| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01021282001 |
| Family | CBM57 |
| Protein Properties | Length: 1002 Molecular Weight: 111015 Isoelectric Point: 6.4164 |
| Chromosome | Chromosome/Scaffold: 10 Start: 3402601 End: 3416864 |
| Description | receptor-like kinase in flowers 1 |
| 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 | 83 | 257 | 2.3e-28 |
| HVNCGGDDLTIKESKRKVFYEGDAEVEGGTAKYFRSKNSYWGLSSTGDFMDDNNDQNMRYIETLSSGNISGVYTTARLSPLSLTYFGYCLENGDYTLQLH FAEIYFTNDKTYDSLGKRLFDIYIQEQLVHKDFNIEDEARGARKPVMKQFNTSVTNNVLEIRFYWAGKGTTRIPS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1002 Download |
| MSVSTSYGNL LSGNIPDLFL KKGSSIDLSY NNFSWQGPEQ PACQENMNLN VNLYRSSSME 60 NNLRAVLPCS KNDNCPQYAC SFHVNCGGDD LTIKESKRKV FYEGDAEVEG GTAKYFRSKN 120 SYWGLSSTGD FMDDNNDQNM RYIETLSSGN ISGVYTTARL SPLSLTYFGY CLENGDYTLQ 180 LHFAEIYFTN DKTYDSLGKR LFDIYIQEQL VHKDFNIEDE ARGARKPVMK QFNTSVTNNV 240 LEIRFYWAGK GTTRIPSRGV YGPLISAISV HPNFKSCSSS GKKGMTAYII GGVVGLCIIL 300 LILGFLQWKG CLRGRKREEK DPEGLDLQTS SFTLKQIKNA TNNFDSANKI GEGGFGPVFK 360 GLLSDGTTVA VKQLSSGSRQ GNREFLNEIG MISCLQHPNL VELHGCCVEG DQLLLVYEYM 420 ENNSLARALF GPENSQLILD WPTRLKICIG IAKGLAFLHE ESRLKIVHRD IKATNVLLDR 480 DLNPKISDFG LARLDDGGKS HISTRIAGTI GYMAPEYALR GYLTYKADVY SFGIVVLEIV 540 SGKNNDYMPS NSCFCLLDWA CHLQQSGKLL ELVDEALGSE VREEEAEMMV KMAILCTNAS 600 PSLRPTMSEV VSMLEGRKPT PDIILEPNSH NEDVRFKAIR DFRQEKRNQS LTGIQTQNST 660 APTELYYSSA SGVDFCEINP ASKSYQANSR REMATVVHIP LLILLLHTCF GSTSVEALAG 720 HLPDEEKGVL EEIAEQLGKK DWKFELNPCD GNSNWNTLGS RSNPFYNNTI TCNCSFPNGE 780 CHVDSISLKG QDLAGVLPPA LAKLSYLKKI DLARNYLSGN IPPEWETTKL ETLSISMNRL 840 SGRIPNFLGN ITTLKNLGLE GNLFSGTVPP ELGKLVDLQK LILNSNNLTG PLPQALAHLT 900 NLKELRISSN NFTGKIPSFI QSWKQLQQLE IQASGLEGPI PSNISVLSNL TELRISDLNG 960 EGSTFPPLRS MKRMYKLMLR GCNISGPIPP DIAEMTELRF L* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00219 | TyrKc | 2.0e-50 | 349 | 614 | 281 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 9.0e-51 | 349 | 614 | 281 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| pfam07714 | Pkinase_Tyr | 7.0e-51 | 349 | 614 | 284 | + Protein tyrosine kinase. | ||
| cd00192 | PTKc | 3.0e-53 | 348 | 615 | 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. | ||
| pfam11721 | Malectin | 6.0e-59 | 81 | 268 | 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 | |
|---|---|
| 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 | CBI30742.1 | 0 | 1 | 1001 | 1 | 1001 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264679.1 | 0 | 8 | 684 | 332 | 1007 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264679.1 | 0 | 783 | 1001 | 86 | 304 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002522276.1 | 0 | 8 | 998 | 330 | 1354 | kinase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 319 | 616 | 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 | 319 | 616 | 7 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 319 | 616 | 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 | 319 | 616 | 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 | 319 | 616 | 15 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
