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Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os08g10320.3 |
Family | CBM57 |
Protein Properties | Length: 963 Molecular Weight: 105679 Isoelectric Point: 6.7806 |
Chromosome | Chromosome/Scaffold: 8 Start: 6032447 End: 6039155 |
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 | 369 | 539 | 5.3e-24 |
FAVDCGSNRSIRGSDNTMYELDFTDLGSSSYYVTSETRWGVSNVGKYFQSPNDSKIIYSNEKIQNAVVSELLQTARMSPSSLRYFGLGLENGNYTVLLQF AELGYPDSPTWKSLGRRVFDIYIQGDLKEKDFDIRKMAGGKSFTAVYKSYTATVSKNFLEIHLFWAGKGTC |
Full Sequence |
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Protein Sequence Length: 963 Download |
MSGEPCRGVP VDGVTGLDGN PKNNPGIKCD CSYINGTVCH ITQLKVYALN VVGQIPAELQ 60 NLTYLNYLDL DQNYLSGPIP SFIGQLTALT ELHVGFNALS GPIPKELGNL TNLNLLGISL 120 TNFTGQLPEE LGNLTKLQRL YTDSAGLSGP FPSTFSKLKN LKLLRASDND FTGKIPDYIG 180 SLTNLEDLAF QGNSFEGPIP ESLSNLTKLT TLRIGDIVSG SSSFAFVSSL TSLNILVLRN 240 CRISGDLGAV DFSKFTKLAF LDLSFNNISG KVPQSILNLQ MLTDLFLGNN SLTGGLPDGI 300 SPSLKNLDFS YNQLTGSFPS WATQNNLQLN LVANNFDLGS TNNGILPPGL NCLQKDTPCL 360 RGSPEYYSFA VDCGSNRSIR GSDNTMYELD FTDLGSSSYY VTSETRWGVS NVGKYFQSPN 420 DSKIIYSNEK IQNAVVSELL QTARMSPSSL RYFGLGLENG NYTVLLQFAE LGYPDSPTWK 480 SLGRRVFDIY IQGDLKEKDF DIRKMAGGKS FTAVYKSYTA TVSKNFLEIH LFWAGKGTCC 540 IPIQGYYGPL ISALSITPNF TPTVRNGVPK RKSKVGAIAG ISIGASVVGL AALFGIFMFI 600 KKRRRLAQQQ GELYNLVGRP DVFSNAELKL ATNNYSSQNI LGEGGYGPVY KGMLPDGRVI 660 AVKQLSQSSH QGKNQFVTEV ATISSVQHRN LVKLHGCCID SNTPLLVYEY LENGSLDQAL 720 FRKNSLKLDW ATRFEIILGI ARGLTYLHEE SSVRIVHRDI KASNVLLDTD LTPKISDFGL 780 ARLYDEKKTH VSTGIAGTFG YLAPEYAMRR HLTEKVDVYA FGVVALETVA GRSNTNNSIE 840 ESKIYLLEWA WDLYEKEQAQ RIVDPRLEDF NKDEVLRVIH VALLCTQGSP NQRPPMSRVM 900 AVLTGDAEVV EMVTKPSYIT EWQYRDGNST NSESTTSEFS RQKEIDPLTM SPTITGSSHD 960 GR* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00069 | Pkinase | 3.0e-47 | 640 | 877 | 250 | + Protein kinase domain. | ||
smart00221 | STYKc | 2.0e-47 | 640 | 824 | 192 | + 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-49 | 640 | 824 | 191 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 2.0e-50 | 641 | 827 | 191 | + 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 | 5.0e-57 | 367 | 554 | 190 | + 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:0000166 | nucleotide binding |
GO:0004672 | protein kinase activity |
GO:0005515 | protein binding |
GO:0005524 | ATP binding |
GO:0005886 | plasma membrane |
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 | AAY67902.1 | 0 | 1 | 962 | 63 | 1027 | SHR5-receptor-like kinase [Saccharum hybrid cultivar SP70-1143] |
GenBank | EEC78858.1 | 0 | 1 | 954 | 63 | 1018 | hypothetical protein OsI_19210 [Oryza sativa Indica Group] |
RefSeq | NP_001061221.1 | 0 | 3 | 962 | 87 | 1037 | Os08g0203100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001061223.1 | 0 | 1 | 960 | 57 | 1020 | Os08g0203400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002444009.1 | 0 | 1 | 962 | 68 | 1009 | hypothetical protein SORBIDRAFT_07g005820 [Sorghum bicolor] |
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 | 607 | 906 | 6 | 309 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 607 | 906 | 6 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 607 | 906 | 14 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 607 | 906 | 14 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 607 | 906 | 14 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |