| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01021662001 |
| Family | CBM57 |
| Protein Properties | Length: 845 Molecular Weight: 93853.9 Isoelectric Point: 6.3573 |
| Chromosome | Chromosome/Scaffold: 10 Start: 8903917 End: 8907377 |
| Description | hercules receptor kinase 2 |
| 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 | 222 | 375 | 4.7e-21 |
| YRLNVGGPEITPDQDLDLWRTWDVDSSYMFTANAGSEVHNSSNITYASMNDSVVAPLAVYETARSMSNTEVLEKRFNMSWKFEVDPDFEYLIRLHFCELF YERANQRSFRIYINNRTAADNFDVFLRAGGMNKAYHQDFLDMVSSKINTLWIQL | |||
| Full Sequence |
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| Protein Sequence Length: 845 Download |
| MEVWGLILVV MVSVFVGNGE AQAKSLLINC GTNSSVNVDG RRWVGDLAPD NNLTLSSLGV 60 AASTDTFSGD TTFAQLYETA RIFPDSLNYT ASLNQGNYSV RLHFYPFSFE KYNTNESSFS 120 VTANGLKLAS QLNVPGEISH KNSYLQSSGS NSSSFSMIKE YFLTVDSGLL VIEFAPTKGS 180 FGFINAIEIV PVVDNLFFSS VSKVGGTNSV LNLSGRGIEA MYRLNVGGPE ITPDQDLDLW 240 RTWDVDSSYM FTANAGSEVH NSSNITYASM NDSVVAPLAV YETARSMSNT EVLEKRFNMS 300 WKFEVDPDFE YLIRLHFCEL FYERANQRSF RIYINNRTAA DNFDVFLRAG GMNKAYHQDF 360 LDMVSSKINT LWIQLGPDTT VGASGTDAIL NGLEIFKLSR NGNLAYVERF DSTKSSAGSK 420 TSKTQTLWVG LGAGVASIAM MAVIFSLIFY FCKRWRKKSS ATKNKSPGWR PLFLHVNSTN 480 AKGMSQSLSV SLASNRAGKR FTLTEIRAAT NNFDESLVIG VGGFGKVYKG EIDDGTPAAI 540 KRANPQSEQG LAEFQTEIEM LSKLRHRHLV SMIGFCEEQN EMILVYEYMA NGTLRSHLFG 600 SELPPLTWKQ RLEACIGAAR GLHYLHTGAE RGIIHRDVKT TNILIDENFV AKMADFGLSK 660 TGPAWEHTHV STAVKGSFGY LDPEYFRRQQ LTEKSDVYSF GVVLFEVVCA RAVINPSLPR 720 DQINLAEWAM HWQHQRSLET IIDPHLKGNY SPDSLRKFGE IAEKCLADEG KNRPTMGEVL 780 WHLEYVLQLH EAWLRTNVGE NSFSSSQALG NLEEGLESAH LDEENEISLK MKQKRESATR 840 GINA* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00219 | TyrKc | 8.0e-51 | 518 | 783 | 278 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 3.0e-51 | 518 | 783 | 278 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| cd00180 | PKc | 3.0e-51 | 519 | 714 | 200 | + 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. | ||
| cd00192 | PTKc | 1.0e-52 | 518 | 784 | 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. | ||
| pfam12819 | Malectin_like | 2.0e-66 | 28 | 398 | 385 | + Carbohydrate-binding protein of the ER. Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognises and binds Glc2-N-glycan. The domain is found on a number of plant receptor kinases. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004672 | protein kinase activity |
| 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 | CAN73534.1 | 0 | 1 | 844 | 1 | 802 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI31024.1 | 0 | 1 | 844 | 1 | 844 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002264211.1 | 0 | 1 | 844 | 46 | 889 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002330599.1 | 0 | 3 | 813 | 9 | 821 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523186.1 | 0 | 2 | 817 | 8 | 822 | 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 | 2qkw_B | 0 | 500 | 792 | 28 | 319 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |
| PDB | 3hgk_D | 0 | 500 | 792 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_C | 0 | 500 | 792 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_B | 0 | 500 | 792 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_A | 0 | 500 | 792 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| Transmembrane Domains | ||||
|---|---|---|---|---|
| Start | End | |||
| 427 | 449 | |||
| Signal Peptide | ||||
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| Cleavage Site | ||||
| 21 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| ES805185 | 379 | 448 | 813 | 0 |
| EX357602 | 257 | 523 | 779 | 0 |
| HO798798 | 504 | 267 | 745 | 0 |
| DY971329 | 290 | 500 | 789 | 0 |
| ES793081 | 245 | 569 | 813 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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