Basic Information | |
---|---|
Species | Cucumis sativus |
Cazyme ID | Cucsa.273550.1 |
Family | CBM57 |
Protein Properties | Length: 1031 Molecular Weight: 113554 Isoelectric Point: 6.4285 |
Chromosome | Chromosome/Scaffold: 02511 Start: 630807 End: 645894 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CBM57 | 411 | 575 | 9.5e-28 |
INCGGTRVTADGHDYEEDLTTEGKSNFFSVSEKWAYSSTGVFLGDENADYLATNKFGLNVSGPRYYQNARLSPLSLKYYGLCLRSGSYNVKLHFAEIMYS NDQTFSSLGKRIFDISIQGKLVKKDFNIVEAAGGVGKNFTVEDKNVLVNGSTLEINLYWAGKGTT |
Full Sequence |
---|
Protein Sequence Length: 1031 Download |
MDFPGSLLIR ILAFFLPWIL LFQAFGSDAQ LLPESEVKTL QTISSKLENL SWNVTRSSCI 60 RGEGFSNQAF QGNQILRNIS CNCTSTLCHV TIVLLKGLNL TGTFPAEFGN LTHLQELDLT 120 RNHINGQLPS SLANAPLVKL SLLGNRLNGS IPKEIGEIGT LEELILEDNQ LTGSLPASLG 180 NLNSLRRLLL SANNFTGKIP DSFGKLTNLV DFRVDGNGLS GKIPEFIGNW INLDRLDMQG 240 TSMENPIPST ISQLKNLTQL RISDLKGSFI SFPNLTDMIN MKELVLRNCL INGSIPEYIG 300 EMNKLSTLDL SFNHLNGDIP ETFQNLMKRK IDFMFLTNNS LSGEVPGWIL RSKKNIDLSY 360 NNFSGSTLAS CQQSPVNLIA SYPPATNHQV PWCLKKDLPC SGKAEYHSLF INCGGTRVTA 420 DGHDYEEDLT TEGKSNFFSV SEKWAYSSTG VFLGDENADY LATNKFGLNV SGPRYYQNAR 480 LSPLSLKYYG LCLRSGSYNV KLHFAEIMYS NDQTFSSLGK RIFDISIQGK LVKKDFNIVE 540 AAGGVGKNFT VEDKNVLVNG STLEINLYWA GKGTTAVPDR GVYGPLISAI TVTPNFKINE 600 GGLSSGALAG IIVSSCVVVI ILVLVFLWMT GYICKKEDLA NELSGIDLQT GHFTLKQIKA 660 ATNNFDPKSK IGEGGFGPVY KGVLSDGALI AVKQLSSKSK QGSREFVTEI GMISALQHPN 720 LVKLYGCCVE GNQLLLVYEY MENNSLARAL FGREEQRLHL DWRTRKKICL EIARGLAYLH 780 EESRLKIVHR DIKATNVLLD KDLNAKISDF GLAKLDEEEN THISTRIAGT IGYMAPEYAM 840 RGYLTDKADV YSFGIVALEI VSGKSNTNYR PKEEFVYLLD WAYVLEEQGN LLELADPDLG 900 SNYSSEEAMR MLNVALLCTN PSPTLRPTMS SVVSMLEGKI AVQAPIIKRT SSGQDPRFRA 960 FEKLSHDSRS QISSSTVSLD AEPQKSMLMD GPCPDSSVTI DTNGNNHYHS ASSDPLENHR 1020 RVDNLKDSAN * |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00220 | S_TKc | 5.0e-51 | 665 | 865 | 203 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
pfam11721 | Malectin | 2.0e-54 | 407 | 590 | 186 | + 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. | ||
cd00192 | PTKc | 6.0e-55 | 670 | 937 | 282 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
smart00221 | STYKc | 2.0e-55 | 668 | 936 | 280 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
smart00219 | TyrKc | 1.0e-55 | 668 | 936 | 280 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
Gene Ontology | |
---|---|
GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005515 | protein binding |
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 |
EMBL | CBI20142.1 | 0 | 25 | 1013 | 20 | 1006 | unnamed protein product [Vitis vinifera] |
EMBL | CBI20154.1 | 0 | 29 | 1013 | 195 | 1174 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283453.1 | 0 | 25 | 1013 | 22 | 1002 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283521.1 | 0 | 25 | 1013 | 20 | 1008 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316847.1 | 0 | 1 | 1002 | 1 | 1008 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 649 | 938 | 16 | 308 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3uim_A | 0 | 649 | 938 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 649 | 938 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 649 | 938 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 649 | 938 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |