Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10012029m |
Family | CBM57 |
Protein Properties | Length: 950 Molecular Weight: 105811 Isoelectric Point: 5.4107 |
Chromosome | Chromosome/Scaffold: 7 Start: 1097806 End: 1102884 |
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 | 363 | 533 | 1.2e-29 |
YINCGGDEVTINGTMYEADKYDRLESLYESQNGWFSSNIGVFVDDKHVPERVTIGSNTSELNVVDSSLYTQARLSAISLTYYALCLGNGNYNVTLHFAEI LFSGNNTYQSLGRRFFDIYIQRKLEVKDFNIVEEAKGVGNVVVKTFPVEITDGKLEIRLSWAGKGTTVIPT |
Full Sequence |
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Protein Sequence Length: 950 Download |
MLFNRSFFTS FLLFLIFLFG CASSATLPTR EAEAFKAALT TLKKTNIDLN VDPCEVSSTG 60 NRHLKEENLQ GSLPKEFVGL PFLQDIDLSR NYLNGSIPPE WEVLPLVNIS LLGNRLTGPI 120 PKEVGNITTL TNLVLEANQL SGELPPELGN LPNIQQIILS SNNFIGEIPT TFAKLTTLRD 180 FRVSDNQLTG TIPDFIQNWT KLERLFIQAS GLVGPIPMAI APLAELKDLR ISDLNGPESP 240 FPPLKNTTKM ETLILRSCNL TGDLPSYLGN LASLKLLDLS FNKLSGTIPS TYSNLSDGCY 300 LYLTGNMLNG SIPIWMINKG YRIDLSYNNF SVDPSPTNAV CQYNDVVSCM RSYQCPKTFN 360 GLYINCGGDE VTINGTMYEA DKYDRLESLY ESQNGWFSSN IGVFVDDKHV PERVTIGSNT 420 SELNVVDSSL YTQARLSAIS LTYYALCLGN GNYNVTLHFA EILFSGNNTY QSLGRRFFDI 480 YIQRKLEVKD FNIVEEAKGV GNVVVKTFPV EITDGKLEIR LSWAGKGTTV IPTEDVYGPL 540 ISAISVDPNF KAPPRSGMST TLHVVAVMAY VFLILLIFVL IGMLLKISHS RSRNQMGRDF 600 RSLDPMISSF SLRQIKTATN NFDLANRIGE GGFGPVHKGE LSDGTIIAVK QLSTGSRQGN 660 REFLNEIGMI SALHHPNLVK LYGCCAEGDQ LLLVYEFVEN NSLARALFGP QETQLRLDWP 720 TRLKICIGVA RGLAYLHEES RLKIVHRDIK ATNVLLDKDL NPKISDFGIA KLNEEDSTHI 780 STRVAGTFGY MAPEYAMRGH LTDKADVYSF GIVALEIVHG RSNKTDLSNN YTYLIDWVEI 840 LREQNNLLEL VDPRLGSDYN REEAMTMIQV VIMCTSQDPS DRPLMSEVVK MLEGKKVVQM 900 EKLEEASIHR ETKRLENINT MKKYYEMIGN EISTSMSMTL TDQSTSSEH* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 2.0e-48 | 628 | 892 | 277 | + Protein tyrosine kinase. | ||
smart00221 | STYKc | 4.0e-50 | 628 | 892 | 272 | + 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 | 7.0e-51 | 628 | 892 | 272 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 5.0e-54 | 626 | 893 | 281 | + 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. | ||
pfam11721 | Malectin | 6.0e-56 | 362 | 544 | 188 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAF69542.1 | 0.0000000002 | 64 | 284 | 71 | 267 | AC008007_17 F12M16.30 [Arabidopsis thaliana] |
GenBank | AAF69542.1 | 0 | 111 | 947 | 36 | 851 | AC008007_17 F12M16.30 [Arabidopsis thaliana] |
GenBank | ACN59317.1 | 0 | 1 | 929 | 7 | 979 | leucine-rich repeat receptor-like protein kinase [Arabidopsis thaliana] |
RefSeq | NP_175747.2 | 0 | 22 | 947 | 22 | 950 | serine/threonine protein kinase-related [Arabidopsis thaliana] |
RefSeq | NP_188102.4 | 0 | 1 | 929 | 7 | 976 | leucine-rich repeat family protein / protein kinase family protein [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 | 607 | 905 | 17 | 317 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 3uim_A | 0 | 607 | 905 | 17 | 317 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 607 | 905 | 25 | 325 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 607 | 905 | 25 | 325 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 607 | 905 | 25 | 325 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |