Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.K01781.2 |
Family | CBM57 |
Protein Properties | Length: 604 Molecular Weight: 67159.8 Isoelectric Point: 8.0634 |
Chromosome | Chromosome/Scaffold: 11 Start: 22065014 End: 22072148 |
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 | 107 | 271 | 2.3e-27 |
INCGGSKAKVRGITYEDDSQRATPSSFFKSNYWAYSSTGDFTDDDGTAVGYEVKNTSTLSMNNAQLYMEARRSAISLTYYGFCLMDGPYNVTLHFAEIMF TGDKSYKSLGRRAFNIYIQGKLVWKDFNIESEAGGVGKEVMRNFAAIVTKGTLEIRFYWAGKGTT |
Full Sequence |
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Protein Sequence Length: 604 Download |
MTFSVFFKLM RFWKWLTVSL CSDLSYNNFA AGDSECQEGS VYVLLPSVSP GLPPNVHLLT 60 LNFIKNDDDY NSKIFADLLR TSYSATSGLV SCLQSQRCAK TRYNLFINCG GSKAKVRGIT 120 YEDDSQRATP SSFFKSNYWA YSSTGDFTDD DGTAVGYEVK NTSTLSMNNA QLYMEARRSA 180 ISLTYYGFCL MDGPYNVTLH FAEIMFTGDK SYKSLGRRAF NIYIQGKLVW KDFNIESEAG 240 GVGKEVMRNF AAIVTKGTLE IRFYWAGKGT TAIPDVGVYG PLISAISVYP GFDPPASISA 300 GTVAGILTAI VFVVFLILVI LWWRGCLGRK DKMAQDLKGL ASQIGLFTLR QIKAATNNFD 360 AANKIGEGGF GSVYKGFLSD GTTIAVKQLS SKSQQGNNEF LTEIGTISAL QHPHLVKLYG 420 CCIEGNQLLL VYEYMENNSL ARALFGPEEF QLKLDWWTRH KICVGIARGL AYLHEESRLK 480 IVHRDIKATN VLLDKDLNPK ISDFGLAKLD EEEKTHISTK IAGTYGYMAP EYAMHGYLTD 540 KADIYSFGVV ALEVVNGRSN TSSQRTEECF NLLDWHSGRQ CHLWLACLKA RLLFQCWTLR 600 ALS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00069 | Pkinase | 5.0e-48 | 364 | 558 | 199 | + Protein kinase domain. | ||
smart00219 | TyrKc | 7.0e-50 | 364 | 554 | 199 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 3.0e-50 | 364 | 554 | 199 | + 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 | 7.0e-53 | 365 | 553 | 193 | + 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. | ||
pfam11721 | Malectin | 4.0e-55 | 103 | 286 | 187 | + 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: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 | CBI20124.1 | 0 | 23 | 575 | 380 | 906 | unnamed protein product [Vitis vinifera] |
EMBL | CBI20127.1 | 0 | 23 | 574 | 351 | 880 | unnamed protein product [Vitis vinifera] |
EMBL | CBI20136.1 | 0 | 23 | 575 | 55 | 579 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283596.1 | 0 | 23 | 575 | 380 | 906 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002524511.1 | 0 | 23 | 575 | 330 | 854 | 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 | 2qkw_B | 0 | 349 | 575 | 31 | 255 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |
PDB | 3hgk_D | 0 | 349 | 575 | 31 | 255 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_C | 0 | 349 | 575 | 31 | 255 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_B | 0 | 349 | 575 | 31 | 255 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
PDB | 3hgk_A | 0 | 349 | 575 | 31 | 255 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |