y
Basic Information | |
---|---|
Species | Malus domestica |
Cazyme ID | MDP0000283397 |
Family | CBM57 |
Protein Properties | Length: 671 Molecular Weight: 73869.9 Isoelectric Point: 6.4517 |
Chromosome | Chromosome/Scaffold: 007092780 Start: 452 End: 5243 |
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 | 202 | 374 | 2.1e-30 |
SINCGGQQMTGSDGILYESDDSELGLTSFRVTSTENGAVSNAGSISYDTSFSDDTPSLNKTLAQVTGTDVTPVLFQTSRMSTGSLRYYGLGLENGLYTVT LHFAETAYESRTSQTRQSLGRRVFDIYIQGTRRTKDFDISKEASGVNRAVVRKFNVNMSENYLEIHLFWAGEG |
Full Sequence |
---|
Protein Sequence Length: 671 Download |
MTCRDIGSNN FSRTLPPELG NLVKLENLNL DSCGHGGEIP STFANLTNMQ AFSASDNPFS 60 GKIPDFHREL DKPHFFGISR ELFRRPNTNQ LFSTDLIEVS VPSTIIEMVR FLGNNSLSGP 120 HQSQKSDQLQ TMQRLVLQFL SGSFPQWVTT MWVAPIPQLN VVVNNFTFNS SNITLPGLNC 180 LQRNFPCNRN TPRYSGITAS FSINCGGQQM TGSDGILYES DDSELGLTSF RVTSTENGAV 240 SNAGSISYDT SFSDDTPSLN KTLAQVTGTD VTPVLFQTSR MSTGSLRYYG LGLENGLYTV 300 TLHFAETAYE SRTSQTRQSL GRRVFDIYIQ GTRRTKDFDI SKEASGVNRA VVRKFNVNMS 360 ENYLEIHLFW AGEGTCCIPD SGDFGPLIAA VHAASDILGL GPRPYTFSYV ELRNATKDFN 420 PSNKLGEGGY GPVYKGTLSD GRVVAVKQLS VSSHQGKSQF VSEIATISAV QHRNLVKLYG 480 CCIEGRHRIL VYEYLENKSL DQALFGTSNL HLDWPTRFNI LLGTARGFAY LHEESRPRIE 540 AILAPEYAMF GHLTEKADVF GFGVVVLEIL SGRPNSYNNL DPEKIYLLEW GSPMARPSMS 600 RVVAMLSGDI DISTVMSKPS YLTDYDFKGV TTSLTSRFLV EDDTPSTSSK GSNVRLNYQS 660 GGSNASGANT P 720 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 1.0e-25 | 423 | 598 | 233 | + 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 | 8.0e-26 | 424 | 598 | 224 | + 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 | 5.0e-26 | 424 | 598 | 222 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam07714 | Pkinase_Tyr | 2.0e-27 | 424 | 597 | 222 | + Protein tyrosine kinase. | ||
pfam11721 | Malectin | 5.0e-51 | 200 | 391 | 194 | + 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. |
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 |
EMBL | CBI39026.1 | 0 | 1 | 650 | 178 | 1007 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002272404.1 | 0 | 1 | 396 | 85 | 576 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002272404.1 | 0 | 1 | 650 | 133 | 964 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002273016.1 | 0 | 1 | 396 | 130 | 623 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002273016.1 | 0 | 6 | 644 | 183 | 1003 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 8e-36 | 407 | 609 | 20 | 309 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
PDB | 3uim_A | 8e-36 | 407 | 609 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 2e-35 | 407 | 609 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 2e-35 | 407 | 609 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 2e-35 | 407 | 609 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
CN899853 | 223 | 237 | 416 | 0 |
CO865700 | 210 | 199 | 402 | 0 |
CO097515 | 259 | 376 | 591 | 0 |
FP051832 | 232 | 396 | 584 | 0 |
DY261470 | 238 | 397 | 591 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|