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Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G053900.2 |
Family | GH18 |
Protein Properties | Length: 712 Molecular Weight: 79783.3 Isoelectric Point: 8.914 |
Chromosome | Chromosome/Scaffold: 09 Start: 3903541 End: 3906798 |
Description | cysteine-rich RLK (RECEPTOR-like protein kinase) 5 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 180 | 301 | 1.6e-23 |
DFGIREWLNKGMPPSKLVLGLPYHGYAWKLVSSQDNAIGAPSSGPAVNIDGSMGYKAIKSYIRDYGYGATSVYNATYVVNLLTTPTIWINFDDVETIKAK MSYVKEKKLIGFKAFQLSNDDN |
Full Sequence |
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Protein Sequence Length: 712 Download |
MASKIIFFFL FILFPSSQFH LCGAQTLVKA GYWYASGEFP IQDINSALFT HLSYAFADVN 60 ASNYQLLIPS ASQQYLSTFP TIVKRRNPSV KPLLSIWNGI SATGKSIAGE NVTDSVLSSM 120 VSASSKRKSF IDSSIKTARR YGFQGMDLFW VWPNSTDLSN IGVLLDEWRA AINSEQRQPD 180 FGIREWLNKG MPPSKLVLGL PYHGYAWKLV SSQDNAIGAP SSGPAVNIDG SMGYKAIKSY 240 IRDYGYGATS VYNATYVVNL LTTPTIWINF DDVETIKAKM SYVKEKKLIG FKAFQLSNDD 300 NWVLSRAAQE GENQANKQQL LLKIILPVSL IVILAVALLF YLRRRKVQSE AEMVLTSIPS 360 PRINAPAAEN FGSDASHLQV FKFANIKGAT NNFSSANKLG EGGFGPVYKG KLPGGQEIAV 420 KRLSRTSTQG HEEFQNEVTL TARLQHVNLV RLLGYCTEKE EKLLIYEFMP NKSLELYLFD 480 PVRRYVLDWE KRVRIIEGVT QGLLYLQEYS NITVIHRDLK ASNILLDCDM NPKISDFGMA 540 RLFKKDVNEA NTGRIVGTYG YVPPEYVRKG IYSMKYDVYS FGVLLLQIIS GKRNTCYYGP 600 QENLNLLEYA YELWSDDRGT EFIDTSLDDS SSTCKIMRCM QIALLCVQEN PENRPTMLEV 660 FSMLKNASMA ATTPRRPAFS VKADKNTGST SASQQEICSF NDPQISQLEP R* 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 1.0e-46 | 397 | 665 | 284 | + 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 | 6.0e-47 | 398 | 660 | 274 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 4.0e-47 | 398 | 660 | 274 | + 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-47 | 399 | 664 | 270 | + 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-65 | 25 | 305 | 324 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAD52097.1 | 0 | 24 | 711 | 23 | 739 | AF088885_1 receptor-like kinase CHRK1 [Nicotiana tabacum] |
EMBL | CBI25625.1 | 0 | 180 | 711 | 58 | 580 | unnamed protein product [Vitis vinifera] |
EMBL | CBI35714.1 | 0 | 1 | 711 | 396 | 1130 | unnamed protein product [Vitis vinifera] |
EMBL | CBI35714.1 | 0 | 24 | 407 | 22 | 393 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263709.1 | 0 | 180 | 711 | 244 | 764 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 364 | 670 | 3 | 312 | A Chain A, Crystal Structure Of Class V Chitinase From Nicotiana Tobaccum |
PDB | 3uim_A | 0 | 364 | 670 | 3 | 312 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 364 | 670 | 11 | 320 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 364 | 670 | 11 | 320 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 364 | 670 | 11 | 320 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |