Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10019658m |
Family | CBM57 |
Protein Properties | Length: 880 Molecular Weight: 97200.9 Isoelectric Point: 8.2991 |
Chromosome | Chromosome/Scaffold: 9 Start: 5977801 End: 5984422 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 414 | 568 | 2.6e-25 |
SINCGGPQIRSATGAIFERDDEDLGSASFVVSDVQRWAASSVGYFAGSSNNIWVVNTLDSEIFQSARQSSSSRRYYGLGLENGGYTVTLQFAEIDILGTN SWRGLGRRRFDIYVQGKLVEKDFDIRKTACDTTVQAVQREYKTNVSENYLEIHLL |
Full Sequence |
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Protein Sequence Length: 880 Download |
QALNLIFAAW KIRATKEWNI SGELCSGAAI DESITIDDKA YNPFIKCRCI FHNSTICRIT 60 ALKVFAIDVI GPIPPQLWTL TYLTNLKIEP VNAFILYVHQ KSHASFFQEP GSKFSYRLHF 120 SCNWKFDSNG MDVRLLKLFG VNALSGPIPK EIGLLTELRS LGIGLNNFSG SIPAEIGNCT 180 KLLKIYLGIS GLRGEIPSSF ANLVDLEDAW IHDMDVSGPI PEFIGKWTKL TILKILGTGL 240 SGPIPLSFSN LTSLRELSLG DISNIGSSSL EFIKGMKSLS ILVLRNSNLT GTIPSNIGKN 300 SNLQQVDLSF NKLHGPIPAS LLNLNQLTHL FLGNNTLDGS LPTQKSQTLR NIDVSYNDLS 360 GSLPSWVSLP NLKLNLVANN FTLEGLDKRV LPGLKCLQKN FPCNRGKGIY SDFSINCGGP 420 QIRSATGAIF ERDDEDLGSA SFVVSDVQRW AASSVGYFAG SSNNIWVVNT LDSEIFQSAR 480 QSSSSRRYYG LGLENGGYTV TLQFAEIDIL GTNSWRGLGR RRFDIYVQGK LVEKDFDIRK 540 TACDTTVQAV QREYKTNVSE NYLEIHLLWA GKGSFSIPVL GTYGPLISAV SAKPVKVLSV 600 GSRHGKGQFV AEIITISSVL HRNLVKLYGC CYEGDHRLLV YEYLPNGSLD HALFGGKKAL 660 HLDWPTRFEI CLGVARGLAY LHEEVSVRIV HRDVKAINIL LDSKLLPIVS DFGLAKLYDD 720 KKTHISTRVA GTIGYLAPEY AMRGHLTEKT DVYAFGVVVL ELVSGRPNFD MSLDDEKKYL 780 LEWAWNLHEK SREVELIDHK LTEFNMEEVK RMIGIALLCI QASHALRPPM SKVVAMLSGD 840 LEVSDVTSKP GYLTDLSFED TSKLKLKTQG PLRPTPRAL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 3.0e-37 | 571 | 782 | 222 | + 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. | ||
pfam07714 | Pkinase_Tyr | 3.0e-38 | 571 | 780 | 215 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 4.0e-39 | 571 | 780 | 214 | + 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 | 1.0e-41 | 571 | 780 | 214 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 4.0e-44 | 413 | 590 | 180 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAF02838.1 | 0 | 1 | 594 | 16 | 614 | AC009894_9 Similar to serine/threonine kinases [Arabidopsis thaliana] |
GenBank | AAF02838.1 | 0 | 595 | 862 | 718 | 984 | AC009894_9 Similar to serine/threonine kinases [Arabidopsis thaliana] |
Swiss-Prot | C0LGH3 | 0 | 2 | 603 | 43 | 625 | Y5614_ARATH RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g56140; Flags: Precursor |
RefSeq | NP_176009.1 | 0 | 1 | 594 | 43 | 617 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
RefSeq | NP_176009.1 | 0 | 595 | 862 | 721 | 987 | leucine-rich repeat family protein / protein kinase family protein [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 | 558 | 840 | 28 | 309 | A Chain A, Arabidopsis Thaliana Peroxidase N |
PDB | 3uim_A | 0 | 558 | 840 | 28 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 558 | 840 | 36 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 558 | 840 | 36 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 558 | 840 | 36 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
GR452330 | 257 | 606 | 862 | 0 |
EE563239 | 249 | 607 | 855 | 0 |
FY446223 | 252 | 609 | 859 | 0 |
DN774187 | 235 | 153 | 387 | 0 |
DK474396 | 251 | 353 | 603 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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