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Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os04g22470.1 |
Family | CBM57 |
Protein Properties | Length: 862 Molecular Weight: 95008 Isoelectric Point: 6.8509 |
Chromosome | Chromosome/Scaffold: 4 Start: 12718050 End: 12726551 |
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 | 335 | 501 | 6.5e-25 |
GSDNTIYEADPANLGAATYYVTGQTRWGVSSVGHYFRATDAKNIIYSSQNFNNVVDSKLFETGRVSPSSLRYYGLGLENGNYTVLLRFAEIAFPDSQTWL SLGRRVFDIYIQGALKEKDFDIRKTAGGKSFSVVNRSFMVTVSKNFLEIHLFWAGKGGGIYGPMISA |
Full Sequence |
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Protein Sequence Length: 862 Download |
MRSSRGVIRH SVWCLVFVWS WRVAAAQDQQ APKTDPVEAV ALNTIMRRWG KEASSEWNVS 60 GDLCSGFAAD KNDWDYYPNI NPFIKCDCTF SNNTLCRITK LDLNYNYLTG FIPSFIGKFT 120 SMKYLALGFN PLSGPLPKEL GNLTNLISLG ISLNNFTGGL PEELGNLTKL KQFLASDNGF 180 TGKIPDYLGS MTNLEEMRIG DIVNGISPLA LISNLTSLNT LILRNCKIYG DLGAVDFSMF 240 EKLSLLDLSF NNITGKVSQS ILNLGNLQFL FLGNNNLAGR LPDGISSSLK AIDFSYNQLT 300 GSIPSWASQN NLQLNLVANN FLLGSTSNSN TSTRGSDNTI YEADPANLGA ATYYVTGQTR 360 WGVSSVGHYF RATDAKNIIY SSQNFNNVVD SKLFETGRVS PSSLRYYGLG LENGNYTVLL 420 RFAEIAFPDS QTWLSLGRRV FDIYIQGALK EKDFDIRKTA GGKSFSVVNR SFMVTVSKNF 480 LEIHLFWAGK GGGIYGPMIS ALSVTPNFTP TVRNGIPKSE SKVGIIAGIS IGAIVLVLAA 540 LFGVFTLLKK RRALAYQKEE LYYLVGQPDV FNYAELKLAT DNFSSQNILG EGGFGPVYKQ 600 YFVHAQNIHV TNLAGKTPLL VYEYLENGSL DQAIFGDSSL NLDWVTRFEI ILGIASGLTY 660 LHEESSVRIV HRDIKASNVL LDTDLTPKIS DFGLAKLYDE KQTHVSTRIA GTLGYLAPEY 720 AMRGHLSEKA DVFAFGVVML ETVAGRPNTN NSLEENKIYL LEWAWGMYDK DQALEIVDPT 780 IKDFDKDEAF RVINVALLCT QGSPHQRPPM SRVVAMLTRD VDVPKVVTKP SYITEWQLRG 840 GGNNGNTSNS YAGSSYQPEV Q* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 1.0e-28 | 618 | 817 | 202 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00220 | S_TKc | 8.0e-29 | 620 | 747 | 128 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
pfam00069 | Pkinase | 6.0e-30 | 615 | 762 | 149 | + Protein kinase domain. | ||
cd00180 | PKc | 2.0e-30 | 620 | 741 | 124 | + 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-43 | 340 | 502 | 171 | + 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:0006464 | cellular protein modification process |
GO:0006468 | protein phosphorylation |
GO:0008152 | metabolic process |
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 | CAE04470.3 | 0 | 1 | 861 | 1 | 861 | OSJNBa0029L02.11 [Oryza sativa (japonica cultivar-group)] |
GenBank | EEC76964.1 | 0 | 1 | 861 | 1 | 883 | hypothetical protein OsI_15252 [Oryza sativa Indica Group] |
GenBank | EEE60691.1 | 0 | 1 | 861 | 1 | 815 | hypothetical protein OsJ_14169 [Oryza sativa Japonica Group] |
GenBank | EEE63030.1 | 0 | 98 | 860 | 604 | 1434 | hypothetical protein OsJ_17838 [Oryza sativa Japonica Group] |
RefSeq | NP_001052392.1 | 0 | 40 | 846 | 29 | 972 | Os04g0291900 [Oryza sativa (japonica cultivar-group)] |
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 | 565 | 820 | 14 | 309 | A Chain A, X-Ray Crystal Structure Of Tdp-Vancosaminyltransferase Gtfd As A Complex With Tdp And The Natural Substrate, Desvancosaminyl Vancomycin. |
PDB | 3uim_A | 0 | 565 | 820 | 14 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 565 | 820 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 565 | 820 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 565 | 820 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |