| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra032331 |
| Family | CBM57 |
| Protein Properties | Length: 709 Molecular Weight: 78406.9 Isoelectric Point: 6.3127 |
| Chromosome | Chromosome/Scaffold: 09 Start: 22493264 End: 22498558 |
| 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 | 146 | 322 | 2.8e-27 |
| LHINCGGQNTVIKNSSHKISYEADDSTVYSTTNQHFKTWGISNTGVFAADEHSENDTYIILASSKLPGDSPNLYKTARRSALSLVYYAFCLENGEYNLKL HFMEIQFSDEEPFSRLGRRIFDVYVQGELFLKDFNIKEESNGTMTPVVKEVKAVNVTNHMLEIQLYWAGKGTTLIPK | |||
| Full Sequence |
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| Protein Sequence Length: 709 Download |
| MMQDVDVISN PDTGNSTIRC DCSFNKSTTC HITSMHLTSN QFTGSLPNSL AKLMNLEDLV 60 SDNNFNGTIP EYIGNWSRLQ RLILRNVSLS GAIPSYIWSL PELKTLDLSF NSLTGEVRGI 120 QSAPKFTTGL LPCAGPINCT SYQRTLHINC GGQNTVIKNS SHKISYEADD STVYSTTNQH 180 FKTWGISNTG VFAADEHSEN DTYIILASSK LPGDSPNLYK TARRSALSLV YYAFCLENGE 240 YNLKLHFMEI QFSDEEPFSR LGRRIFDVYV QGELFLKDFN IKEESNGTMT PVVKEVKAVN 300 VTNHMLEIQL YWAGKGTTLI PKRGNYGPLI SAISLCHHNL RVEGLPTVCF TWRQLQAATN 360 NFDQANKLGE GGFGSVFKGE LSDGTIIAVK QLSSKSHQVN REFVNDIGMI SGLNHPNLVK 420 LYGCCVEKNQ LMLVYEYMEN NSLAHMLHGK SSLNLNWRAR QKICVGIARG LEFLHEGSMI 480 RMVHRDIKTT NVLLDADLNA KISDFGLARL HEEEHSHIST KIAGTIGYMA PEYALWGQLS 540 EKADVYSFGI VAMEIVSGQS NTKQKGSADH VSLINWAVKL QQKGDITEIV DPVLQGDFNT 600 KEAVRMIKVA IVCTNSSPSL RPTMSEVVQM LEGEVEITQV LSDPGLYGHN WSISNLRDID 660 TDGGLSTSVV TDQTATRMKS SVSGCDLYPL YPESMILNST VDFSSSSL* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 1.0e-51 | 367 | 558 | 200 | + Protein tyrosine kinase. | ||
| smart00219 | TyrKc | 2.0e-52 | 367 | 631 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00192 | PTKc | 8.0e-53 | 366 | 632 | 298 | + 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. | ||
| smart00221 | STYKc | 5.0e-53 | 367 | 631 | 276 | + 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 | 9.0e-56 | 146 | 333 | 189 | + 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 | AAG10622.1 | 0.000000003 | 1 | 132 | 97 | 238 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
| GenBank | AAG10622.1 | 0 | 32 | 704 | 223 | 1013 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
| GenBank | AAG50772.1 | 0.000000003 | 1 | 132 | 39 | 180 | AC079288_1 receptor-like serine/threonine kinase (RFK1), putative [Arabidopsis thaliana] |
| GenBank | AAG50772.1 | 0 | 32 | 708 | 165 | 920 | AC079288_1 receptor-like serine/threonine kinase (RFK1), putative [Arabidopsis thaliana] |
| RefSeq | NP_001154382.1 | 0 | 248 | 708 | 1 | 511 | 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 | 350 | 634 | 20 | 309 | A Chain A, The Structure Of A Protein In Glycosyl Transferase Family 8 From Anaerococcus Prevotii. |
| PDB | 3uim_A | 0 | 350 | 634 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 350 | 634 | 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 | 350 | 634 | 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 | 350 | 634 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GR933408 | 267 | 349 | 615 | 0 |
| EY940306 | 238 | 347 | 584 | 0 |
| EX770235 | 227 | 369 | 595 | 0 |
| EX773661 | 227 | 369 | 595 | 0 |
| EX773661 | 27 | 595 | 621 | 0.007 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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