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Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 474473 |
Family | CBM57 |
Protein Properties | Length: 1038 Molecular Weight: 114980 Isoelectric Point: 5.5589 |
Chromosome | Chromosome/Scaffold: 1 Start: 28533247 End: 28545852 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 412 | 592 | 7.2e-26 |
INCGGNRLKVDKDEYADDLNKRGASTFSSVSERWGYSSSGAWLGNDSAPYLATDTFNLINESTPEYYKTARLASQSLKYYGLCMRRGSYKVQLHFAEIMF SNDQTYSSLGQRVFDIYVQGILLERDFNIAERAGGVGKPFLRQIDDVQVNGSTLEIHLKWLGKGTNVIPTRGVYGPLISAI |
Full Sequence |
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Protein Sequence Length: 1038 Download |
MGFIFSTKEV VYVLLLIFIC LENFGSNAQL LPDDEVQTLR TIFRKLQNQT VNIERTSCTD 60 ENWNFVAGSS PNAVTSNITC DCTFNASSVC RVTNIQLRGF NLRGIIPPEF GNLTRLTEID 120 LMLNFLSGTI PTTLSQIPLE ILAVTGNRLS GPFPPQLGEI TTLTDVVMET NLFTGQLPSN 180 LGNLRSLKRL LISSNNITGR IPESLSNLKN LTDFRIDGNS LTGKIPDFIG NWTRLVRLDL 240 QGTSMEGPIP ASISNLKNLT QLRVTDLRGP TSPFPDLQNM TNMERLVLRN CLIREPIPEY 300 IGTSMSMLKL LDLSSNMLNG TIPDTFRSLT AFNFMYLNNN SLTGPVPQFI INSKENIDLS 360 DNNFTQPPTL SCNQLDVNLI SSYPSVTDNS VQWCLRKDLP CPGDAHHSSL FINCGGNRLK 420 VDKDEYADDL NKRGASTFSS VSERWGYSSS GAWLGNDSAP YLATDTFNLI NESTPEYYKT 480 ARLASQSLKY YGLCMRRGSY KVQLHFAEIM FSNDQTYSSL GQRVFDIYVQ GILLERDFNI 540 AERAGGVGKP FLRQIDDVQV NGSTLEIHLK WLGKGTNVIP TRGVYGPLIS AITITPNFKV 600 DTGKPLSNKA VAGIVIAACA AFGLLVLVIL WLTGYLGGKE VDENEELRGL DLQTGSFTLK 660 QIKRATNNFD PENKIGEGGF GPVYKGVLAD GMTIAVKQLS SKSKQGNREF VTEIGMISAL 720 QHPNLVKLYG CCIEGKELLL VYEYLENNSL ARALFGTEKQ RLHLDWSTRN KICLGIAKGL 780 AYLHEESRLK IVHRDIKATN VLLDQSLNAK ISDFGLAKLD EEENTHISTR IAGTIGYMAP 840 EYAMRGYLTD KADVYSFGVV CLEIVSGKSN TNYRPKEEFI YLLDWAYVLQ EQGSLLELMD 900 PDLGTSFSKK EAMRMLNIAL LCTNPSPTLR PPMSSVVRML EGKIKVQPPL VKREADPSGS 960 AAMRFKAFEL LSQDSESQVS THTSNREHKS SSSMDGPWVD SSFSEPSKDV SLQQQEEGNS 1020 SSSSRRLLDD LTDVEIE* 1080 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 1.0e-41 | 674 | 940 | 281 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 9.0e-44 | 673 | 941 | 288 | + 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 | 1.0e-45 | 672 | 940 | 282 | + 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-47 | 672 | 940 | 282 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 4.0e-52 | 409 | 592 | 186 | + 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 - 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 | 653 | 942 | 16 | 308 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3uim_A | 0 | 653 | 942 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 653 | 942 | 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 | 653 | 942 | 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 | 653 | 942 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |