| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.007G329800.1 |
| Family | CBM57 |
| Protein Properties | Length: 582 Molecular Weight: 64588.3 Isoelectric Point: 5.7859 |
| Chromosome | Chromosome/Scaffold: 07 Start: 55199441 End: 55203920 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 7 | 189 | 8.8e-31 |
| VHINCGGRITTVNDTTYEADYDQAGPSTFYRSTNWAFSSTGIFLSDDRPDDILVLNNGQVSVDGDEEELYTNARLAPSSLTYYAFCLANATYTVNLHFAE IQFTDDQTYSSLGRRIFDVYIQGKQELKDFNIEEEAGGAGIPIVKKFTVNVSDGTLEIHFRWAGKGTTSMPERSIYGPLISAI | |||
| Full Sequence |
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| Protein Sequence Length: 582 Download |
| MSSLHFVHIN CGGRITTVND TTYEADYDQA GPSTFYRSTN WAFSSTGIFL SDDRPDDILV 60 LNNGQVSVDG DEEELYTNAR LAPSSLTYYA FCLANATYTV NLHFAEIQFT DDQTYSSLGR 120 RIFDVYIQGK QELKDFNIEE EAGGAGIPIV KKFTVNVSDG TLEIHFRWAG KGTTSMPERS 180 IYGPLISAIS VLDPGYKPPS KSGGRISTAT MAGIVAGATS ATLLIVGIFW WNCCYKLDDE 240 VSGVLFGDEF QNGMELRKFS LVQIAKMTNN FNGEKLGKGG FGVVYKGYLR DSDTYVAVKR 300 ISKASKQGIK EYASEVKIIS QLRHKNLVKL IGQCHEKGEL ILVYELMANS SLDSYLFKGK 360 TLLTWEVRFK IVQDLASALF YLHEEGDHCV LHRDIKASNI MLDSSFNAKL GDFGLARLVD 420 HEKASQTTHL AGTLGYLAPE CVSSGKASKE SDVYSFGVVA LEIACGRRSI ESKYEESQVP 480 LVAWVWDSYG SQRLLDVADP KLSMNFDAKQ MECLLMIGLW CVHPDQHFRP SIRQTIQVLN 540 FEAPWPKLPS TRPTATYNAQ ITSEIQTSEP CFSDMSIMVP R* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00219 | TyrKc | 3.0e-41 | 296 | 463 | 169 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| pfam00069 | Pkinase | 6.0e-44 | 290 | 534 | 258 | + Protein kinase domain. | ||
| cd00180 | PKc | 2.0e-47 | 290 | 463 | 177 | + 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. | ||
| smart00220 | S_TKc | 9.0e-50 | 290 | 467 | 179 | + Serine/Threonine protein kinases, catalytic domain. Phosphotransferases. Serine or threonine-specific kinase subfamily. | ||
| pfam11721 | Malectin | 8.0e-60 | 7 | 189 | 187 | + 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: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 | CBI20136.1 | 0 | 7 | 573 | 104 | 680 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002334872.1 | 0 | 233 | 559 | 296 | 627 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002518333.1 | 0 | 238 | 559 | 331 | 653 | kinase, putative [Ricinus communis] |
| RefSeq | XP_002522044.1 | 0 | 238 | 559 | 244 | 569 | kinase, putative [Ricinus communis] |
| RefSeq | XP_002532988.1 | 0 | 7 | 539 | 323 | 856 | conserved hypothetical protein [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 | 255 | 540 | 16 | 307 | A Chain A, Crystal Structure Of Human Glycogenin-1 (Gyg1), Apo Form |
| PDB | 3uim_A | 0 | 255 | 540 | 16 | 307 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 255 | 540 | 24 | 315 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 255 | 540 | 24 | 315 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 255 | 540 | 24 | 315 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| JG857373 | 239 | 344 | 582 | 0 |
| ES818477 | 290 | 13 | 302 | 0 |
| EH769638 | 267 | 291 | 557 | 0 |
| GE543168 | 254 | 290 | 543 | 0 |
| EH777889 | 245 | 294 | 538 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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