Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma13g34090.2 |
Family | CBM57 |
Protein Properties | Length: 1037 Molecular Weight: 116001 Isoelectric Point: 6.6491 |
Chromosome | Chromosome/Scaffold: 13 Start: 35735406 End: 35748401 |
Description | Leucine-rich repeat transmembrane protein kinase |
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 |
CBM57 | 400 | 586 | 6.8e-31 |
LYINCGGKQVVVGGITYDEDMDSAGPAVYKQSRNNWAFSNTGQFMDNNTLAIQGKLPAYTTENETRLYMTDAELYKNARISPMSLTYYGFCLENGDYTVK LHFAEIMFTADSTYSCLGRRLFDVYIQGRRVLKDFNIANEAQGVGKELIKEFPAHVSTNDLEIRFYWAGKGTTNIPYKSVYGPLISA |
Full Sequence |
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Protein Sequence Length: 1037 Download |
MPISMKTIIS SQFVLLSLLP ICFTWLAFGA NKLPQNEVDA LKEIAKTLGK ENWDFSVNPC 60 YSWNLSKDNM VSCNCDISND SFCHVMKIAL KSQNLRGNLP PQLIELPYLQ EIELSRNYLS 120 GTIPRQWGSS NLQKISLLGN RITGPIPKEL GKLTNLTRLI LEFNQLSGKL PSELGNLVLI 180 KQLHLSSNNF TGPLPATLAR LTTMDEFRIN DNQFSGNIPD FIGSWKSLDQ LHMQGSGLSG 240 PIPSGISLLN LTDLRISDLN GPDSTFPRLE NMTYLKYLIL RSCNINDTFP QYLVRLSRLQ 300 ILDLSYNKLN GPVPKNLQEV ALASYIYLTG NFLTGLVPEW TSANNKNLDL SYNNFSVEDR 360 ESKICYQKTA NLFGSFSRTN LGPVSCENST RTCTKNVQSL YINCGGKQVV VGGITYDEDM 420 DSAGPAVYKQ SRNNWAFSNT GQFMDNNTLA IQGKLPAYTT ENETRLYMTD AELYKNARIS 480 PMSLTYYGFC LENGDYTVKL HFAEIMFTAD STYSCLGRRL FDVYIQGRRV LKDFNIANEA 540 QGVGKELIKE FPAHVSTNDL EIRFYWAGKG TTNIPYKSVY GPLISAISVK YAQYDSTGDM 600 SAGVIVAIVA ALVIVVILIV LGILWWMGFI GDCCWNASVE GLLSTSNFLP HFGRKKHLLM 660 KELRDLDLQT GVFTLHQIKV ATNNFDISNK IGEGGFGPVY KGILSNSKPI AVKQLSPKSE 720 QGTREFINEI GMISALQHPN LVKLYGCCVE GDQLLLVYEY MENNSLAHAL FDSGDRHLKL 780 SWPTRKKICV GIARGLAFMH EESRLKVVHR DLKTSNVLLD EDLNPKISDF GLARLREGDN 840 THISTRIAGT WGYMAPEYAM HGYLTEKADV YSFGVITIEI VSGKRNTIHQ SKEEAFYLLD 900 WARLLKDRGS IMELVDPRLG IDFNEEEVML MVKVALLCTN VTSTLRPSMS TVLNMLEGRT 960 VVPEFVALSS EVLDEMKLGI MREFYSQMEE NNTSEARSLS LTMDVPWTCS SSSAVDLNPA 1020 HLDASCWEKK KLRESV* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 1.0e-50 | 687 | 882 | 204 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
smart00221 | STYKc | 9.0e-51 | 687 | 956 | 281 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00192 | PTKc | 7.0e-51 | 689 | 957 | 290 | + 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. | ||
pfam00069 | Pkinase | 3.0e-51 | 690 | 884 | 199 | + Protein kinase domain. | ||
pfam11721 | Malectin | 3.0e-56 | 399 | 587 | 193 | + 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: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 |
GenBank | AAU10526.1 | 0 | 33 | 1030 | 29 | 998 | putative receptor-like protein kinase 2 [Glycine max] |
EMBL | CBI30746.1 | 0 | 13 | 1004 | 15 | 986 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264249.1 | 0 | 13 | 1004 | 39 | 1007 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002278131.1 | 0 | 14 | 1001 | 7 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002306015.1 | 0 | 38 | 1016 | 1 | 969 | 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 | 669 | 958 | 16 | 308 | A Chain A, Crystal Structure Of Putative Metal-Dependent Hydrolase (Yp_805737.1) From Lactobacillus Casei Atcc 334 At 1.40 A Resolution |
PDB | 3uim_A | 0 | 669 | 958 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 669 | 958 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 669 | 958 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 669 | 958 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |