQNPTVNLF ESFPMSQNGP 60 IHCLTTTNDC PKTAFNSFHI NCGGERELSS EGIVYDPDLD PSGAATSKIM GSNWAFSNTG 120 HFLDAQKPVS ETYIQQQNKT GLSKLYQTAR VSPISLTYYG FCLENGDYTV LLHFAEIMFT 180 DDNTYSSLGR RIFDVYIQGV QVMKDFNIAN EAGGVGKNIT RSFPAHVRNN SLIIRFYWAG 240 KGTTAIPYGP LISAISVTHV STTTSGSMST GVIVGIVVAA IVLVILIVLG WRIYIGKRNS 300 FGKELKDLNL RTNLFTMRQI KVATNNFDIS NKIGEGGFGP VYKGILSNGM IIAVKMLSSK 360 SKQGNREFIN EIGLISALQH PCLVKLHGCC VEGDQLLLVY EYMENNSLAQ ALFGNGASQL 420 KLNWPTRHKI CIGIARGLAF LHEESTLKIV HRDIKATNVL LDKDLNPKIS DFGLAKLDEE 480 DNTHISTRVA GTYGYMAPEY AMHGYLTDKA DVYSFGVVAL EIVSGKSNTI HRSKQEALHL 540 LDWAHLLKEK GNLMELVDRR LGSDFNENEV MMMIKVALLC TNTTSNLRPT MSSVLSMLEG 600 KTMIPEFVSD PSEIMDEMKL EAMRQHYFQK ENERSETQEQ NHSLSIEGPW TASSSSAADL 660 YPVHVDSSYW EKRN* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 5.0e-50 | 332 | 598 | 286 | + Protein tyrosine kinase. | ||
| cd00180 | PKc | 2.0e-50 | 333 | 522 | 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 | 329 | 598 | 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 | 9.0e-52 | 77 | 247 | 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 | 329 | 598 | 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 | 1 | 674 | 333 | 999 | putative receptor-like protein kinase 2 [Glycine max] |
| EMBL | CBI20124.1 | 0 | 1 | 674 | 358 | 1036 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002283578.1 | 0 | 1 | 674 | 329 | 984 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002283596.1 | 0 | 1 | 674 | 358 | 1036 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002524514.1 | 0 | 1 | 674 | 330 | 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 | 315 | 600 | 20 | 308 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
| PDB | 3uim_A | 0 | 315 | 600 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 315 | 600 | 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 | 315 | 600 | 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 | 315 | 600 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
