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Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10011128m |
Family | CBM57 |
Protein Properties | Length: 1009 Molecular Weight: 110838 Isoelectric Point: 7.1698 |
Chromosome | Chromosome/Scaffold: 1 Start: 10158338 End: 10164260 |
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 | 405 | 571 | 9.8e-25 |
HINCGGESENIPTSLGKITYQADNSETKAATNQHFENWGVSSTGYLPNDIYIISPSLPLSGDSPIFYKTARQSALSLSYYAFCLKNGAYNVKLHFMEIQF SNKDLSSSLGIRIFDIYVQGELFVKDFNIKEDANGTLKPVVKEANANVTNHMLEIRLYWAGKGTTLI |
Full Sequence |
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Protein Sequence Length: 1009 Download |
MSILFSIFLL FTIITTFLAA LRTSAISPVL HPDELKALGE IASTLGITRL NLHYGDPCAL 60 GGLKMDVAPI LGSENTIVCD CNINNSTSCH ITNIILKTLS LPGKLPPELV KLPYLRSIDL 120 CRNYLSGSIP MEWASMPHLT FISLCANRLS GNLPSGLQNF KNLTFLGLEA NQFSGPIPDE 180 IGNLINLEKL HLASNQFTGS LPSTLAKLVN LQDFRVSDNN FDGIIPGYIG NWSRLRILYL 240 HASGLKGPIP TNIFRLQNLT DVRIIDMTTE INSFPFIPSK AMEILILRNM SLSGPIPSYI 300 WNMPVLRTLD LSFNQLTGEV QSALKKPPQY TYLTGNMLSG NVGSDVFLNS KSYIDLSYNN 360 FSYSSSCQDK SNINTYRSSY LKNNLTGLLP CSGPIKCTRY QSSLHINCGG ESENIPTSLG 420 KITYQADNSE TKAATNQHFE NWGVSSTGYL PNDIYIISPS LPLSGDSPIF YKTARQSALS 480 LSYYAFCLKN GAYNVKLHFM EIQFSNKDLS SSLGIRIFDI YVQGELFVKD FNIKEDANGT 540 LKPVVKEANA NVTNHMLEIR LYWAGKGTTL IPQRGNYGPL ISAISLCHSL EPQCGAEKTE 600 HHTKYPLIVG VTIASVTVVL SAMGIYAWKR SRGDKNIIER ELRAQGLQTL CFTWRQLQAA 660 TNNFDEANKL GEGGFGSVFK GELSDGTIIA VKQLSSKSCQ GNREFVNEIG MISGLNHPNL 720 VKLYGCCVEK DHLLLVYEYM KNNSLAHPLF EKGSLKLEWA ARQQICLGIA RGLAFLHEGS 780 AMRMVHRDIK TTNVLLDAGL NAKISDFGLA RLHEAEHSHI STKIAGTIGY MAPEYALWGQ 840 LTEKADVYSF GVVAMEIVSG KSNTKQQGNV PLINWALTLQ QTGDIMEIVD AMLKGEFNNN 900 EAARMIKVAL VCINSSPSLR PTMSEVVQML EGEMEIPQVM SGPGLYGPNW SISKLKEIDT 960 DGSSSKFGVT DHQTTTTVKS SASGSDLYPL YPESMILNST IEFSSSSL* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 1.0e-51 | 669 | 930 | 270 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam07714 | Pkinase_Tyr | 1.0e-52 | 669 | 930 | 270 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 3.0e-53 | 669 | 930 | 270 | + 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 | 2.0e-54 | 403 | 584 | 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. | ||
cd00192 | PTKc | 1.0e-54 | 668 | 931 | 282 | + 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. |
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 | AAG10622.1 | 0 | 33 | 1004 | 65 | 1013 | AC008030_22 Putative receptor-like serine/threonine kinase - partial protein [Arabidopsis thaliana] |
GenBank | AAG50772.1 | 0 | 33 | 1008 | 7 | 920 | AC079288_1 receptor-like serine/threonine kinase (RFK1), putative [Arabidopsis thaliana] |
GenBank | AAG50774.1 | 0 | 1 | 995 | 16 | 968 | AC079288_3 receptor protein kinase, putative [Arabidopsis thaliana] |
RefSeq | NP_174266.2 | 0 | 2 | 997 | 13 | 966 | ATP binding / kinase/ protein binding / protein kinase/ protein serine/threonine kinase/ protein tyrosine kinase [Arabidopsis thaliana] |
RefSeq | NP_174267.4 | 0 | 1 | 995 | 16 | 1006 | 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 | 652 | 933 | 20 | 309 | A Chain A, Structural Insights Into The Processivity Of Endopolygalacturonase I From Aspergillus Niger |
PDB | 3uim_A | 0 | 652 | 933 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 652 | 933 | 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 | 652 | 933 | 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 | 652 | 933 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |