| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01013608001 |
| Family | CBM57 |
| Protein Properties | Length: 995 Molecular Weight: 110807 Isoelectric Point: 6.4692 |
| Chromosome | Chromosome/Scaffold: Start: 1284866 End: 1301072 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 415 | 581 | 8.7e-30 |
| SIKCGGPEVIMPDGMVYEADNSISSTASTSFHESRSEKWAVSNVGLYVDKIANTTSQVNGTNTPELFKTSRISPGSLRYYGLGLQNGPYIVSLQFAEMLF KDPSTRTWESTGRRVFDIYIQGIRLERDFDISKEAGGVQRAVVRKFHATVSKNYLEIHLLWAGKGTC | |||
| Full Sequence |
|---|
| Protein Sequence Length: 995 Download |
| MNYRMKLCAF SFFLLLLFQK SPAQNATLDP SEVETLNFLF NKWNMTSTEF WNMSGDPCSG 60 PPITPSQYDD IYYKQAIKCN CTFNDNTTCH ISHLKVLNLN KTGSIPKELT ALTFLSDLRL 120 DKNYFTGPLP SFIANLSRMQ FIDVGHNALS GTIPKELGNL KELLMLAIGS NNFSGTLPPE 180 LGNLPKLELI FIDSSGVGGE IPSTFVKLKN MREMFLSDTP LTGKIPDFIG NWTKLKRLRI 240 QGNSFEGPIP STFSQLISME SLRISDLANV SSSLDFIKDM KNLTDLVLRN TLISGSIPSY 300 IEEYRSLETL DLSFNNITGR IPKALFNMNN LTALFLGNNS FYGPLPEEKS DKLQTIDLSY 360 NEISGGFPTW IDPTLRLNLV ANNFVFDNTN KTIFEGLDCL QRNFPCNTSR YTNVSIKCGG 420 PEVIMPDGMV YEADNSISST ASTSFHESRS EKWAVSNVGL YVDKIANTTS QVNGTNTPEL 480 FKTSRISPGS LRYYGLGLQN GPYIVSLQFA EMLFKDPSTR TWESTGRRVF DIYIQGIRLE 540 RDFDISKEAG GVQRAVVRKF HATVSKNYLE IHLLWAGKGT CCIPFEGYYG PSISALSVVS 600 GITLERYNTG FIAGIAVVAG IVCFILVCAV FYIQRRGSNV NEEIELLEIG PRPNTFSYAE 660 LRTATGNFNP TNKLGEGGFG VVFKGTLLDG RAIAVKDLMV ASQQGKSQFI AEIATISAVQ 720 HRNLVKLHGF CIKENKRLLV YEYLENKSLD HALFGKIDLH LDWPTRYNIC LGTARGLAYL 780 HEESRPRIVH RDVKASNILL DAELCPKISD FGLAKLYDDK KTHISTRVAG TIGYLAPEYA 840 MRGHLTEKAD VFGFGVVALE ILSGRPNTDN SLDAKKMYLL EWAWTLHENN QSMDLVDPTL 900 TEFDENEVNR VMRVALLCTQ GSPMLRPTMS RVVAMLVGDV EVSAVTSKPS YLTDWHYNDI 960 TNSFLSENTQ TSTASTSMTD QVPSPVLHIE PILR* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00220 | S_TKc | 1.0e-41 | 672 | 866 | 197 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
| cd00180 | PKc | 6.0e-45 | 674 | 861 | 192 | + 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 | 7.0e-46 | 673 | 863 | 197 | + 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 | 3.0e-46 | 673 | 863 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| pfam11721 | Malectin | 2.0e-55 | 412 | 596 | 187 | + 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: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 | CBI20535.1 | 0 | 1 | 994 | 1 | 994 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI20543.1 | 0 | 94 | 993 | 4 | 908 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI20543.1 | 0.0003 | 259 | 369 | 1 | 113 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI39037.1 | 0 | 5 | 993 | 1 | 995 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002271607.1 | 0 | 33 | 994 | 9 | 951 | 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 | 0 | 656 | 939 | 20 | 309 | 1 Chain 1, E. Coli (Lacz) Beta-Galactosidase (R599a) |
| PDB | 3uim_A | 0 | 656 | 939 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 656 | 939 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 656 | 939 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 656 | 939 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
