| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra032404 |
| Family | CBM57 |
| Protein Properties | Length: 854 Molecular Weight: 94483.2 Isoelectric Point: 6.4794 |
| Chromosome | Chromosome/Scaffold: 09 Start: 21710289 End: 21712850 |
| Description | hercules receptor kinase 2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 231 | 386 | 2.4e-21 |
| YRLNVGGPKLGPSQDLKLYRTWETDSSYMVIENAGEHVDNSSSITYALANESPVAPLLVYETARTMSSDTEVLEKRFNISWKFEVDPNFDYLVRLHFCEL VVDKQNQRIFRIYINNQTAAGNFDIYAHAGGKNKAIYQDYFDPVSSKNDVLWIQLG | |||
| Full Sequence |
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| Protein Sequence Length: 854 Download |
| MLKQRKKFME LVLCLLIIFT FVVGYGEAQS KSFLVDCGSN TSTKADGRIW VGDLSPNNSL 60 SLSSSGLDAT SPTPLKSSAF AEIYKSARVF TTTLNYSFYE IPQGSYFVRL HFSPFPMETH 120 NVNESSFSVY ANGLRLMLDI NIQGEIAHKN LILLSSGHNA TASSLVKEFL LPIGPEKLVL 180 SFIPEKESFG FVNAIEVVSV DDKLFKDSVT KVGGSEVELG LGGGRGVETM YRLNVGGPKL 240 GPSQDLKLYR TWETDSSYMV IENAGEHVDN SSSITYALAN ESPVAPLLVY ETARTMSSDT 300 EVLEKRFNIS WKFEVDPNFD YLVRLHFCEL VVDKQNQRIF RIYINNQTAA GNFDIYAHAG 360 GKNKAIYQDY FDPVSSKNDV LWIQLGPDTS AGASGTDALL SGLEIFKLSK NGNLAHLMRF 420 DSSGHSVDNS RMRIIWISVG AGVATIILLA FLVTMVVCLC KMRRNKSDDD SKNNPPGWRP 480 LFLHVNNSTT NAKAAGGSLR LNTLAASTLG RKFTLAEIRA ATKNFDDGLA IGVGGFGKVY 540 RGELEDGTVI AIKRATPHSQ QGLAEFETEI VMLSRLRHRH LVSLIGFCDE HNEMILVYEY 600 MANGTLRSHL FGSNLPPLSW KQRLEACIGS ARGLHYLHTG SERGIIHRDV KTTNILLDEN 660 FVAKMSDFGL SKAGPSMDHT HVSTAVKGSF GYLDPEYFRR QQLTEKSDVY SFGVVLFEAV 720 CARAVINPTL PKDQINLAEW ALSWQKQRSL ESIIDPNLRG NYSPESLEKY GEIAEKCLAD 780 EGKNRPMMGE VLWHLEYVLQ LHEAWLRKQN GENSFSSSQA LEEAPESSLQ ACSNQDSSEA 840 EKSQTGSTLH NMV* 900 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 5.0e-41 | 531 | 726 | 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 | 3.0e-41 | 531 | 796 | 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. | ||
| smart00219 | TyrKc | 8.0e-42 | 531 | 718 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| smart00221 | STYKc | 4.0e-42 | 531 | 718 | 197 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| pfam12819 | Malectin_like | 5.0e-52 | 35 | 408 | 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 | CBI31024.1 | 0 | 13 | 848 | 6 | 839 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_174345.1 | 0 | 1 | 851 | 1 | 847 | protein kinase family protein [Arabidopsis thaliana] |
| RefSeq | XP_002264211.1 | 0 | 13 | 848 | 51 | 884 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299052.1 | 0 | 4 | 823 | 5 | 813 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523186.1 | 0 | 12 | 847 | 9 | 840 | 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 | 512 | 804 | 28 | 319 | A Chain A, Structural Basis For Activation Of Plant Immunity By Bacterial Effector Protein Avrpto |
| PDB | 3hgk_D | 0 | 512 | 804 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_C | 0 | 512 | 804 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_B | 0 | 512 | 804 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| PDB | 3hgk_A | 0 | 512 | 804 | 28 | 319 | E Chain E, Crystal Structure Of Effect Protein Avrptob Complexed With Kinase Pto |
| Transmembrane Domains | ||||
|---|---|---|---|---|
| Start | End | |||
| 7 | 26 | |||
| 434 | 456 | |||
| Signal Peptide | ||||
|---|---|---|---|---|
| Cleavage Site | ||||
| 24 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| ES805185 | 342 | 456 | 791 | 0 |
| GH270923 | 255 | 590 | 844 | 0 |
| ES793081 | 239 | 585 | 823 | 0 |
| EX053573 | 205 | 588 | 792 | 0 |
| EX357602 | 257 | 535 | 791 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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