| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra001566 |
| Family | CBM57 |
| Protein Properties | Length: 986 Molecular Weight: 108364 Isoelectric Point: 6.3242 |
| Chromosome | Chromosome/Scaffold: 03 Start: 17093203 End: 17100118 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 369 | 527 | 2.1e-29 |
| HINCGGNELTINGTKYDADTSDRPIFYNSRNGWVSSNTGNFLDDDRSPKEVTLWTNRSELKIAEPRLYTHARLSAISLTYYALCLGEGNYTVNLHFSEIM FSDNETYGSLGRRFFDIYVQGKLEVKDFDIVNEAKGVGRAVVKSFQVMITNGKLEIRLF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 986 Download |
| MSFNLLLFPY FILFLILSDF AYSQTLPKQE VDALRAVATA LKKSNWKFNV NPCDLTSSDG 60 GWRNPNAGKG FEDAVTCNCS STVCHVTSIV LKAQDLQGSL PKELAGLPFL QEIDLSRNYL 120 NGSIPPEWGT LPLVNISLLG NRISGPIPKE IGNITTLTSL VLEFNQISGK LPPELGNLQK 180 IERILLSSNY LTGDIPSTFS KLTTLTDFRI SDNQFIGVIP DFIENWIELG KLVIQASGLV 240 GTIPSTIGPL GKLTDLRISD LNGPGSPFPP LQNMTSLKTL ILRNSNLTGE LPAYLGSITT 300 LKLLDLSFNK LSGPIPETYS ALSNVDNIYF TSNMLTGEVP SWMVDKGDKI SNVSCLSNYI 360 CPKTFYGLHI NCGGNELTIN GTKYDADTSD RPIFYNSRNG WVSSNTGNFL DDDRSPKEVT 420 LWTNRSELKI AEPRLYTHAR LSAISLTYYA LCLGEGNYTV NLHFSEIMFS DNETYGSLGR 480 RFFDIYVQGK LEVKDFDIVN EAKGVGRAVV KSFQVMITNG KLEIRLFWAG KGTQAIPSRG 540 VYGSLISAVS VDPNFIPPKE AGAGTGVGSS IGIVVGAVVA STVFLVLLIG GILWWRGCLR 600 PKSQMEKDFK NLDFQISSFS LKQIKVATDN FDPANKIGEG GFGPVHKGKL TDGTVIAVKQ 660 LSSKSKQGNR EFLNEIGMIS ALQHPHLVKL YGCCVEGGQL LLVYEYLENN SLARALFGPQ 720 ETQIRLDWPT RQNICVGIAR GLAYLHEESR LKIVHRDIKA TNVLLDKELN PKISDFGLAK 780 LDEDENTHMS TRVAGTYGYM APEYAMRGHL TDKADVYSFG VVALEIVHGR SNTSAQSKAE 840 TFYLLDWVHV LREQNKLMEV VDPRLGTDYN REEAKTMIHI GILCTSQVPS DRPSMSTVVS 900 MLEGHSTVDV EKLLEASFNR GNEKDEESVR AMKKHYAMIG GEVMTNVTDQ TTTTDGPFTS 960 SSTSTANAGD LYPVKLDSAY WNSRV* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 1.0e-49 | 637 | 826 | 194 | + 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 | 1.0e-50 | 636 | 902 | 278 | + 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-51 | 636 | 902 | 278 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00192 | PTKc | 1.0e-52 | 635 | 903 | 289 | + 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. | ||
| pfam11721 | Malectin | 9.0e-55 | 366 | 549 | 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 |
| GenBank | ACN59317.1 | 0 | 1 | 984 | 1 | 1019 | leucine-rich repeat receptor-like protein kinase [Arabidopsis thaliana] |
| DDBJ | BAB02650.1 | 0 | 1 | 984 | 1 | 1041 | receptor-like serine/threonine kinase [Arabidopsis thaliana] |
| RefSeq | NP_175747.2 | 0 | 20 | 948 | 21 | 940 | serine/threonine protein kinase-related [Arabidopsis thaliana] |
| RefSeq | NP_188102.4 | 0 | 1 | 984 | 1 | 1016 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002524511.1 | 0 | 26 | 984 | 27 | 984 | ATP binding protein, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 615 | 904 | 16 | 308 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
| PDB | 3uim_A | 0 | 615 | 904 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 615 | 904 | 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 | 615 | 904 | 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 | 615 | 904 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
