| Basic Information | |
|---|---|
| Species | Arabidopsis thaliana |
| Cazyme ID | AT1G56130.1 |
| Family | CBM57 |
| Protein Properties | Length: 1033 Molecular Weight: 113042 Isoelectric Point: 6.8959 |
| Chromosome | Chromosome/Scaffold: 1 Start: 20994931 End: 21000887 |
| Description | SHR5-receptor-like kinase, putative, expressed |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 428 | 597 | 6e-24 |
| SINCGGPEKRSVTGALFEREDEDFGPASFFVSAGQRWAASSVGLFAGSSNNIYIATSQSQFVNTLDSELFQSARLSASSVRYYGLGLENGGYTVTLQFAE IQILGSTSTTWKGLGRRRFDIYVQGRLVEKDFDVRRTAGDSTVRAVQRVYKANVSENHLEVHLFWAGKGT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1033 Download |
| MTRIRRSPCL LLLIIWFMCI AGSVQVVQSQ NQTGATTHPD EARALNSIFA AWKIQAPREW 60 NISGELCSGA AIDASVLDSN PAYNPLIKCD CSFQNSTICR ITNIKVYAID VVGPIPPELW 120 TLTYLTNLNL GQNVLTGSLP PAIGNLTRMQ WMTFGINALS GPVPKEIGLL TDLRLLGISS 180 NNFSGSIPDE IGRCTKLQQM YIDSSGLSGR IPLSFANLVQ LEQAWIADLE VTDQIPDFIG 240 DWTKLTTLRI IGTGLSGPIP SSFSNLTSLT ELRLGDISSG SSSLDFIKDM KSLSVLVLRN 300 NNLTGTIPST IGEHSSLRQV DLSFNKLHGP IPASLFNLSQ LTHLFLGNNT LNGSFPTQKT 360 QSLRNVDVSY NDLSGSLPSW VSLPSLKLNL VANNFTLEGL DNRVLPGLNC LQKNFPCNRG 420 KGIYSDFSIN CGGPEKRSVT GALFEREDED FGPASFFVSA GQRWAASSVG LFAGSSNNIY 480 IATSQSQFVN TLDSELFQSA RLSASSVRYY GLGLENGGYT VTLQFAEIQI LGSTSTTWKG 540 LGRRRFDIYV QGRLVEKDFD VRRTAGDSTV RAVQRVYKAN VSENHLEVHL FWAGKGTCCI 600 PIQGAYGPLI SAVSATPDFT PTVANKPPSK GKNRTGTIVG VIVGVGLLSI LAGVVMFTIR 660 KRRKRYTDDE ELLGMDVKPY IFTYSELKSA TQDFDPSNKL GEGGFGPVYK GNLNDGRVVA 720 VKLLSVGSRQ GKGQFVAEIV AISSVLHRNL VKLYGCCFEG EHRMLVYEYL PNGSLDQALF 780 GDKTLHLDWS TRYEICLGVA RGLVYLHEEA SVRIVHRDVK ASNILLDSRL VPQISDFGLA 840 KLYDDKKTHI STRVAGTIGY LAPEYAMRGH LTEKTDVYAF GVVALELVSG RPNSDENLEE 900 EKKYLLEWAW NLHEKSRDIE LIDDKLTDFN MEEAKRMIGI ALLCTQTSHA LRPPMSRVVA 960 MLSGDVEIGD VTSKPGYVSD WRFDDTTGSS LSGFQIKDTT GYSMSLVAPG SEISPRDSDF 1020 KPMLGSKINE GR* 1080 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00192 | PTKc | 2.0e-47 | 698 | 889 | 207 | + 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 | 2.0e-48 | 699 | 889 | 197 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| cd00180 | PKc | 1.0e-48 | 700 | 887 | 192 | + 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. | ||
| smart00219 | TyrKc | 1.0e-49 | 699 | 889 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| pfam11721 | Malectin | 7.0e-52 | 427 | 613 | 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 | |
|---|---|
| GO Term | Description |
| GO:0004672 | protein kinase activity |
| GO:0004674 | protein serine/threonine kinase activity |
| GO:0005515 | protein binding |
| GO:0005524 | ATP binding |
| GO:0005886 | plasma membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAF02838.1 | 0 | 42 | 1032 | 15 | 1029 | AC009894_9 Similar to serine/threonine kinases [Arabidopsis thaliana] |
| GenBank | AAG50909.1 | 0 | 11 | 1032 | 1026 | 2062 | AC069159_10 receptor protein kinase, putative [Arabidopsis thaliana] |
| Swiss-Prot | C0LGH3 | 0 | 1 | 1032 | 1 | 1033 | Y5614_ARATH RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g56140; Flags: Precursor |
| RefSeq | NP_176009.1 | 0 | 1 | 1032 | 1 | 1032 | leucine-rich repeat family protein / protein kinase family protein [Arabidopsis thaliana] |
| RefSeq | NP_564709.1 | 0 | 1 | 1032 | 1 | 1032 | 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 | 682 | 965 | 20 | 309 | A Chain A, Rice Bglu1 Beta-Glucosidase, A Plant ExoglucanaseBETA-Glucosidase |
| PDB | 3uim_A | 0 | 682 | 965 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 682 | 965 | 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 | 682 | 965 | 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 | 682 | 965 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
