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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma15g01820.2 |
Family | GH18 |
Protein Properties | Length: 821 Molecular Weight: 91012.7 Isoelectric Point: 6.7308 |
Chromosome | Chromosome/Scaffold: 15 Start: 1200171 End: 1204142 |
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 | 27 | 255 | 3.6e-25 |
NVAIYWGQNADEGTLNETCATGTYSHVIIAFLSTFGNGQTPQLSLADHCDPSTNGCTKIGREIKNCQEQGITVMLSIGGGSGNYSITSDEDANNVSNYLW DNFFGGFSSSRPFGDAVLDGLDFDIALGDNTSFMANLAQYLKSNSDSQTIQQKQLPASLYLSAAPQCPFPDARLGSAIGTGIFDYVWVQFYNNPSCSYSQ NNLDNFLKSWREWATSLKVGKLFLGLPAD |
Full Sequence |
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Protein Sequence Length: 821 Download |
MSTSVLPSLL FFLVLILLLL DPSEPENVAI YWGQNADEGT LNETCATGTY SHVIIAFLST 60 FGNGQTPQLS LADHCDPSTN GCTKIGREIK NCQEQGITVM LSIGGGSGNY SITSDEDANN 120 VSNYLWDNFF GGFSSSRPFG DAVLDGLDFD IALGDNTSFM ANLAQYLKSN SDSQTIQQKQ 180 LPASLYLSAA PQCPFPDARL GSAIGTGIFD YVWVQFYNNP SCSYSQNNLD NFLKSWREWA 240 TSLKVGKLFL GLPADEAAAP AGGYVPADVL MSKILPEINK STNYGGLMLW SRYYDKISGY 300 STRIQNPLRN GTANPLCTRK SQACRSHEGG FAELLGYMST LGIKVYEDDN NGTQCCEIIC 360 RNNCSCDAFA PLNHINNTST GCQIWLKGTK FVRASGNIAL PINVSVALLE HKVNSWWIWL 420 IVGVGAAFVI PVIFYLSRAF LRKYKAKVER KKMQKKLLHD IGGNAMLAMV YGKTIKSNNK 480 GKTNNEVELF AFDTIVVATN NFSAANKLGE GGFGPVYKGN LSDQQEVAIK RLSKSSGQGL 540 IEFTNEAKLM AKLQHTNLVK LLGFCIQRDE RILVYEYMSN KSLDFYLFDS ARKDLLDWEK 600 RLNIIGGIAQ GLLYLHKYSR LKVIHRDLKA SNILLDHEMN AKISDFGMAR IFGVRVSEEN 660 TNRVVGTYGY MAPEYAMKGV VSIKTDVFSF GVLLLEILSS KKNNSRYHSD HPLNLIGYAW 720 QLWNAGRALE LIDSTLNGLC SQNEVFRCIH IGLLCVQDQA TDRPTMVDIV SFLSNDTIQL 780 PQPMQPAYFI NEVVEESELP YNQQEFHSEN DVTISSTRAR * 840 |
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-52 | 507 | 773 | 284 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 2.0e-55 | 506 | 773 | 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 | 1.0e-55 | 507 | 773 | 276 | + 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 | 3.0e-56 | 507 | 773 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd02877 | GH18_hevamine_XipI_class_III | 4.0e-112 | 27 | 306 | 287 | + 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 | CAN61711.1 | 0 | 315 | 796 | 377 | 845 | hypothetical protein [Vitis vinifera] |
EMBL | CAN74543.1 | 0 | 308 | 816 | 243 | 742 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268342.1 | 0 | 265 | 820 | 256 | 795 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002516064.1 | 0 | 324 | 820 | 308 | 795 | Serine/threonine-protein kinase PBS1, putative [Ricinus communis] |
RefSeq | XP_002516068.1 | 0 | 317 | 820 | 302 | 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 | 2hvm_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1llo_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 1hvq_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
PDB | 1kr1_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1kqz_A | 0 | 28 | 304 | 3 | 269 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-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 |