Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.T009100.1 |
Family | CBM57 |
Protein Properties | Length: 921 Molecular Weight: 103338 Isoelectric Point: 6.7388 |
Chromosome | Chromosome/Scaffold: 24 Start: 390332 End: 402101 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 359 | 529 | 8.5e-24 |
HINCGGQDVKNGKILYEGDQDSGSNAAARCYNRSGSNWGFSSTGDFMDDENFYDNKYTLQSNSNISLVDFGLYATARKTPLSITYYGYCLETGNYTVRLH FAEIEFTYEKLYNKVARRVFYIYIQGIQVQKDFNFTKEAQGSNRSFTRAYNTTVTDRTLEIRLYWAGKGTT |
Full Sequence |
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Protein Sequence Length: 921 Download |
MFLACFKISE SFSLPVSCRQ IKNLFELLQP ILQHRMLMMF QLCQVMVMIS FSSSITLLAS 60 DQLHPGEVEA LRQIGKTVNE DGQLSLKFVD SCQQKGVVET ELNSAPPNLE GNSTIGCNCS 120 ITDDNYCHIT SFQLKDYSLP GRLPPELANL TCVQKIDFTR NYLYGTIPVE WASMKNLSFI 180 SLTANRLSGN IPGHLGSFTA ITYLSLESNH FWILSGNKLV GTLPEALAQI KDLKDFRVSD 240 NNLNGTVPEF IGNWTQLQKL ELYATGLQGP IPLAIFHLEK LSDLVLRNIN LTGTIPENAW 300 KVEKTLDVWY NNFSRSPRCS SSNENNINWF RSSSSNNKLR DLLPCSEISR CPKYYRSFHI 360 NCGGQDVKNG KILYEGDQDS GSNAAARCYN RSGSNWGFSS TGDFMDDENF YDNKYTLQSN 420 SNISLVDFGL YATARKTPLS ITYYGYCLET GNYTVRLHFA EIEFTYEKLY NKVARRVFYI 480 YIQGIQVQKD FNFTKEAQGS NRSFTRAYNT TVTDRTLEIR LYWAGKGTTV IPIRGNYGPI 540 ISAISVCSGY RTYCEEPEET SKKPIVIGVV TSAVFLIFLV MGVIYWKLCY GDKYTREREL 600 KGLDLKTGSF TLRQLKAATD NFNSENKIGE GGFGSVYKGE LADGTIIAVK QLSPKSRQGN 660 REFVNEIGII SCLQHPNLVR LYGCCIEGDQ LLLVYEYMEN NSLSRALFGA GSETSALMLD 720 WTTRYKICVG IARGLAFLHE GSAIRIVHRD IKGTNVLLDK DLNAKISDFG LAKLNEEENT 780 HISTRAHVLQ KKGNLMEIVD PKLQSEFNKE EAERMIKAAL LCTNASPSLR PAMSDMMSML 840 EGQTSIQEMI SDPSIYGDDL HSKHLKGHYE QVMDQSLNST QDLFPRSDKS WIGKSSTAHD 900 LYPINPESIS LNLSETSSLI * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 6.0e-37 | 627 | 774 | 154 | + Protein tyrosine kinase. | ||
smart00219 | TyrKc | 6.0e-38 | 625 | 778 | 160 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 4.0e-38 | 626 | 773 | 159 | + 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. | ||
smart00221 | STYKc | 3.0e-38 | 625 | 778 | 160 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
pfam11721 | Malectin | 1.0e-44 | 357 | 544 | 191 | + 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: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 |
RefSeq | XP_002317319.1 | 0 | 68 | 913 | 15 | 969 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317383.1 | 0 | 90 | 920 | 2 | 909 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332248.1 | 0 | 112 | 920 | 1 | 915 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332683.1 | 0 | 348 | 920 | 11 | 642 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002522278.1 | 0 | 39 | 919 | 1 | 963 | kinase, putative [Ricinus communis] |
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 | 610 | 842 | 20 | 308 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 610 | 842 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 610 | 842 | 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 | 610 | 842 | 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 | 610 | 842 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |