| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra001567 |
| Family | CBM57 |
| Protein Properties | Length: 1016 Molecular Weight: 111856 Isoelectric Point: 7.0538 |
| Chromosome | Chromosome/Scaffold: 03 Start: 17102189 End: 17108140 |
| 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 | 408 | 566 | 5e-29 |
| HINCGGDELTVNGTMYDSDTWEKPFHDGSRTGWVSSNTGNFLDDERDLKVTTLWTNTSELKTAEPSLYTQARLSAISLTYLALCLGNGSYTVKLHFAETM FGNNETYSSLGRRFFDIYVQGKLVVKDFDIVSEAKGAGRVVVKSFQVMITNGMLEIRLF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1016 Download |
| MSLNRLIFPF FILVSLILSG FASSQTLPKE EVDALRAVAT ALKKSNWNFN VDPCDLTSSE 60 GGWRNLNATS KQFADTVTCN CSSTVCHVTS IVLKAQSLQG SLPKEFAGLP FLQEIDLSRN 120 YLNGSIPPEW GTLPLVNISL LANRISGPIP KEIGNITTLK TLVLESNQIS GNLPPELGNL 180 QNIDKILLGT NYLTGDIPST FSKLTTLIDF RISDNQFTGT IPDFIKNWTK LFKLAIQASG 240 LVGPIPSTIG TLVKLTDLRI SDLNGPGSPF PPIQNMTSLK TLILRNSNLT GELPAYLGSI 300 TTLKLLDLSF NKLSGPIPAT YSNLWNVDNI YFTSNMLNGE VPRWAVDKGN NIDLTYNNFS 360 KDRTTKECSL RNANMFSSTT TSPLAANNYS NVACLSYYIC PKTFYGLHIN CGGDELTVNG 420 TMYDSDTWEK PFHDGSRTGW VSSNTGNFLD DERDLKVTTL WTNTSELKTA EPSLYTQARL 480 SAISLTYLAL CLGNGSYTVK LHFAETMFGN NETYSSLGRR FFDIYVQGKL VVKDFDIVSE 540 AKGAGRVVVK SFQVMITNGM LEIRLFWAGK GTQAIPVRGS YGVLISAVSV DPNFNVSGTS 600 IGIIVGAAVA SLVFLVLLIV GILWCRGCFR PKSQMEKDFK NLDFQISSFS LKQIKDATDN 660 FYPANKIGEG GFGPVHKGKL PNGTLIAVKQ LSSKSNQGNR EFLNEIGMIS ALEHPHLVKL 720 YGCCVEGGQL LLIYEYLVNN SLARALFGPL ETQIRLDWPI RQKICVGIAR GLAYLHEESR 780 LKIVHRDIKA TNVLLDKELN PKISDFGLAK LDEQEDTHMS TRVAGTYGYM APEYAMRGHL 840 TDKADVYSFG VVALEIVHGR GNTSARSKAE TFYLLDWVHV LREQNKLMEV VDPRLGTDYN 900 REEAMKMIQI GILCTSLVPS DRPSMSTVVS MLEGHSTVDV EELLENSFSR GNEKDEESVR 960 AMKRHFAMIG GQEMTNVTKH TTNNDGPFTS SSSSSANAGD LYPVKLDSAY WNSRV* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 6.0e-48 | 667 | 856 | 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 | 4.0e-49 | 666 | 932 | 276 | + 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-50 | 666 | 932 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00192 | PTKc | 6.0e-52 | 665 | 933 | 287 | + 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 | 1.0e-54 | 405 | 588 | 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 | 1014 | 1 | 1019 | leucine-rich repeat receptor-like protein kinase [Arabidopsis thaliana] |
| DDBJ | BAB02650.1 | 0 | 1 | 1014 | 1 | 1041 | receptor-like serine/threonine kinase [Arabidopsis thaliana] |
| EMBL | CBI20124.1 | 0 | 32 | 1014 | 62 | 1035 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_175747.2 | 0 | 1 | 978 | 1 | 940 | serine/threonine protein kinase-related [Arabidopsis thaliana] |
| RefSeq | NP_188102.4 | 0 | 1 | 1014 | 1 | 1016 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 645 | 934 | 16 | 308 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
| PDB | 3uim_A | 0 | 645 | 934 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 645 | 934 | 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 | 645 | 934 | 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 | 645 | 934 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
