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Basic Information | |
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Species | Arabidopsis thaliana |
Cazyme ID | AT1G29730.1 |
Family | CBM57 |
Protein Properties | Length: 970 Molecular Weight: 107675 Isoelectric Point: 7.4699 |
Chromosome | Chromosome/Scaffold: 1 Start: 10400564 End: 10405874 |
Description | receptor-like protein kinase 2, putative, expressed |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 413 | 578 | 1.2e-26 |
HINCGGPDVTIENSRGRFLYEGDNYGLTGSATNYYRKNWGYSNTGDFMDDAITEDTYTVSSESAVSAKYPDLYQNARRSPLSLAYYAFCFENGSYNVKLH FAEIQFSDVEPYTKLAKRVFNIYIQGKLIWEDFSIREEANGTHKEVIREVNTTVTDNTLEIRLYWA |
Full Sequence |
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Protein Sequence Length: 970 Download |
MSAAYNLMIK SKSCLFSSSI LFVVTLIYLL CTVSASPSLH PDEVEALKDI TETLGVKHLN 60 LSEDPCLTKT LVISQGVLKE GQNSTIRCDC HFNNYSTCHI KHFVLQKFNL PGRLPPMLYK 120 FRHLESIDLY NNYLYGSIPM EWASLPYLKS ISVCANRLSG DIPKGLGKFI NLTLLVLEAN 180 QFSGTIPKEL GNLVNLQGLG LSSNQLVGGL PKTLAKLTKL TNLHLSDNRL NGSIPEFIGK 240 LPKLQRLELY ASGLRGPIPD SIFHLENLID VRISDTVAGL GHVPQITSTS LKYLVLRNIN 300 LSGPIPTSIW DLPSLMTLDL SFNRLTGEIP AYATAPKYTY LAGNMLSGKV ETGAFLTAST 360 NIDLSYNNFT WSPMCKERKN INTYESSHSK NRLTRLLPCS AIKQCQNYSR SLHINCGGPD 420 VTIENSRGRF LYEGDNYGLT GSATNYYRKN WGYSNTGDFM DDAITEDTYT VSSESAVSAK 480 YPDLYQNARR SPLSLAYYAF CFENGSYNVK LHFAEIQFSD VEPYTKLAKR VFNIYIQGKL 540 IWEDFSIREE ANGTHKEVIR EVNTTVTDNT LEIRLYWAGK GTMIIPQRGY YGSLISAVSV 600 CPSSESECGG MKKKISKLKG PDLRTGSFSL RQLKVATNDF DPLNKIGEGG FGSVYKGRLP 660 DGTLIAVKKL SSKSHQGNKE FVNEIGMIAC LQHPNLVKLY GCCVEKNQLL LVYEYLENNC 720 LSDALFAGRS CLKLEWGTRH KICLGIARGL AFLHEDSAVK IIHRDIKGTN VLLDKDLNSK 780 ISDFGLARLH EDNQSHITTR VAGTIGYMAP EYAMRGHLTE KADVYSFGVV AMEIVSGKSN 840 AKYTPDDECC VGLLDWAFVL QKKGDIAEIL DPRLEGMFDV MEAERMIKVS LLCANKSSTL 900 RPNMSQVVKM LEGETEIEQI ISDPGVYSDN LHFKPSSLSS DYILSIPSSS ESAYDLYPLS 960 PESIVFTIQ* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 2.0e-49 | 644 | 912 | 289 | + 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. | ||
pfam00069 | Pkinase | 1.0e-49 | 645 | 838 | 198 | + Protein kinase domain. | ||
smart00221 | STYKc | 4.0e-50 | 643 | 911 | 278 | + 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 | 3.0e-50 | 643 | 911 | 278 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 9.0e-57 | 411 | 598 | 190 | + 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:0004674 | protein serine/threonine 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 | AAG10621.1 | 0 | 1 | 969 | 1 | 947 | AC008030_21 Putative receptor-like serine/threonine kinase [Arabidopsis thaliana] |
GenBank | AAG50774.1 | 0 | 1 | 964 | 1 | 968 | AC079288_3 receptor protein kinase, putative [Arabidopsis thaliana] |
GenBank | AAG50775.1 | 0 | 1 | 969 | 1 | 940 | AC079288_4 receptor-like serine/threonine kinase, putative [Arabidopsis thaliana] |
RefSeq | NP_174266.2 | 0 | 1 | 969 | 1 | 969 | ATP binding / kinase/ protein binding / protein kinase/ protein serine/threonine kinase/ protein tyrosine kinase [Arabidopsis thaliana] |
RefSeq | NP_174267.4 | 0 | 1 | 964 | 1 | 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 | 621 | 914 | 10 | 309 | A Chain A, Structure Of Mth11: A Homologue Of Human Rnase P Protein Rp |
PDB | 3uim_A | 0 | 621 | 914 | 10 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 621 | 914 | 18 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 621 | 914 | 18 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 621 | 914 | 18 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |