| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.018G111800.1 |
| Family | GH18 |
| Protein Properties | Length: 594 Molecular Weight: 66983.7 Isoelectric Point: 5.4413 |
| Chromosome | Chromosome/Scaffold: 18 Start: 13775419 End: 13778620 |
| Description | cysteine-rich RLK (RECEPTOR-like protein kinase) 34 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH18 | 3 | 255 | 2.50006e-41 |
| NQSSYRKSFIESSIYTARLYGFDGLDLSVGPSMSINMTNLGILFDEWRDAIASDSRKSGKSQLLLVMSATHSPAQHSATYPIDIMKKTLDWIHLVAYDYH VPAEFNFTGAHAALYGTSNWVNTDEWIKEWLRGGLSASKLVLGLPYHGYAWKLVNPNEKEFGAPSSGPDVTSDGSMGYKNIKSFIQGYGYGAAAVYNSTY VTKLFVVGSTWINFDDVETIKAKISYAKENNLSGYSVFQLSNDDNWNLSRAVI | |||
| Full Sequence |
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| Protein Sequence Length: 594 Download |
| MINQSSYRKS FIESSIYTAR LYGFDGLDLS VGPSMSINMT NLGILFDEWR DAIASDSRKS 60 GKSQLLLVMS ATHSPAQHSA TYPIDIMKKT LDWIHLVAYD YHVPAEFNFT GAHAALYGTS 120 NWVNTDEWIK EWLRGGLSAS KLVLGLPYHG YAWKLVNPNE KEFGAPSSGP DVTSDGSMGY 180 KNIKSFIQGY GYGAAAVYNS TYVTKLFVVG STWINFDDVE TIKAKISYAK ENNLSGYSVF 240 QLSNDDNWNL SRAVINSDAP NLQALSFDTI AAATNNFSSE NKLGTGGFGS VYKGKLPNGK 300 EIAVKRLSKT STQGEEEFKN EVTLTEKLQH VNIVTVLGFC AEREEKMLIY EYMPNKSLDI 360 YIYDPIRRYM LDWRKRVQII EGLTQGLLYL QEYSNFTIIH RDIKSSNVLL DEEMNPKISD 420 FGMARLFRKD ELEANTSRIV GTYGYVPPEY VRKGIYSMKY DVYSFGVLLL QIISGKKSTC 480 YYGADENWNL LEYAYELWKD GEGVEFFDPS LDDSFSSCKL TRCLQVALLC VQENPLDRPS 540 MLKISSMLKN ENAPIATPKR PSFSTKRDEE EDSVNRNKIY SVNDATISDL EPR* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00221 | STYKc | 4.0e-45 | 280 | 548 | 277 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| smart00636 | Glyco_18 | 2.0e-45 | 1 | 245 | 260 | + Glyco_18 domain. | ||
| pfam00704 | Glyco_hydro_18 | 1.0e-45 | 1 | 245 | 247 | + Glycosyl hydrolases family 18. | ||
| cd00180 | PKc | 1.0e-47 | 283 | 472 | 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. | ||
| cd02879 | GH18_plant_chitinase_class_V | 2.0e-69 | 1 | 251 | 256 | + The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0004672 | protein kinase activity |
| GO:0005524 | ATP binding |
| GO:0005975 | carbohydrate metabolic process |
| GO:0006468 | protein phosphorylation |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_002263709.1 | 0 | 1 | 593 | 118 | 764 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002263792.1 | 0 | 1 | 593 | 106 | 753 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002270006.1 | 0 | 1 | 593 | 118 | 765 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324558.1 | 0 | 1 | 593 | 109 | 763 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523520.1 | 0 | 1 | 593 | 87 | 721 | conserved hypothetical protein [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 261 | 552 | 16 | 310 | A Chain A, Crystal Structure Of Class V Chitinase (E115q Mutant) From Nicotiana Tobaccum In Complex With Nag4 |
| PDB | 3uim_A | 0 | 261 | 552 | 16 | 310 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 261 | 551 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 261 | 551 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 261 | 551 | 24 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| GO916691 | 263 | 299 | 561 | 0 |
| CX667178 | 260 | 337 | 594 | 0 |
| EC924914 | 257 | 322 | 578 | 0 |
| CV630371 | 214 | 251 | 464 | 0 |
| HO783910 | 341 | 256 | 594 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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