| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra018693 |
| Family | CBM57 |
| Protein Properties | Length: 1001 Molecular Weight: 111173 Isoelectric Point: 9.1141 |
| Chromosome | Chromosome/Scaffold: 06 Start: 2577232 End: 2584111 |
| 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 | 404 | 571 | 4.6e-31 |
| YINCGGGELKVDKGTTYEADQNSKGPSMFFSVNHWAYSSTGNFMDNDDDADDYIVQNTSRLSVNASSPSFGLYRTARVSPSSLTYYGLCLGNGNYTVHLH FAEITFTDDKTLYSLGKRLFDIYLQDKLVIKNFNIQEAASGSGKPVIKSFPVNVKDHNVKIGLRWAGK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1001 Download |
| MISWLSKYCI IILFTLIFHG RLGFSDNNKL HEAEVRALKE IGKKLGKKDW DFNKDPCSGQ 60 GNWVVTTYTS KEFESNITCD CSFLPLNSSC HVIRIALKSQ NLTGIVPPEF SKLRHLKVLD 120 LSRNYLTGSI PKEWASMRVE DLSFMGNRLS GPFPKVLTRL TTLRNLSLEG NLFSGQIPPE 180 IKRMIHLERL HLPSNAFTGP LPKELALLQN LTDMRISDNN FTGRIPDFIG NWTSIMKLQL 240 HGSGLDGPIP SSISALTSLT DLRISDLGGK PSPFPPLNNL DSIKTLILRK CNLNGEIPKY 300 IGKLKKLKTL DLSFNQLTGE IPSTFENMKK ADFIYLTGNK LTGAIPSYFV NKNKNVDVSY 360 NNFTDASTIT GSKCSDVTSR KESSCYLHHI PCRLPKRDHK YNLYINCGGG ELKVDKGTTY 420 EADQNSKGPS MFFSVNHWAY SSTGNFMDND DDADDYIVQN TSRLSVNASS PSFGLYRTAR 480 VSPSSLTYYG LCLGNGNYTV HLHFAEITFT DDKTLYSLGK RLFDIYLQDK LVIKNFNIQE 540 AASGSGKPVI KSFPVNVKDH NVKIGLRWAG KGTTGIPIRG VYGPMISAIS VEPNFKPPVY 600 HDKKEVILKA GIPVAAALLL LLIFGIFLKK RRDKNAIDKE LRNLDLQTGS FTLRQIKAAT 660 DNFDATLKIG EGGFGSVYKG VLSEGKLIAV KQLSAKSRQG NREFVNEIGM ISALQHPNLV 720 KLYGCCVEGN QLILVYEYLE NNCLSRALFG KDVSARLKLD WSTRKKICLG IAKGLTFLHE 780 ESRIKIVHRD IKASNVLLDK DLNAKISDFG LAKLNDDGNT HISTRIAGTV GYMAPEYAMR 840 GYLTEKADVY SFGVVALEIV SGKSNTNFRP SEEFVYLLDW AYVLQEKGCL LELVDPTLAS 900 DYSEEEAMLM LNVALMCTNA SPTLRPTMSQ VVSLLEGKTA MQELLSDPSF STVNPKLKAL 960 RNHFWQNEFS RTLSFSTTSG PKTASANSQL DAEEKTGLLD * 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 2.0e-51 | 668 | 935 | 282 | + Protein tyrosine kinase. | ||
| smart00221 | STYKc | 1.0e-52 | 668 | 935 | 277 | + 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-53 | 668 | 935 | 282 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00192 | PTKc | 8.0e-54 | 668 | 936 | 284 | + 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 | 4.0e-57 | 401 | 589 | 191 | + 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 |
| RefSeq | NP_172244.2 | 0 | 1 | 1000 | 1 | 1014 | leucine-rich repeat transmembrane protein kinase, putative [Arabidopsis thaliana] |
| RefSeq | XP_002278131.1 | 0 | 11 | 999 | 6 | 1002 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002306015.1 | 0 | 35 | 999 | 1 | 977 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002532988.1 | 0 | 96 | 994 | 6 | 913 | conserved hypothetical protein [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 | 647 | 937 | 16 | 308 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
| PDB | 3uim_A | 0 | 647 | 937 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 647 | 937 | 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 | 647 | 937 | 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 | 647 | 937 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
