y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma20g04645.1 |
Family | GH18 |
Protein Properties | Length: 803 Molecular Weight: 89190 Isoelectric Point: 7.8131 |
Chromosome | Chromosome/Scaffold: 20 Start: 4946074 End: 4950402 |
Description | lectin protein kinase family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 28 | 251 | 3.3e-21 |
DIAIYWGSNDGEGSLAETCATGLYSFVNIAFLAHFGNGQVPQVILGRHCDPFGGNCSVLGRDIRNCQKQGIKVMLSIGGPSMSYSLVSSEDAKSVSDYLW NNFLGGGGNSSSSSSPLGDVILDGIDFGLGGSLMTKHWEDLAHYLKSHRRNVYLSAAPQCIFPDSALGKALETGLFDYVWIQFYNNPLCQYNEGNASNLL NAWKQWTTSLKSGKMFLGLPASPT |
Full Sequence |
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Protein Sequence Length: 803 Download |
MNMFLFPSYV LLLLFLILNL PHTTHSDDIA IYWGSNDGEG SLAETCATGL YSFVNIAFLA 60 HFGNGQVPQV ILGRHCDPFG GNCSVLGRDI RNCQKQGIKV MLSIGGPSMS YSLVSSEDAK 120 SVSDYLWNNF LGGGGNSSSS SSPLGDVILD GIDFGLGGSL MTKHWEDLAH YLKSHRRNVY 180 LSAAPQCIFP DSALGKALET GLFDYVWIQF YNNPLCQYNE GNASNLLNAW KQWTTSLKSG 240 KMFLGLPASP TASIGGYVPP DLLISRILST VKTSSNYGGI MLWSRLFDKE SGYSKRILEN 300 SVCLQKRETE CGRHKNGFIE HLGYMAKEGF VASESKSIDM QCCEVICRNN CSCEAYAPLN 360 FVNNTGCQFW GKGTKFIKDS GGNFKRVYFV KHKVAVNKLW KWIVIGVGAA VAALVSCYLF 420 YVLRRKCKEE VDRKMKRKEL LVEVGGNAMG NYGKAKGSKK EGKTINEIEV FSLENIIVAT 480 HNFSPDNKLG EGGFGPVYKG TLIDGQEIAI KRLSKSSGQG LVEFKNEAKI MAKLQHTNLV 540 RLLGFCIDSD ERILVYEYMS NKSLDHYLFD ASRNNELEWN KRLKIIEGTA QGLVYLHRYS 600 RLKVIHRDLK ASNILLDEEM NPRISDFGLA RIFGLKGSEE NTSRVVGTYG YMSPEYAING 660 VVSVKTDVYS FGVLLLEIIS GMKNNSCIHS NHPFNLIAHA WQLWNQGRAL ELMDPSLNES 720 FSSDEVERCI QIGLLCVQDH AIERPTMEDV VTFLSNDTTQ LGQPKQPAFF MYVVAGESGC 780 PNNSKQENYS LNHLSISTAY GR* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00069 | Pkinase | 1.0e-50 | 488 | 751 | 269 | + Protein kinase domain. | ||
smart00221 | STYKc | 9.0e-51 | 486 | 754 | 285 | + 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 | 9.0e-51 | 486 | 754 | 285 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00180 | PKc | 6.0e-51 | 489 | 678 | 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. | ||
cd02877 | GH18_hevamine_XipI_class_III | 2.0e-111 | 28 | 297 | 281 | + This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. |
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 |
EMBL | CBI25711.1 | 0 | 303 | 802 | 107 | 619 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002268267.1 | 0 | 432 | 769 | 14 | 351 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268342.1 | 0 | 296 | 769 | 288 | 764 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002516064.1 | 0 | 303 | 802 | 300 | 795 | Serine/threonine-protein kinase PBS1, putative [Ricinus communis] |
RefSeq | XP_002516068.1 | 0 | 281 | 802 | 271 | 789 | receptor protein kinase, 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 | 1kr1_A | 0 | 29 | 300 | 3 | 272 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1kqz_A | 0 | 29 | 300 | 3 | 272 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1kqy_A | 0 | 29 | 300 | 3 | 272 | A Chain A, Hevamine Mutant D125aE127AY183F IN COMPLEX WITH PENTA-Nag |
PDB | 2hvm_A | 0 | 29 | 300 | 3 | 272 | A Chain A, Hevamine Mutant D125aE127AY183F IN COMPLEX WITH PENTA-Nag |
PDB | 1llo_A | 0 | 29 | 300 | 3 | 272 | A Chain A, Hevamine Mutant D125aE127AY183F IN COMPLEX WITH PENTA-Nag |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
chitin degradation II | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12623 | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12624 | EC-3.2.1.14 | chitinase |
chitin degradation III (carnivorous plants) | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |