Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.019G006000.1 |
Family | CBM57 |
Protein Properties | Length: 965 Molecular Weight: 107129 Isoelectric Point: 7.7649 |
Chromosome | Chromosome/Scaffold: 19 Start: 699797 End: 709413 |
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 | 365 | 547 | 3.7e-29 |
VHINCGGPEATIGNTIYEADDEPGGAAKYVSKREDWQTSTTGHIWDVPASLDNYIAQNKSMLRMDNSVLYTNARLTPLSLTYHVRCLVNGKYKVKLHFAE IVMRDNRSYYSLGRRIFDVYIQDIVVLKDFDIVKEAGGVDKVYIHNYTAPVTNGALEIRLHWAGKGTTRSPKKGIYGPLISAI |
Full Sequence |
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Protein Sequence Length: 965 Download |
MLTLEALLEV ATQLGKKGWN RNMTLCTDTI LPPESDADNK VVCNCSFPGG VCRVIAIYLK 60 RQDLNGSLPK AIEKLPHLKH LDLWTNYLSG NIPSEWANTK LEILSIGVNH LTGKIPSYLG 120 NITTLRSLNI QDNMFSGTVP PELGGLVNLE NLTLSANYLT GELPPALTNL TGLKELRLSS 180 NNFTGRIPDF IQSWKQLDTL EIQAGGFTGP IPSSISLLTD LTDLKISNLL GDGSEFPHLE 240 SIKGIKYLLL SNCNLSGNFP IYLTRMAQLK ILDLSFNRLN GSLPEKYEGL QSLEKMYLTR 300 NMFTGTIPEW INQRDTSSEI DLSYNNFTSE AKCRETLNLF KSTWGGNYSK PVECLSACSE 360 ERYSVHINCG GPEATIGNTI YEADDEPGGA AKYVSKREDW QTSTTGHIWD VPASLDNYIA 420 QNKSMLRMDN SVLYTNARLT PLSLTYHVRC LVNGKYKVKL HFAEIVMRDN RSYYSLGRRI 480 FDVYIQDIVV LKDFDIVKEA GGVDKVYIHN YTAPVTNGAL EIRLHWAGKG TTRSPKKGIY 540 GPLISAIDVE SDFKPPNKGR RKRFIVAGAV VLSLFLVFIL LSSLWWKGYL GGRKSRDREL 600 VGLDLLTGIF TFRQIKAATN DFDPANKLGE GGFGCVYKGV LSDGTRIAVK QLSAKSKQGN 660 REFVNEIGMI SALQHPNLVR LYGCCIEGKQ LLLAYEYMEN NSLAHVLFGT KEIKATKLDW 720 RTRQRICVSI AKGLVFLHEE STLKIVHRDI KGTNILLDKD MNAKISDFGM AKLDDEDNTH 780 IDTRIAGTMG YMAPEYALYG YLTYKADVYS FGVVALEIVS GMNNVKFRRD ENFVCLLDRA 840 LYLQKNGDIM EMVDPRLGSE FNKKEVVRMI NVALLCTNQS PALRPTMSTV VSMLEGKTDV 900 EDLVMVPSTL VDPSGYATAL HNKFAQSSVS GSLSESQSLV KSSEGPWTAS SSSSAQDLYP 960 ISKS* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
smart00219 | TyrKc | 3.0e-48 | 627 | 894 | 283 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
smart00221 | STYKc | 6.0e-49 | 627 | 894 | 283 | + 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 | 2.0e-49 | 628 | 818 | 195 | + 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 | 9.0e-52 | 626 | 895 | 287 | + 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 | 2.0e-53 | 363 | 547 | 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 |
EMBL | CBI30745.1 | 0 | 13 | 957 | 950 | 1900 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002300205.1 | 0 | 4 | 959 | 1 | 960 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331887.1 | 0 | 4 | 964 | 42 | 989 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522279.1 | 0 | 4 | 961 | 40 | 982 | ATP binding protein, putative [Ricinus communis] |
RefSeq | XP_002528777.1 | 0 | 6 | 958 | 45 | 975 | ATP binding protein, putative [Ricinus communis] |
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 | 610 | 896 | 20 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 610 | 896 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 610 | 896 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 610 | 896 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 610 | 896 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |