| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G031536_T01 |
| Family | CBM57 |
| Protein Properties | Length: 622 Molecular Weight: 68872.3 Isoelectric Point: 7.6818 |
| Chromosome | Chromosome/Scaffold: 2 Start: 9918723 End: 9922543 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 30 | 199 | 5e-28 |
| LAVDCGSSRSISGSDKSMYQRDDANLGAASYYVTGAQTWGVSNVGKFTEAVYESYIISSSRQFYNTLDPELFQTARMSASSLRYYGIGLQNGNYTVALQF ADFDFEDSQTWQSVGRRIFDIYLQGERKEKNFDIMKAAGGKSYTAVEKQYIVPVTRNFLEIHLFWAGKGT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 622 Download |
| MFYICSGPWG LPCLQRDTPC FLGSPQSASL AVDCGSSRSI SGSDKSMYQR DDANLGAASY 60 YVTGAQTWGV SNVGKFTEAV YESYIISSSR QFYNTLDPEL FQTARMSASS LRYYGIGLQN 120 GNYTVALQFA DFDFEDSQTW QSVGRRIFDI YLQGERKEKN FDIMKAAGGK SYTAVEKQYI 180 VPVTRNFLEI HLFWAGKGTC CIPFRGYYGP AISAFSVTPN FNPTVQTSRK TGIIVGVVVG 240 AAVLGVLALA GLCMRRQKRR KLLLEQQELY SIVGRPNVFT YGELRTSTEN FSSNNLLGEG 300 GYGSVYKGKL AEGRVVAVKQ LSETSHQGKQ QFAAEIGTIS RVQHRNLVKL YGCCLEGNKP 360 LLVYEYLENG SLDKALFGSG RLNLDWPTRF EICLGIARGI AYLHEESSIR IVHRDIKASN 420 ILLDANFNPK ISDFGLAKLY DDKKTHVSTK VAGTFGYLAP EYAMRGHMTE KVDVFAFGMV 480 ILETLAGRPN FDNMLDEIKV YILEWVWQLY EDKHPLDMVD PKLEEFNSGE VIRAIHVALL 540 CTQGSPHQRP SMSRAVSMLA GDVEVGEVVN KPSYITEWQI KGGNTSSFMS NNVSGQSSMA 600 PRSSASHTSS PFLNSVIEEG W* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00069 | Pkinase | 3.0e-52 | 297 | 501 | 211 | + Protein kinase domain. | ||
| pfam11721 | Malectin | 1.0e-53 | 29 | 215 | 189 | + 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. | ||
| smart00219 | TyrKc | 3.0e-54 | 294 | 559 | 274 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00180 | PKc | 2.0e-54 | 297 | 515 | 223 | + 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. | ||
| smart00221 | STYKc | 2.0e-54 | 294 | 559 | 274 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| 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 | CAD41882.2 | 0 | 8 | 620 | 405 | 1024 | OSJNBa0093O08.1 [Oryza sativa (japonica cultivar-group)] |
| GenBank | EEC78008.1 | 0 | 8 | 608 | 316 | 923 | hypothetical protein OsI_17411 [Oryza sativa Indica Group] |
| GenBank | EEC78008.1 | 0 | 8 | 620 | 1309 | 1929 | hypothetical protein OsI_17411 [Oryza sativa Indica Group] |
| GenBank | EEE61686.1 | 0 | 8 | 620 | 381 | 1000 | hypothetical protein OsJ_16159 [Oryza sativa Japonica Group] |
| RefSeq | XP_002448532.1 | 0 | 8 | 620 | 265 | 885 | hypothetical protein SORBIDRAFT_06g028570 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 273 | 562 | 14 | 309 | A Chain A, Structure Of Ugt78g1 Complexed With Myricetin And Udp |
| PDB | 3uim_A | 0 | 273 | 562 | 14 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 273 | 562 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 273 | 562 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 273 | 562 | 22 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
