Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000307776 |
Family | CBM57 |
Protein Properties | Length: 834 Molecular Weight: 91632.5 Isoelectric Point: 6.0224 |
Chromosome | Chromosome/Scaffold: 018018176 Start: 5489 End: 11567 |
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 | |||
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Family | Start | End | Evalue |
CBM57 | 300 | 445 | 2.2e-31 |
SINCGGQQMKGDGILYETDESVLGSATFSVTSAENWAVSNADVTPELFQTSRVSXGSLRYYGLGLENGPYTVTLHFAETVYESRTSQTWXSLGRRVFDIY IQGTRRXKDFDISKEAGGVNRAVVRKFNVSMSENYLEIHXFWAGKG |
Full Sequence |
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Protein Sequence Length: 834 Download |
MTELTESAVR ALNSIFEQWD TQAAPGLWNI SGEPCSGSAI NGTEFNFPDN SAAVVCNCTY 60 DNNATCHITK LYIDHNYFTG PLPAFIGNMS ALTELTISRN SFSGSIPKEL GNLLELTMLS 120 IASNNFSGTL PPELGNLVKL ERLYMDSCGL GGEIPSTFAK LTNMQVLQFQ GNSFEGPIPT 180 SFSQLTSLNS LRISDIYNGS SSLDFIKNLK NLTELKLRNA LITGTIPSNI GEYQSLETLF 240 LGNNSLSGPL LNQKSDQLQT MNLVVNNFTF DXSNITLRGL NCLQRNFPCN RNTPRYASFS 300 INCGGQQMKG DGILYETDES VLGSATFSVT SAENWAVSNA DVTPELFQTS RVSXGSLRYY 360 GLGLENGPYT VTLHFAETVY ESRTSQTWXS LGRRVFDIYI QGTRRXKDFD ISKEAGGVNR 420 AVVRKFNVSM SENYLEIHXF WAGKGTCCIP DYGHYGPLIA AVHASSDFTK KSKAGLIVGI 480 XVLVGVVSLL LIFAILFMRR KKXEKEDDED ILGLGPXPYT FSYXELRXAT EDFNLSNKLG 540 EGGYGPVYKG TLSDGRVVXV KQLSVASHQG XSQFVSEIAT ISAVQHRNLV KLYGCCIEGS 600 HXILVYEYLE NKSLDQALFG TSNLHLDWPT RFNILLGTAR GLAYIHEESR PRIVHRDVKA 660 SNILLDAKLS PKISDFGLAK LYDDEKTHIS TRVAGTIGYL APEYALFGHL TEKANVFGFG 720 VVVLEILSGR PNSYNNLDPE KIYLLEWGSP MARPSMSRVV AMLSGDIDIG TVMSKPSYLT 780 DYNFIDDDTP STASKHSNVR LNYQPEGNNA SGANTPGVKP VPSTPLGLSL RLLQ 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 3.0e-44 | 537 | 755 | 237 | + 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. | ||
pfam00069 | Pkinase | 1.0e-44 | 533 | 746 | 219 | + Protein kinase domain. | ||
smart00221 | STYKc | 7.0e-45 | 535 | 755 | 230 | + 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 | 4.0e-45 | 535 | 755 | 228 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 5.0e-53 | 298 | 462 | 169 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI39026.1 | 0 | 4 | 795 | 43 | 1007 | unnamed protein product [Vitis vinifera] |
EMBL | CBI39030.1 | 0 | 4 | 811 | 43 | 1026 | unnamed protein product [Vitis vinifera] |
EMBL | CBI39030.1 | 0 | 10 | 786 | 1320 | 2255 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002272404.1 | 0 | 8 | 795 | 2 | 964 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002273016.1 | 0 | 4 | 811 | 43 | 1026 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3ulz_A | 0 | 521 | 766 | 20 | 309 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3uim_A | 0 | 521 | 766 | 20 | 309 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 521 | 766 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 521 | 766 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 521 | 766 | 28 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |