| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01038011001 |
| Family | CBM57 |
| Protein Properties | Length: 1004 Molecular Weight: 110920 Isoelectric Point: 5.7404 |
| Chromosome | Chromosome/Scaffold: 10 Start: 12545889 End: 12562513 |
| Description | Leucine-rich repeat transmembrane protein kinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM57 | 411 | 577 | 9.3e-29 |
| SIKCGGQEVTTPDGMVYESDNSILGTASTSYYVSRSEKWAVSNVGLYVDRIANTSSLVNGTDTPELFKTSRISPGSLRYYGLGLKNGPYVVSLQFAEMLL KDPSTRTWESTGRRVFDIYIQGALKEKDFDISKEAGGVQRAIVKKFNTTVSKNYLEIHLLWAGKGTC | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1004 Download |
| MKLCSISFFL LLLFQKSLAK NATLDSSEVE ALNFLFNKWN MTSTEFWNMS GDPCSGPPIN 60 QSQYDDIYYR QAIKCNCTYN DNTTCHITHL KVLNLNKTGL IPEELTALTF LSDLRLNKNY 120 FTGPLPLFIA NLSQMQFIDV GHNALSGTIP KELGNLKELQ MLAIGSNNFS GTLPPELGNL 180 PKLELIFIDS SGVGGEIPST FVKLKNMREM FLSDTPLTGK IPDFIGNWTK LKRLRIQGNS 240 FEGPIPSTFS QLISMESLRI SDLANVSSSL DFIKDMKNLT DLVLRNALLS GGIPSDIEEY 300 RSLETLDLSF NNLTGGIPNA LFNMNNLTAL FLGNNSFYGS LPDKKSDKLQ TIDLSYNEIS 360 GGFPTWIDPT LQLNLVANNF VFDNTNNSIF EGLNCLQRNF PCNTPRYTNV SIKCGGQEVT 420 TPDGMVYESD NSILGTASTS YYVSRSEKWA VSNVGLYVDR IANTSSLVNG TDTPELFKTS 480 RISPGSLRYY GLGLKNGPYV VSLQFAEMLL KDPSTRTWES TGRRVFDIYI QGALKEKDFD 540 ISKEAGGVQR AIVKKFNTTV SKNYLEIHLL WAGKGTCCIP FEGYYGPSIS ALSVVSALER 600 MPPPPSETSN TGLIAGIAVT AGILCFILVC AVFYIKRRGS NSNEEIELLE IGPISNTFSY 660 AELRTATENF NPTNKLGEGG FGAVFKGTLL DGRVVAVKDL MVASQQGKSQ FIAEIATISA 720 VQHRNLVKLH GFCIKENKRL LVYEYLENKS LDRALFGKSD LHLDWPTRFN ICLGTARGLA 780 YLHEESRARI VHRDVKASNI LLDAELCPKI SDFGLAKLYD DKKTHISTRV AGTIGYLAPE 840 YAMRGHLTEK ADVFGFGVVA LEILSGRPNS DNSLDARKMY LLEWAWTLHE NNQSMDLVDP 900 TLTEFDENEV SRVVRVALLC TQGSPMLRPA MSRVVAMLAG GVEISAVTSK PSYLTDWDFN 960 DITSSFLSEN TRTSTASTSM TDQLPSPIYH TEPMLLGVIG EGR* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00069 | Pkinase | 4.0e-43 | 675 | 905 | 237 | + Protein kinase domain. | ||
| cd00180 | PKc | 1.0e-45 | 676 | 863 | 192 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
| smart00221 | STYKc | 6.0e-47 | 675 | 865 | 197 | + 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 | 7.0e-48 | 675 | 865 | 197 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
| pfam11721 | Malectin | 7.0e-57 | 408 | 592 | 187 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI20535.1 | 0 | 1 | 995 | 5 | 993 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI20543.1 | 0 | 90 | 995 | 4 | 908 | unnamed protein product [Vitis vinifera] |
| EMBL | CBI39037.1 | 0 | 1 | 1003 | 1 | 1003 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002271607.1 | 0 | 29 | 995 | 9 | 950 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ulz_A | 0 | 658 | 940 | 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 | 658 | 940 | 20 | 308 | A Chain A, Structural Basis For The Impact Of Phosphorylation On Plant Receptor- Like Kinase Bak1 Activation |
| PDB | 3tl8_H | 0 | 658 | 940 | 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 | 658 | 940 | 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 | 658 | 940 | 28 | 316 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
