| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G53430.2 |
| Family | CBM57 |
| Protein Properties | Length: 998 Molecular Weight: 110231 Isoelectric Point: 5.7305 |
| Chromosome | Chromosome/Scaffold: 1 Start: 19935163 End: 19941088 |
| Description | receptor-like protein kinase 2, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 371 | 550 | 1.2e-24 |
| INCGGSRLKIGKDTYTDDLNSRGQSTFSSVSERWGYSSSGVWLGKEDAGYLATDRFNLINGSTPEYYKTARLSPQSLKYYGLCLRRGSYKLQLHFAEIMF SNDQTFNSLGRRIFDIYVQGNLLERDFNIAERAGGVGKPFIRQIDGVQVNGSTLEIHLQWTGKGTNVIPTRGVYGPLISA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 998 Download |
| MAIQTLRTIF RKLQNQTVNI ERTSCSDQNW NFVVESASNS PTSNITCDCT FNASSVCRVT 60 NIQLKSFSLP GIFPPEFGNL TRLREIDLSR NFLNGTIPTT LSQIPLEILS VIGNRLSGPF 120 PPQLGDITTL TDVNLETNLF TGPLPRNLGN LRSLKELLLS ANNFTGQIPE SLSNLKNLTE 180 FRIDGNSLSG KIPDFIGNWT LLERLDLQGT SMEGPIPPSI SNLTNLTELR ITDLRGQAAF 240 SFPDLRNLMK MKRLGPIPEY IGSMSELKTL DLSSNMLTGV IPDTFRNLDA FNFMFLNNNS 300 LTGPVPQFII NSKENLDLSD NNFTQPPTLS CNQLDVNLIS SYPSVTDNSV QWCLREGLPC 360 PEDAKQSSLF INCGGSRLKI GKDTYTDDLN SRGQSTFSSV SERWGYSSSG VWLGKEDAGY 420 LATDRFNLIN GSTPEYYKTA RLSPQSLKYY GLCLRRGSYK LQLHFAEIMF SNDQTFNSLG 480 RRIFDIYVQG NLLERDFNIA ERAGGVGKPF IRQIDGVQVN GSTLEIHLQW TGKGTNVIPT 540 RGVYGPLISA ITITPNFKVD TGKPLSNGAV AGIVIAACAV FGLLVLVILR LTGYLGGKEV 600 DENEELRGLD LQTGSFTLKQ IKRATNNFDP ENKIGEGGFG PVYKGVLADG MTIAVKQLSS 660 KSKQGNREFV TEIGMISALQ HPNLVKLYGC CIEGKELLLV YEYLENNSLA RALFGTEKQR 720 LHLDWSTRNK ICIGIAKGLA YLHEESRLKI VHRDIKATNV LLDLSLNAKI SDFGLAKLND 780 DENTHISTRI AGTIGYMAPE YAMRGYLTDK ADVYSFGVVC LEIVSGKSNT NYRPKEEFVY 840 LLDWAYVLQE QGSLLELVDP DLGTSFSKKE AMRMLNIALL CTNPSPTLRP PMSSVVSMLE 900 GKIKVQPPLV KREADPSGSA AMRFKALELL SQDSESQVST YARNREQDIS SSSMDGPWVD 960 SSFSEPGKDV SLQQQEEGRS SSSSRKLLDD LTDVKIE* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 7.0e-42 | 634 | 823 | 194 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
| cd00192 | PTKc | 2.0e-44 | 632 | 900 | 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. | ||
| smart00221 | STYKc | 5.0e-45 | 631 | 899 | 280 | + 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-46 | 631 | 899 | 280 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| pfam11721 | Malectin | 1.0e-54 | 368 | 551 | 187 | + 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:0005886 | plasma membrane |
| GO:0006468 | protein phosphorylation |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAF78446.1 | 0 | 127 | 997 | 89 | 942 | AC018748_25 Contains similarity to receptor-like serine/threonine kinase from Arabidopsis thaliana gb |
| Swiss-Prot | C0LGG8 | 0 | 3 | 997 | 36 | 1038 | Y5343_ARATH RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g53430; Flags: Precursor |
| RefSeq | NP_001117479.1 | 0 | 1 | 997 | 1 | 997 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| RefSeq | NP_175748.1 | 0 | 3 | 997 | 36 | 1030 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| RefSeq | NP_175749.1 | 0 | 3 | 997 | 34 | 1035 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 612 | 901 | 16 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3uim_A | 0 | 612 | 901 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 612 | 901 | 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 | 612 | 901 | 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 | 612 | 901 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
