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Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra030167 |
Family | CBM57 |
Protein Properties | Length: 975 Molecular Weight: 108327 Isoelectric Point: 6.945 |
Chromosome | Chromosome/Scaffold: 07 Start: 6006872 End: 6016483 |
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 | |||
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Family | Start | End | Evalue |
CBM57 | 375 | 541 | 1.9e-26 |
HINCGGDNVVITNSSHKITYQADNNETKAATNQHFENWGVSSTGYLPNDIYIITPTFALPENSPAFYKSARQSAQSLVYYAFCLENGAYNVKLHFMEIQF SNEEPYSRLGRRIFDIYLQGELFKRDFNIKEEANGNRKPIVKEANVNVANHLLEIRLYWAGKGTTLI |
Full Sequence |
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Protein Sequence Length: 975 Download |
MDMSIVFSSF ILLFTIATSF LAAQITPVAS PALLHPDELK ALEEIASTLG ITKLNLGNGD 60 PCDLKRLKID VAQDPTSENI IVCDCSRNNT CHITDLTLKT LGLPGKVPPE LVKLQYLRSI 120 SVCANNLSGP LPTGLQNFKK LEFLGVEANQ FSGPIPAELG NLISLTGLQL GSNQFTSTLP 180 TTLSKLVNLK EFRISDNKFI GIIPRFIGDW SRLEKIHLFA SGLKGPIPDA LARLENLIDL 240 RISDMTGINS FPNISSKSMN TLILRNLSLS GQIPSFVWSM PVLKTLDVSF NKLSGEVDLQ 300 GKVPKYTMYH DSLFWKKYIL FMQKPHVHIL FMQKTHFHSY IYFYSVSNTM MDRGFVSNTS 360 DDGDNRSIVD QRSLHINCGG DNVVITNSSH KITYQADNNE TKAATNQHFE NWGVSSTGYL 420 PNDIYIITPT FALPENSPAF YKSARQSAQS LVYYAFCLEN GAYNVKLHFM EIQFSNEEPY 480 SRLGRRIFDI YLQGELFKRD FNIKEEANGN RKPIVKEANV NVANHLLEIR LYWAGKGTTL 540 IPQRGNYGPI ISAISLCHST EKTIHRTNYP LIFGITGALL AVMLLALGLY AQKRCRGDKN 600 TRERDLRAQG LQTVCFTWRQ LQAATNNFDE AKKLGEGGFG SVFKGELSDG TIIAVKQLSA 660 KSCQGNREFV NEIGMISGLN HPNLVKLYGC CVEKNQLLLV YEYMENNSLA LALNGESAPN 720 LDWAARQRIC VGIARGLEFL HEGSMIRMVH RDIKTTNVLL DADLNAKISD FGLARLHEEE 780 HTHISTKIAG TIGYMAPEYA LYGELTEKAD VFSFGVVAME IVSGKSNTKQ KGSADHVWLI 840 KWARKLQQTG DIMDIIDPVL EGDFNRKEAE RMIKVSLVCT NSSPLLRPTM SEVVQMLEGE 900 IEITQVLSDP GLYEHNFSIS KLMGTDTHGS SSTSGLTDQT ETTMKSSVSS TDLYPLYPES 960 MLLNSTQNFS SSAF* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 1.0e-50 | 632 | 897 | 278 | + Protein tyrosine kinase. | ||
pfam11721 | Malectin | 6.0e-52 | 373 | 554 | 184 | + 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. | ||
smart00221 | STYKc | 1.0e-52 | 632 | 897 | 282 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00192 | PTKc | 9.0e-53 | 632 | 898 | 292 | + 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 | 7.0e-53 | 632 | 897 | 282 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAG10621.1 | 0 | 4 | 963 | 13 | 944 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
GenBank | AAG10622.1 | 0 | 37 | 966 | 65 | 1009 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
GenBank | AAG50772.1 | 0 | 37 | 974 | 7 | 920 | AC079288_1 receptor-like serine/threonine kinase (RFK1), putative [Arabidopsis thaliana] |
GenBank | AAG50775.1 | 0 | 4 | 963 | 13 | 937 | AC079288_4 receptor-like serine/threonine kinase, putative [Arabidopsis thaliana] |
RefSeq | NP_174266.2 | 0 | 4 | 963 | 13 | 966 | ATP binding / kinase/ protein binding / protein kinase/ protein serine/threonine kinase/ protein tyrosine kinase [Arabidopsis thaliana] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 616 | 900 | 20 | 309 | 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 | 616 | 900 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 616 | 900 | 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 | 616 | 900 | 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 | 616 | 900 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |