Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000292097 |
Family | CBM57 |
Protein Properties | Length: 1197 Molecular Weight: 133486 Isoelectric Point: 7.0855 |
Chromosome | Chromosome/Scaffold: 009872264 Start: 13941 End: 24487 |
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 | 275 | 454 | 3.7e-27 |
FINCGGRKMEFEGNEYEEDLSTVGQSHFISTSEKWGYSSTGVYMNKDKADYIATNTFSLNVDGPDFYQTARLSPLSLKYYGLCMLKGSYKVQLHFSEIMY TDDQTFSSLGKRIFDISIQGNLVWKDFNIMEEAGGVGKVVVKELDNVIVHGSTLEIHLYWAGKGTTAIPNRGVYGPLISA |
Full Sequence |
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Protein Sequence Length: 1197 Download |
MRFMFTSSEI VFVLLLGFLA LSCFTEFESN AQLLPLEEVK ILETISKKLH NTHWNISQSS 60 CQDGGAGFYK YFTDDILSNV TCNCSFPSNT CHVTIIEMKG LNLTGVIPEE LGNLTHLEAI 120 DLTRNYINGS IPATLSRAPF RALNLLGNRL SGSIPIDGFT MLTELVLEDN QFEGXLPQNI 180 GKLTNLKRLR ISDLNGSSPF PNLEDMKDIE LVDLSFNNLT GEIPQTIQRV DTLDYMDLSY 240 NNFTGSPSVS CQQLTVWCLK KDLPCSSKPK HHSIFINCGG RKMEFEGNEY EEDLSTVGQS 300 HFISTSEKWG YSSTGVYMNK DKADYIATNT FSLNVDGPDF YQTARLSPLS LKYYGLCMLK 360 GSYKVQLHFS EIMYTDDQTF SSLGKRIFDI SIQGNLVWKD FNIMEEAGGV GKVVVKELDN 420 VIVHGSTLEI HLYWAGKGTT AIPNRGVYGP LISAITVTPN FKVDTGGLSA GAIAGIVVAS 480 FVSVVLVLVI LRKAGYLGGK DEDEELRRGL EQKTGYFTLR QIKAATGNFD PTNKIGEGGF 540 GPVYKGVLSD GSIIAVKQLS AKSKQGNREF VNEIGMISAL QHPNLVRLFG CCIEGNQLLL 600 IYEYMENNSL ARALFGKHLQ HLEQNVKFGR EEQRLHLDWK TRKXICLGIA RGLXYLHEES 660 VLKIVHRDIK ATNVLLDKDL NAKISDFGLA KLDEEENTHI STRIAGTIGY MAPEYAMRGY 720 LTDKADVYSF GIVALEIVSG KSNTGYKPKE EFVYLLDGAY VLQEQGNMLE LVDPDLGSNY 780 SKTEAMTMLN LALLCTNPSP TLRPTMSSVV SMLEGKTPVQ APMKRGPVEQ DARFKAFERL 840 SQDSQTNVSX FSQDSHGGHG KERRPSSDWS VKNEVEERRD FINLAEMVHS PLRSYNPFLL 900 KTLAFVVALL IKIIGFQLSL VVAFFTLPIR LSYFSFMLFL FPFRTLKNVP RXCSVISKNV 960 TSAVSXRVQA QKSVAVNVGF AFFRSLYVRS MLLGILAXXF VLSGFIMRHL VENPIQTTEA 1020 LNFDYTKSXP VAFVPLMSSS RVSSDRAIPY NHKLQLAVSL TAPESEYNHK LGVFQVRVEF 1080 LSANGSVKAS SSHPCMLRYK SXPIHFIETF LKTAPLIXGL QSETXVLNIK MSGHIEGLEP 1140 TAYLKNTLSV ILNDVKFGFS YPEKNSRNSR HSAVEEQAKL XGLSYIRQSR QEPDDPE 1200 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00180 | PKc | 1.0e-47 | 535 | 737 | 207 | + 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. | ||
pfam11721 | Malectin | 1.0e-48 | 272 | 455 | 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. | ||
smart00221 | STYKc | 8.0e-52 | 534 | 813 | 290 | + 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 | 2.0e-52 | 534 | 813 | 292 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 7.0e-55 | 533 | 814 | 290 | + 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. |
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 | CAN81779.1 | 0 | 27 | 856 | 22 | 932 | hypothetical protein [Vitis vinifera] |
EMBL | CBI20142.1 | 0 | 26 | 856 | 19 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283521.1 | 0 | 26 | 856 | 19 | 977 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002316847.1 | 0 | 1 | 855 | 1 | 987 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332762.1 | 0 | 56 | 856 | 1 | 830 | predicted protein [Populus trichocarpa] |
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 | 501 | 815 | 7 | 308 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 3uim_A | 0 | 501 | 815 | 7 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 501 | 815 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 501 | 815 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 501 | 815 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |