Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.005G078400.1 |
Family | CBM57 |
Protein Properties | Length: 1035 Molecular Weight: 115005 Isoelectric Point: 6.2382 |
Chromosome | Chromosome/Scaffold: 05 Start: 16399037 End: 16412015 |
Description | Leucine-rich repeat transmembrane protein kinase |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 400 | 571 | 8.4e-30 |
HINCGGNQTTIGGITYDEDLYPAGPAVYKQTGKNWALSNTGHFMDNDSIPQGQFLPYTTENETRLYMTNAELYKNARVSPMSLTYYGFCLANGVYTVKLH FAEIMFTDDNTYSDLGRRVFDVYIQGERVLKDFNIANEAQGVRKELIKEFVAHVSGNDLEIRFYWAGKGTTY |
Full Sequence |
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Protein Sequence Length: 1035 Download |
MPTTMNTIIS SHFFLLSLLP ICFSCLAFGL TLPEYEVSVL KDIAKTLGKK DWDFHVDPCS 60 WTQSNDSMVF CNCKITNDSF CHVEKIALKS QSLQGILPPQ LNKLPYLQEI ELSRNYLCGS 120 IPREWGSSNL QKISLLGNRL TGPIPSELGN LTNLTRLILE FNQLSGNLPS ELGNLVHIEK 180 LHLSSNNFTG QLPANLSSLT AMKQFRISDN QLSGNIPDWL QNLTSLGQLH MQGSGLSGPI 240 PPGISDLNLT DLRISDLNGP DSTFPPLENM KSLDTLILRS CNINDTFPQY LADLSILKVL 300 DLSYNKLYGP VPRNLQQLIA SAANIYLAGN FFTGPVPEWT VDNNRSLDLS YNNFSVGNQE 360 PKTCNQQNVN LFASFSRNNL GPVSCDSSNR TCTKKVTSLH INCGGNQTTI GGITYDEDLY 420 PAGPAVYKQT GKNWALSNTG HFMDNDSIPQ GQFLPYTTEN ETRLYMTNAE LYKNARVSPM 480 SLTYYGFCLA NGVYTVKLHF AEIMFTDDNT YSDLGRRVFD VYIQGERVLK DFNIANEAQG 540 VRKELIKEFV AHVSGNDLEI RFYWAGKGTT YIPYKSVNGP LISALSVTYG GLSCGTKTKE 600 DSTGGHSVGL IVVIAVALVI VVILITVGVL RWRGFINCCY LDTCWHSVVE GLRSKPKFGR 660 HFGGNEHLLM KGLGDIELLT GVFTLHQIKV ATNNFDISNK IGEGGFGPVY KGILRNSKPI 720 AVKQLSSNSD QGTREFINEI GMISALQHPN LVKLYGCCAE GDQLLLVYEY MENNSLAHAL 780 FDSEDSHLKL NWPTRKNICL GIARGLAFLH EESRLKVVHR DLKTSNVLLD EDLNPKISDF 840 GLARLRVGDN THISTRIAGT WGYMAPEYAM HGYLTEKADV FSFGVVISEI VSGKRNTIRQ 900 SKGEAFYLLD WARLLNERGN IMELVDPKLN LDVNEDEVRL IVKVALLCTH VTSSYRPCMS 960 LVLSMLEGRT MVSEFDSHCS EVMDEMKLEV MREFYSQMDE NKTSDTRSLS LTKGVPWTDS 1020 SSTATDLNLV QLDP* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 3.0e-51 | 700 | 893 | 208 | + Protein tyrosine kinase. | ||
cd00192 | PTKc | 3.0e-52 | 699 | 892 | 207 | + 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 | 1.0e-53 | 697 | 960 | 275 | + 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 | 5.0e-54 | 697 | 960 | 275 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
pfam11721 | Malectin | 2.0e-54 | 397 | 585 | 193 | + 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 | CBI30748.1 | 0 | 23 | 1034 | 25 | 1013 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_175747.2 | 0 | 26 | 1026 | 21 | 952 | serine/threonine protein kinase-related [Arabidopsis thaliana] |
RefSeq | XP_002264109.1 | 0 | 22 | 1027 | 48 | 1025 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264180.1 | 0 | 31 | 1034 | 40 | 1002 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264642.1 | 0 | 22 | 1025 | 17 | 986 | 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 | 683 | 983 | 20 | 323 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3uim_A | 0 | 683 | 983 | 20 | 323 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 683 | 983 | 28 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 683 | 983 | 28 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 683 | 983 | 28 | 331 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |