| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01014150001 |
| Family | CBM57 |
| Protein Properties | Length: 1182 Molecular Weight: 131009 Isoelectric Point: 5.1203 |
| Chromosome | Chromosome/Scaffold: 19 Start: 846312 End: 864401 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 574 | 737 | 2.2e-29 |
| INCGGSEINYEGNDYERDLDGSGASHFSDYSEKWGYSSTGVFTNNDDAAYVATNTFSLNITGPEYLQTARTSPISLKYYGLCMRKGSYRVQLHFAEIMFS DDETFSSLGKRIFDVSIQGVTVLKDFNIVEEAKGVGKAITKDFETSVNGSTLEIHLYWAGKGTN | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1182 Download |
| MGLGIYIDIY DSLHEGPFLW FSFSFHGVAI CFSVLYAIPI AFMNYNPVFM QTEITQIQMD 60 ENLVVDPLQP NAQNILFLHL LSYLDEQLVF IYLPFLADFD SNPGLSVRGV IGIVMASCLK 120 RTPTSAQNSW NKYIQDSTFS LIIFAIGKSF GFLHILSGQS FPFIFKFHYH FQGMRFKAFE 180 KLSLDSQLQY SLRPAQLLPE DEVQTLETIA TRLNNRYWNI SQTSCGGGFN VNFTSDYFSN 240 VTCDCTFENS TVCHVTNIQL KGLNLTGIMP DEFGNLTYLQ EIDLTRNYLN GSIPTSLAQI 300 PLVTLSALGN RLSGSIPKEI GDIATLEELV LEDNQLEGSL PENLGNLSSL SRLLLTANNF 360 TGTIPETFGN LKNLTDVRLD GNAFSGKIPD FIGNWTQLDR LDMQGTSMDG PIPSTISLLT 420 NLTQLRIADL NGSSMAFPNL QNLTKMEELV LRNCSITDSI PDYIGKMASL KTLDLSFNRL 480 SGQVSDTWSL SQLEYLFLTN NSLSGTLPSW ISDSNQKFDV SYNNFTGPSS LTVCQQRAVN 540 LVSSFSSSDS NSVLWCLKKG LPCPGNAKHY SLFINCGGSE INYEGNDYER DLDGSGASHF 600 SDYSEKWGYS STGVFTNNDD AAYVATNTFS LNITGPEYLQ TARTSPISLK YYGLCMRKGS 660 YRVQLHFAEI MFSDDETFSS LGKRIFDVSI QGVTVLKDFN IVEEAKGVGK AITKDFETSV 720 NGSTLEIHLY WAGKGTNAIP SRGVYGPLIS AITVTPNFDV STGLSAGAIA GIVIASIAAV 780 VLILIVLRLT GYLGGKDQED KELQALKLQT GYFSLRQIKA ATNNFDPANK IGEGGFGPVY 840 KGVLPDGSVI AVKQLSSKSK QGNREFVNEI GMISALQHPN LVKLYGWCIE GNQLLLIYEY 900 LENNCLARAL FGRIEQRLNL DWPTRNKICL GIARGLAYLH EESRLKIVHR DIKATNVLLD 960 KDLNAKISDF GLAKLDEEEN THISTRIAGT IGYMAPEYAM RGYLTDKADV YSFGIVALEI 1020 VSGKSNTNYR PKEEFVYLLD WAYVLQEQEN LLELVDPSLG SKYSKEEAQR MLNLALLCAN 1080 PSPTLRPSMS SVVSMLEGKT AVQVPLIKRS SMNSMNLDMR FKAFEKLSQD SQTYVSERSQ 1140 GSQMQRSMSM DGPWFGSSVS FPDKDKTREH SSSSKQKLLH D* 1200 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00069 | Pkinase | 1.0e-47 | 830 | 1024 | 199 | + Protein kinase domain. | ||
| smart00219 | TyrKc | 2.0e-49 | 830 | 1096 | 282 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 1.0e-49 | 830 | 1096 | 282 | + 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 | 2.0e-50 | 829 | 1097 | 281 | + 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. | ||
| pfam11721 | Malectin | 3.0e-56 | 570 | 752 | 186 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN81779.1 | 0 | 195 | 1181 | 26 | 970 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI20142.1 | 0 | 195 | 1175 | 24 | 1007 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI20154.1 | 0 | 1 | 1181 | 1 | 1181 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002283453.1 | 0 | 195 | 1181 | 26 | 1009 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002283521.1 | 0 | 195 | 1175 | 24 | 1009 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 798 | 1098 | 7 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3uim_A | 0 | 798 | 1098 | 7 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 798 | 1098 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 798 | 1098 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 798 | 1098 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
