| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10005418 |
| Family | CBM57 |
| Protein Properties | Length: 794 Molecular Weight: 87789.8 Isoelectric Point: 5.343 |
| Chromosome | Chromosome/Scaffold: 847 Start: 41787 End: 47055 |
| Description | receptor-like kinase in flowers 1 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 187 | 355 | 4.1e-28 |
| NIGGKDLTVKENKTTILYEGDSQMLGGTARYFLNEQSYWGISSTGDFMDDNDYQNTRYTVATQSSSIPELYQTARIAPISLTYFHHCLENGKYTVKLHFA EIVFTNDRTYTSLGKRVFDVYVQGKLVLKDLNVEDQAGSAQRPLVLPIPNVNVTSNSLEIRFYYAGKGT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 794 Download |
| MGSKYWQFNA DTCEVEAVGM AKVPPGNAEH TIECTCNNGS NTDCHVVRMA LKNHNLPGNL 60 PPQLVKLPYL QQVSLEANQF SGTVPPELGE LVNLETLMLT SNQLTGSLPI SFAELINLTD 120 FILRNCSLSG ELPDYVWLMK NMEMLFLTDN LLSGDVPDSI LKQGSNIDLS YNNFELQGPG 180 HPACEDNIGG KDLTVKENKT TILYEGDSQM LGGTARYFLN EQSYWGISST GDFMDDNDYQ 240 NTRYTVATQS SSIPELYQTA RIAPISLTYF HHCLENGKYT VKLHFAEIVF TNDRTYTSLG 300 KRVFDVYVQG KLVLKDLNVE DQAGSAQRPL VLPIPNVNVT SNSLEIRFYY AGKGTTRIPD 360 RGVYGPIISA ISIVSDDKAC SELDGGGGKK GKTYAIVGVL GAFSLVIMIL GALWWKGYLP 420 GNCTRRKGFD EDDLPKGTFT LKQIRAATND FDHANKIGEG GFGPVYKGVL PDGTLIAVKQ 480 LSSKSRQGNR EFLNEIGMIS CLRHPNLVKL HGFCVEGDQL LVVYEYMVNN SLARVLFGRE 540 NCELKLDWPT RFKICVGIAK GLAFLHEESV IKIVHRDIKA TNVLLDEDLN PKISDFGLAR 600 LDEEEKTHVS TRVAGTIGYM APEYALWGHL SYKADVYSFG VLMLEIVSGK NNNNFMPSNN 660 CVCLLDWACH LQQNGNLLPI IDETLRSEVK KEEAEIMIKV GLLCTNASSS LRPAMSEVVS 720 MLEGRIPVPD TIPEPSSYAE DLRFKALRDL RRHGEGHSQT QSHGFSQNTT ADTCNSSLDT 780 TTQEFFEIKS APH* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam07714 | Pkinase_Tyr | 3.0e-52 | 456 | 722 | 283 | + Protein tyrosine kinase. | ||
| smart00221 | STYKc | 3.0e-52 | 456 | 722 | 280 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| smart00219 | TyrKc | 9.0e-53 | 456 | 722 | 280 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| cd00192 | PTKc | 6.0e-53 | 455 | 723 | 291 | + 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 | 3.0e-55 | 187 | 371 | 186 | + 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 |
| RefSeq | XP_002264679.1 | 0 | 1 | 791 | 16 | 1004 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264717.1 | 0 | 1 | 793 | 1 | 886 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264878.1 | 0 | 1 | 753 | 125 | 1027 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002305711.1 | 0 | 1 | 761 | 11 | 915 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002522277.1 | 0 | 1 | 788 | 1 | 913 | ATP binding protein, 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 | 439 | 724 | 20 | 308 | A Chain A, Insight Into The Mechanism Of Enzymatic Glycosyltransfer With Retention Through The Synthesis And Analysis Of Bisubstrate Glycomimetics Of Trehalose-6-Phosphate Synthase |
| PDB | 3uim_A | 0 | 439 | 724 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 439 | 724 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 439 | 724 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 439 | 724 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
