Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.E02839.1 |
Family | CBM57 |
Protein Properties | Length: 928 Molecular Weight: 103072 Isoelectric Point: 6.4628 |
Chromosome | Chromosome/Scaffold: 5 Start: 46386777 End: 46395731 |
Description | receptor-like kinase in flowers 1 |
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 | 361 | 533 | 8e-25 |
LQVNCGGKDATIEESKQKIIYQGDQDVEGGAAKFYLNYDKFWGFSSTGDFLDDNDAQNLRYNVDLLPSNLTVLDSTARIAAISLTYFHYCLENGMYTVKL RFAEIQFTNDKTYKSLGRRVFDIYVQGELILKDYDIEVAAGGAQKPREEVYNVNVTNNMLEIRLIFAGKGTAR |
Full Sequence |
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Protein Sequence Length: 928 Download |
MAGKNSFVFL IFMGLSCFRL VWLAESRLPQ SEVDALHEIM SAMGLTFWDF DGDNCEIRRV 60 GLGLQLPAEA ESSIGCDCNI GNDTFCHVVR IVLKFYSLPG ILPPELAKLP YLGEIDFAYN 120 YLSGEIPDEL GSMQLTSISL LVNRLSGAIP KSLTNITSLI YLRINDNNFN GKIPSFIQNW 180 KQLNILEMHA SGLEGPIPSL ISALNKVEEL RISDIDGPLQ LFPALDNMTG LVKLLVILRS 240 CNIAGQIPAY MWKLPNLELL DLSFNKLTGQ LPATINLKHL RFIFLTENLL TGSVPDSILK 300 KGTSIDLSYN NFAWQGPHQP ACRESMNLNL NLFRSSSAEN NSGRGVPCLE NFQCPHYSSC 360 LQVNCGGKDA TIEESKQKII YQGDQDVEGG AAKFYLNYDK FWGFSSTGDF LDDNDAQNLR 420 YNVDLLPSNL TVLDSTARIA AISLTYFHYC LENGMYTVKL RFAEIQFTND KTYKSLGRRV 480 FDIYVQGELI LKDYDIEVAA GGAQKPREEV YNVNVTNNML EIRLIFAGKG TARIPMSGVY 540 GPLISSISVV SDVKGCSRGG KQKTAYVIVG VGAGAFCIFL LSLCILKWKG YFRGRTKRRQ 600 GMDGLDLQTG TFSLKQIKAA TNDFDSANKI GEGGFGAVYK GQLNDGTAMA VKQLSSKSRQ 660 GNREFLNEIG MISCLQHPNL VKLHGCCIER DQLLLVYEYM ENNSLARALF GPDDHQLQLD 720 WSTRHKICTG IAKGLAFLHE ESRLKIVHRD IKATNVLLDR DLNPKISDFG LARLHEEEKT 780 HISTKIAGTI GYMAPEYALW GYLTYKADVY SFGVVALEIV SGKSNNSSPP SDDFFCLLEW 840 GCHLQQTGNL MRLVDEKLKA EVNEEEAKIV AKVALLCTNA SPSLRPTMSE VVNMLEGKMA 900 IPDVILESST YCEDLRFKAM RDLRKHG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 6.0e-50 | 629 | 895 | 279 | + Protein tyrosine kinase. | ||
cd00180 | PKc | 4.0e-50 | 630 | 819 | 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. | ||
smart00221 | STYKc | 5.0e-52 | 629 | 895 | 274 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00192 | PTKc | 4.0e-52 | 628 | 896 | 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. | ||
smart00219 | TyrKc | 3.0e-53 | 629 | 895 | 274 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
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 |
RefSeq | NP_174268.7 | 0 | 5 | 925 | 20 | 982 | RKF1 (RECEPTOR-LIKE KINASE IN FLOWERS 1); ATP binding / kinase/ protein serine/threonine kinase/ receptor signaling protein serine/threonine kinase [Arabidopsis thaliana] |
RefSeq | XP_002264679.1 | 0 | 31 | 926 | 4 | 968 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264878.1 | 0 | 21 | 926 | 100 | 1027 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002305711.1 | 0 | 33 | 926 | 1 | 903 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522277.1 | 0 | 43 | 926 | 1 | 878 | 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 | 608 | 897 | 16 | 308 | A Chain A, Arabidopsis Thaliana Peroxidase A2 |
PDB | 3uim_A | 0 | 608 | 897 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 608 | 897 | 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 | 608 | 897 | 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 | 608 | 897 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |