Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.002G048800.1 |
Family | CBM57 |
Protein Properties | Length: 1005 Molecular Weight: 109986 Isoelectric Point: 6.4609 |
Chromosome | Chromosome/Scaffold: 02 Start: 4145459 End: 4152704 |
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 | 400 | 563 | 6.2e-27 |
YINCGGKVETVDNITYESDVYDDKLSTFHRSTYWAFSGTGIFLDDSITKGSLVRENKQVASSVGPLYINARLSYSSLTYYAFCLNNATYNVSLHFAEIDF TDGKNYSSLGRRIFDVYIQGKRELKDFNIKDKAGGVGKPILKNFTANVSDGTLEIRLQWAGKGT |
Full Sequence |
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Protein Sequence Length: 1005 Download |
MLFLPLLVFA SIFSACCLAT STLGTTLAKD EVEALESIGR TLGKTWKFSV DPCGSGDESW 60 AKFAEKDAYY VNNVTCDCRS SPCHIVRIVL KGQNLPGTLP PQLTRLPYLQ EIDLSRNYLS 120 GSIPPQWGSM KQLVKISLLG NRLTGSIPEE LANMSNLTSL VLEHNNFSGK LPAALGNLPK 180 IERLFLNSNN FIGELPETFA RLTTLKEFRI GDNNFTGKIP GFIFQNWTNL TDIYMIASGL 240 SGPIPDIVSS GNLKNIIISD LNGAESQISQ LSNLSNLEIL ILRSCNLIGE LPTSLNHMSS 300 LKTLDFSFNG LSGEISISLP RAKHLILAGN MFTGAVPQWI LDTNQIIDLS YNNFTSTGGV 360 DDCQKSGLNL FASTSRINNS GAVSCLGNLN CPSEPSHYLY INCGGKVETV DNITYESDVY 420 DDKLSTFHRS TYWAFSGTGI FLDDSITKGS LVRENKQVAS SVGPLYINAR LSYSSLTYYA 480 FCLNNATYNV SLHFAEIDFT DGKNYSSLGR RIFDVYIQGK RELKDFNIKD KAGGVGKPIL 540 KNFTANVSDG TLEIRLQWAG KGTTSIPERG VFGPLISAIS IFDPAYKPRK GSGGGISAAA 600 EVGIVAAAIF ATFLIVGGIL WWSGCLRRRS TLERDLKGIE LQTSCFTLRQ IKDATNNFDA 660 ANKIGEGGFG PVYKGILADG TEIAVKQLSA RSKQGNREFV TEIGMISALQ HPHLVKLYGC 720 CIEGNQLLLI YEYLENNSLA RALFGPEEFQ LTLDWPTRRK ICIGIARGLA YLHEESRLKI 780 VHRDIKVTNV LLDKDLNPKI SDFGLAKLDE EDNTHISTRI AGTYGYMAPE YAMHGRLTDK 840 ADVYSFGIVA LEIVSGTCNT KHSRVKEESF YLLDLANTLK QKGNLLDLID PRVASHCDPE 900 GAILMIDVAL LCTNSTAAAR PSMSTVVSIL EGKASFSNII TNSSIYGSEL NPKNLYENVE 960 EKDVENNSLT KRMLGDGQWT SSSDLYPVSL TSSYWQNSSS TSKN* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam07714 | Pkinase_Tyr | 7.0e-49 | 663 | 930 | 284 | + Protein tyrosine kinase. | ||
pfam11721 | Malectin | 2.0e-50 | 397 | 579 | 188 | + 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. | ||
smart00221 | STYKc | 9.0e-52 | 663 | 930 | 278 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00192 | PTKc | 5.0e-52 | 662 | 931 | 292 | + 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 | 3.0e-52 | 663 | 930 | 276 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. |
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 | CBI20124.1 | 0 | 32 | 996 | 62 | 1033 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283578.1 | 0 | 24 | 996 | 25 | 981 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283596.1 | 0 | 31 | 996 | 64 | 1033 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002524511.1 | 0 | 27 | 997 | 27 | 983 | ATP binding protein, putative [Ricinus communis] |
RefSeq | XP_002524514.1 | 0 | 2 | 997 | 1 | 1005 | ATP binding protein, 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 | 642 | 932 | 16 | 308 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3uim_A | 0 | 642 | 932 | 16 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
PDB | 3tl8_H | 0 | 642 | 932 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_G | 0 | 642 | 932 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
PDB | 3tl8_D | 0 | 642 | 932 | 24 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |