| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra030170 |
| Family | CBM57 |
| Protein Properties | Length: 767 Molecular Weight: 84716.9 Isoelectric Point: 5.4649 |
| Chromosome | Chromosome/Scaffold: 07 Start: 5971192 End: 5976705 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 238 | 409 | 8.3e-28 |
| HINCGGPDVTIENSRGRFLYEGDNSGRTGSATNYHGKNWGFSNTGDFMDDAITEDTYSVSSDSTVSAKYPELYQTARRSPLSLAYFAFCFENGSYNVKLH FAEIQFSDEEPYARLATRFFNIYVQGKLVWEDFNIREEANGTHKEVIKEVNTTVTDNTLEIRLYWAGKGTTI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 767 Download |
| MSSAYKLMIM SQSRHFSSLL TVFICICLTC TVSASPSLHP DEVKALKDIA STLGVRHLNL 60 SEDPCLTKTL VITQDVLKEG HNSTIKCDCH FNNNKTCHIT HLILEANQFS GIIPKELGNL 120 VNLEGLELYA SGLREPIPDS IFRLENLFDL VLRNLNLTGP IPTTIWDLPN LMTLDLSFNR 180 LTGEIPADAA APKYTYLAGN MLSGKIESGP FLTASTNITR LLPCSAISQC QNYSKSLHIN 240 CGGPDVTIEN SRGRFLYEGD NSGRTGSATN YHGKNWGFSN TGDFMDDAIT EDTYSVSSDS 300 TVSAKYPELY QTARRSPLSL AYFAFCFENG SYNVKLHFAE IQFSDEEPYA RLATRFFNIY 360 VQGKLVWEDF NIREEANGTH KEVIKEVNTT VTDNTLEIRL YWAGKGTTII PKRGNYGSLI 420 SAISVCPSSE SECGVEVKTP PVTKEPKPRT YPLILGITAL ILSLAFLIFC ALYWKKCVRN 480 AEAGKRGSFS LKQLKVATDN FDPLNKIGEG GFGSVYKGRL PDGTLIAVKK LSSKSCQGNK 540 EFVNEIGMIA CLQHPNLVKL YGCCCENNQL LLVYEYLENN CLADALFGKV LTMKLEGYMA 600 PEYAMRGHLT EKADVYSFGV VAMEIVSGKS NANYTPDNEC CVGLLDWAFV LQKKGAFSEI 660 LDPKLEGVFD VMEAERMIKV SLLCSNKSPT LRPTMSEVVK MLEGETEIEQ IIADPGVYGD 720 ELRFKRFSEI GTSSLPSDYL VSIPSSCESA YDLYPLSPES TVFSRP* 780 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 3.0e-21 | 506 | 702 | 289 | + Protein tyrosine kinase. | ||
| cd00192 | PTKc | 2.0e-21 | 505 | 703 | 285 | + 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. | ||
| smart00219 | TyrKc | 1.0e-22 | 504 | 702 | 283 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 4.0e-23 | 504 | 702 | 284 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| pfam11721 | Malectin | 4.0e-57 | 235 | 423 | 192 | + 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: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 | AAG10621.1 | 0 | 1 | 206 | 1 | 234 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
| GenBank | AAG10621.1 | 0 | 95 | 764 | 168 | 945 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
| RefSeq | NP_174267.4 | 0 | 1 | 186 | 1 | 235 | kinase [Arabidopsis thaliana] |
| RefSeq | NP_174267.4 | 0 | 95 | 589 | 168 | 765 | kinase [Arabidopsis thaliana] |
| RefSeq | NP_174267.4 | 0 | 597 | 759 | 842 | 1004 | kinase [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 | 3e-22 | 484 | 586 | 15 | 118 | A Chain A, Crystal Structure Of C. Jejuni Pglb C-Terminal Domain |
| PDB | 3ulz_A | 3e-18 | 597 | 705 | 200 | 309 | A Chain A, Crystal Structure Of C. Jejuni Pglb C-Terminal Domain |
| PDB | 3uim_A | 3e-22 | 484 | 586 | 15 | 118 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3uim_A | 3e-18 | 597 | 705 | 200 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 3e-22 | 484 | 586 | 23 | 126 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
