Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.011G052600.2 |
Family | CBM57 |
Protein Properties | Length: 1053 Molecular Weight: 115658 Isoelectric Point: 8.0337 |
Chromosome | Chromosome/Scaffold: 11 Start: 4114814 End: 4122075 |
Description | Leucine-rich repeat transmembrane protein kinase |
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 |
CBM57 | 431 | 596 | 9.8e-28 |
SIKCGGPAMIADGISFDVDNSTLGPATFNISSIRKWAVSNAGLFAERPIQQYVQNFAGTVSGTNTPKLYETSRLSPGSLRYYGLGLENGSYTVRLFFAET GFPELASQSWKSLGRRVFDVYIQGTRQLRDFDISKEAGGVNKAIIRNFTTNVTGNHLVIHLFWAGK |
Full Sequence |
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Protein Sequence Length: 1053 Download |
MKPRVKSSWK GLLYYFFFLV VVVLFSCSQS ITAQTNATTD PSEVKALNSI FQQWNAQAVA 60 SWNTTGDPCS GTALSQGLSE FEDPSNNPAI TCDCSFNDNT VCHITRLRVF GLDKRGVLPK 120 ELLDLPYLDF LKLDRNFFSG PLPAFIGNMS RLGLLSLAHN NFSGTIPKEF GNLKKLYLLS 180 LGNNDIFGKL PPELGNLAEL GELYINSCAL SGEIPSTFAK LKDLRTVWAS DNAFTGKIPD 240 FFGNLTKLTA LRFQGNSFEG PIPSSLGNLT SLTSLRIGDI YNGSSSSLDF IRNLKNLTDL 300 VLRNVLLTGN LPSYITELQY LQKLDLSFNN LTGRIPSVLF TMKSLEYLFL GNNGLSGSIP 360 SQKSETLTTI DLSYNFLSGN LPSWVNSRLQ LNLVANNFTF NSSINRLLPG LECLQRSFPC 420 FRNAPRYANF SIKCGGPAMI ADGISFDVDN STLGPATFNI SSIRKWAVSN AGLFAERPIQ 480 QYVQNFAGTV SGTNTPKLYE TSRLSPGSLR YYGLGLENGS YTVRLFFAET GFPELASQSW 540 KSLGRRVFDV YIQGTRQLRD FDISKEAGGV NKAIIRNFTT NVTGNHLVIH LFWAGKGTTG 600 IPTTGTYGPA ISAISVVPNF KPSVSGLPPD NPKKKKHTAL IAGVTIPVVA LALILIFSIL 660 YMKREKEEDD DDEGKMLLGI SPRPNTFSYS ELKAATEDFN PSNKLGEGGF GPVYKGTLSD 720 GKVVAVKQLS VASNQGKDQF VTEIATISAV QHRNLVKLYG CCIGGNRRLL VYEYLVNKSL 780 DHALWGQKDL HLDWPTRFNI CLLTAKGLAY LHEESRPKIV HRDVKASNIL LDAELCPKIS 840 DFGLAKLYDD KKTHITSRAA GTVGYLAPEY AMRGHLSEKV DVFSFGVVAL EIITGRPNSD 900 NRLEDGRVYL LNWAWTLHEN NQLLSLLDPT LVEFDENEAL RVIGVAFLCT QASPSLRPSM 960 SRVIAMLVGD TEVGNVTTKP SYLTDCDFKD VTGDYEYKTD TFMDKESQKS NASDHSSNGI 1020 KSKNNTLSGL NDQPILSPVN VSGFRESIGE GR* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam07714 | Pkinase_Tyr | 2.0e-44 | 704 | 967 | 284 | + Protein tyrosine kinase. |
cd00180 | PKc | 3.0e-47 | 705 | 892 | 192 | + 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 | 5.0e-48 | 703 | 967 | 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. |
smart00221 | STYKc | 2.0e-48 | 704 | 907 | 219 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. |
smart00219 | TyrKc | 2.0e-48 | 704 | 906 | 218 | + 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 |
EMBL | CBI39026.1 | 0 | 29 | 1052 | 34 | 1037 | unnamed protein product [Vitis vinifera] |
EMBL | CBI39030.1 | 0 | 29 | 1035 | 34 | 1033 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002272404.1 | 0 | 44 | 1052 | 3 | 994 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002273016.1 | 0 | 29 | 1052 | 34 | 1048 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002303698.1 | 0 | 32 | 1052 | 7 | 1016 | predicted protein [Populus trichocarpa] |
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 | 687 | 970 | 20 | 309 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 687 | 970 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 687 | 970 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 687 | 970 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 687 | 970 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |