y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000306337 |
Family | CBM57 |
Protein Properties | Length: 865 Molecular Weight: 95280 Isoelectric Point: 6.9208 |
Chromosome | Chromosome/Scaffold: 017553481 Start: 4271 End: 9535 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 293 | 469 | 3.4e-27 |
SIKCGGKQMTGSDGILYETEDSALGRATFSIDSTWKWAVSNAGLFDYYRNVGMLSDGVDRPFLVKTHAQVTGTNVTPELFQTSRVSPGSLRYYGLGLENG LYTVTLHFAETVYESRTSQTWQSLGRRVFDIYIQGTCRTKDFDISKEAGGVNRAVVRKFNVSVLENYLEIHMFWVGK |
Full Sequence |
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Protein Sequence Length: 865 Download |
XSALHLAVAR ISYTWHICLT TLELHTLILT AIDLPFNRTF YHSSIIAFKD IGPNNFSGTL 60 PPELGNLVKL EEIYMDSCGL SGEIPSTFAK LTNMQVLFVR LSSTLRLLFL DELSRALDSP 120 FSGKIPDFIG NWTQLYDLQI QGSSFEGPIP TSFSQLTSLN TLRISDIYNG SSSLDFIKNL 180 TSLTELRLRN ALITGTIPSD IGENQSLQTL NLVVNNFTFD SSNIALAGLN CLQRNFPCNR 240 NTPRCNLLLC HPSFTILTQR HVRGKGIASL VMDIDCKHVF TSSVIRITDA NFSIKCGGKQ 300 MTGSDGILYE TEDSALGRAT FSIDSTWKWA VSNAGLFDYY RNVGMLSDGV DRPFLVKTHA 360 QVTGTNVTPE LFQTSRVSPG SLRYYGLGLE NGLYTVTLHF AETVYESRTS QTWQSLGRRV 420 FDIYIQGTCR TKDFDISKEA GGVNRAVVRK FNVSVLENYL EIHMFWVGKG TCCIPDNGDY 480 GPLIAAVHAA SDFTPTVSRL PSTTPGKKSR TGLIVGIAVP VGVVSLLLIF AILYIRRKKS 540 EKEDDEDILG LXPRPNTFXY XELRXATEDF NPSNKLGEGG YGPVYKGTLX DGRVVAVKQL 600 SVASHQGKSQ FVSEIATISA VQHRNLVFTN ISGTSNLHLD WPTRFNILLG TARGLAYLHE 660 ESRPRIVHRD VKASNILLDA KLSPKISDFG LAKLYDDEKT HISTRVAGTI GYLAPEYAMF 720 GHLTEKVDVF GFGVVVLEIL SGRPNSYNNL DPEKIYLLEW GSPMARPSMS RLVAMLSGDI 780 DIGTVMSKPN YLTDYNFKDV TTFSTGRFLV EDDTPSTASK HSNVRLNYQP EGSDASNANT 840 SGVDLAPSPV NVTQSLLVGI IGEGM 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00221 | STYKc | 4.0e-33 | 575 | 768 | 229 | + 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 | 9.0e-34 | 575 | 768 | 226 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 7.0e-34 | 576 | 739 | 191 | + 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. | ||
pfam00069 | Pkinase | 4.0e-35 | 575 | 759 | 211 | + Protein kinase domain. | ||
pfam11721 | Malectin | 8.0e-48 | 291 | 487 | 199 | + 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 | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI39026.1 | 0 | 54 | 864 | 186 | 1036 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002272404.1 | 0 | 54 | 864 | 141 | 993 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 542 | 779 | 7 | 309 | A Chain A, Crystal Structure Of Class V Chitinase From Nicotiana Tobaccum |
PDB | 3uim_A | 0 | 542 | 779 | 7 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 536 | 779 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 536 | 779 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 536 | 779 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |