Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000228029 |
Family | CBM57 |
Protein Properties | Length: 1364 Molecular Weight: 150988 Isoelectric Point: 6.4843 |
Chromosome | Chromosome/Scaffold: 0378259 Start: 792 End: 12431 |
Description | receptor-like kinase in flowers 1 |
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 | 830 | 1000 | 5.1e-26 |
LHVNCGGNDITVEGNKGNILYEGDGGVEGGTADVFLNDASYWGFSSTGDFMDDNDFQNTRYSVSLASSNISGLYTTARISPLSITYFHYCLENGDYTVTL HFAEIQFTNDQTYTSLGRRIFDIYVQDEVLRKDFNIEEEAKVAQKPAIIQHNVGVTNNILEIRFYFAGKGT |
Full Sequence |
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Protein Sequence Length: 1364 Download |
MELYRKHTMN KDLGQDMQTR TFTLKQIKAA TNNFDSARKI GEGGFGPVYK GHLPNGSLIA 60 VKQLSSNSKQ GNREFLNEIG MITCLQHPNL VTLHGCCIER DQLLLVYEYM ENNSLAHALF 120 GPENQVKLDW PTRLKICTGI ARGLAFLHEE SRLKIVHRDI KATNVLLDGD LNPKISDFGL 180 AKLYGEESTH VSTKVAGTIG YMAPEYALWG HLTYMADVYS FGVVALEIAS GKKNSYVPSN 240 TCVCLLDWAY QLQQSGNLKE LIDVSLGSEV NYKEAEVLIK VGLLCTNVSP SLRPTMSEVV 300 SMLEGRTTVP DTKQEAINYT EDWRLKAVKD RHHQSQTQSS SGSQHESLGH TLKLESSPFY 360 HTTXALADPT TCPNSKVTSF PILKKISQAL LYSTILSQIF QRPGLSSHIF QRAGGQGISS 420 HIFNLLHHAA QEQQLLCSTV DALQEISKTM GANYWKFNGD SCXIESVGVT EEPPKGAESS 480 IGCECNNTVC HVTEIILLAV VELTFGRPCL IGARRGSVAG GIDVLSFPPN AKXGSGNNLD 540 VLDLNVSEVR VVCPYXYFRL KEGVLKGYSL PGMLPPQLVK LPYLKQIDFA LNYLNGTIPK 600 EWGAMQLTSI SLLVNRLSGE IPKELGNITT LTSLVLEANQ FSGVVPHELG SLINLGTMML 660 SSNRLTGNLP MTFSGLRNLT DFRINDNNFS GTIPDFIQNW KQLERLRISD INGTEQGFPV 720 LKSTTGLVRL VLRNCNISGE IPPYVWTMQN LEMLDVSFNK LVGQIPATLN LERLRFLFVT 780 GNSMSGSVPD SVFKDGSNID LSYNNFTWQG PEKPACQDNM SEYFSISTCL HVNCGGNDIT 840 VEGNKGNILY EGDGGVEGGT ADVFLNDASY WGFSSTGDFM DDNDFQNTRY SVSLASSNIS 900 GLYTTARISP LSITYFHYCL ENGDYTVTLH FAEIQFTNDQ TYTSLGRRIF DIYVQDEVLR 960 KDFNIEEEAK VAQKPAIIQH NVGVTNNILE IRFYFAGKGT TRIPDRGIYG PLISAISVES 1020 DSRDCSNGGK KRTAHIVTGV VVGAFLLVFI ILGILWWKGY LPCKRGRKKD RDGLDGQRGG 1080 FTLKQLKAAT NDFNYDNKIG EGGFGPVYKG QLPDGRVIAV KQLSSMSRQG NREFLNEMGM 1140 ISCLQHPNLV KLHGCCIEGG QLLLVYEYME NNNLARALFG RENHLRLDWA TRLKICIGIA 1200 RGLAFLHEES VLKIVHRDIK ATNVLLDEDL NPKISDFGLA KLDEEEKTHI STRVAGTIGY 1260 MAPEYALWGH LTYKADVYSF GVVALEIISG KNNNNYIPSD DWACHLQQTG NLLELIDEKL 1320 GSXVDQKEAE IMVKVALLCT NXSASLRPSM SEAVXMLEGQ IXRP |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00192 | PTKc | 7.0e-48 | 38 | 304 | 281 | + 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. | ||
smart00219 | TyrKc | 1.0e-49 | 38 | 303 | 279 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 1.0e-51 | 1097 | 1358 | 283 | + 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. | ||
smart00219 | TyrKc | 4.0e-52 | 1096 | 1357 | 269 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 5.0e-53 | 828 | 1016 | 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_002264679.1 | 0 | 438 | 1364 | 4 | 944 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002522276.1 | 0 | 6 | 347 | 1683 | 2028 | kinase, putative [Ricinus communis] |
RefSeq | XP_002522276.1 | 0 | 6 | 1364 | 625 | 1990 | kinase, putative [Ricinus communis] |
RefSeq | XP_002522276.1 | 0 | 565 | 1364 | 88 | 932 | kinase, putative [Ricinus communis] |
RefSeq | XP_002522276.1 | 0.001 | 718 | 813 | 76 | 171 | 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 | 18 | 305 | 16 | 308 | A Chain A, Crystal Structure Of Natural Cinnamomin (Isoform Iii) |
PDB | 3ulz_A | 0 | 1076 | 1359 | 15 | 308 | A Chain A, Crystal Structure Of Natural Cinnamomin (Isoform Iii) |
PDB | 3uim_A | 0 | 18 | 305 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3uim_A | 0 | 1076 | 1359 | 15 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 18 | 305 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |