| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01029720001 |
| Family | CBM57 |
| Protein Properties | Length: 2194 Molecular Weight: 240793 Isoelectric Point: 4.9366 |
| Chromosome | Chromosome/Scaffold: 12 Start: 13721467 End: 13758979 |
| 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 | 1580 | 1749 | 5.6e-30 |
| FAIKCGGPQITSSDQIVFERDSETLGPATYYVTDTNRWAFSNVGKFSGSNNYTSTSSSLFTNTLDSELFQTARISAGSLRYYGLGLKNGNYTLTLQFAET AIVNSNSWKTLGRRVFDIYIQGDLILKDFDIRKEAGGVSFQAVKKEFTAQVLENYIEIHLFWAGKGTCCV | |||
| CBM57 | 503 | 674 | 2.9e-31 |
| FAIKCGGPQITSSDQIVFERDNETLGPATYYVTDENRWAVSNVGLFSGSNNPQYTSTSSSQFTNTLDSELFQTARISAGSLRYYGLGLENGNYTLTLQFA ETAIVNSNSWKSLGRRVFDVYIQGDLVLKDFDIRKEAGGVSFQAVKKEFTAQVLENYIEIHLFWAGKGTCCV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 2194 Download |
| MIGLDIFDWA ISIGTQKKKI KDRSPQIVHW AFISNECARG LIFRLMRKRP QCVRSVTKSQ 60 KTTTEEKRER TTMDSVSWVF VALYGVYVIG LFHAAAAQST EANATTDPSE VTILNSIFQQ 120 WGISASNEWN TSGEPCTGAA LDSADIKNPG IKCDCSYDNA STCHITQLKV YALDVVGAIP 180 DELWNLTFLT NLNLGQNYLT GSLSASIGNL TSMQYLSLGI NALSGELPKE LGQLTDLRSI 240 AFGTNNFSGS LPSELGNLVK LEQLICCYCL TNQCYFDSSG LSGDIPSTFA NLQSLTTVWA 300 SDNELTGNIP DFIGNWSKLT VLRLQGNSFE GSIPSSFSNL TSLTDLRISD ISNGSSSSLE 360 FIKDMKSLST LIIRNNNISD AIPSNIGEYG SLTQLDLSFN NLSGQLPESL FNLSQLTYLF 420 LGNNQLTGSL PSQKSTSLLN IDLSYNGLSG SFPSWVDEEN LQLNLVANNF TLDSSNSSVL 480 PSGLNCLQQN FPCNRGSGIY YNFAIKCGGP QITSSDQIVF ERDNETLGPA TYYVTDENRW 540 AVSNVGLFSG SNNPQYTSTS SSQFTNTLDS ELFQTARISA GSLRYYGLGL ENGNYTLTLQ 600 FAETAIVNSN SWKSLGRRVF DVYIQGDLVL KDFDIRKEAG GVSFQAVKKE FTAQVLENYI 660 EIHLFWAGKG TCCVPAQGTY GPSISAISAT PDFEPTVSNT APNGKKNRTG LIVGIAVGLG 720 VVCFLSVFAL YYFVLRRKKP SENQDEELLG MDARPYTFSY AELKNATGDF SPSNKLGEGG 780 FGPVYKGTLS DGRVVAVKQL SVASHQGKKQ FVAEIATISA VQHRNLVKLY GCCIEGVNRS 840 LVYEYLENKS LDQALFGKGN GSLDLDWPTR YDICLGVARG LAYLHEESRV RIVHRDVKAS 900 NILLDYHRNP KISDFGLAKL YDDTKTHIST RVAGTIGYLA PEYAMRGHLT EKADVFGFGV 960 VALEIVSGRP NSDTSLEEEK TYLLEWAWQL HENNHEIELV DSRLSEFSEE EARRMIGVAL 1020 LCTQTSPTLR PPMSRAVAML SGDIEVSRVT TKPGYLTDWK FNDASSFMSE NSHFNSSTSI 1080 SMAADADLAK NAPYIQFIGV MKVNFALWLF ELLSRHCMAF SALVNLVKKY QWEIRLGQTR 1140 NELVKLNVSF GYVIGIQSVS CVFVALCSVY VTGLFHIAAA QTTEANATTD PSEVRVLNSI 1200 FRQWGISASS QWRTIGEPCT GAAIDSTSID SADYNFGIKC DCSYDNASTC HITQLKVYAL 1260 DVVGVIPDEL WNLTFLTSLN LGQNYLTGPL SASIGNLTSM QYLSLGINAL SGELPKELGQ 1320 LTDLRSFAFG TNNFSGSLPS EIGNLVKLEQ LYFDSSGVSG EIPSTFANLQ SLTIVWASDN 1380 ELTGNIPDFI GNWSKLTVLR LQGNSFEGPI PSSFSNLTSL TDLRVSDISN ASSSSLEFIK 1440 NMKLLSTLVL RNNNISDSIP SNIGEYGSLT QLDLSFNNLS GQLPESLFNL SQLTYLFLGN 1500 NQLTGTLPSL KSTSLLNIDL SYNGLSGSFP SWVDEENLQL NLVANNFTLD SSNSSVLPSG 1560 LNCLQQNFPC NRGSGIYYNF AIKCGGPQIT SSDQIVFERD SETLGPATYY VTDTNRWAFS 1620 NVGKFSGSNN YTSTSSSLFT NTLDSELFQT ARISAGSLRY YGLGLKNGNY TLTLQFAETA 1680 IVNSNSWKTL GRRVFDIYIQ GDLILKDFDI RKEAGGVSFQ AVKKEFTAQV LENYIEIHLF 1740 WAGKGTCCVP AQGTYGPSIS AISATPNFEP TVPNTAPNGK KHRTGLIVGI AVALGLVCFL 1800 AVFSVYYFVL RRKKPYENQD EELLGMEARP YTFSYAELKN ATGDFSPSNK LGEGGFGPVY 1860 KGTLSDGRVV AVKQLSVSSH QGKNQFVTEI KTISAVQHRN LVKLYGCCIE GVNRSLVYEY 1920 LENKSLDQAL FGEGNLDLVW QTRYDICLGV ARGLAYLHEE SRLRIVHRDV KASNILLDYY 1980 LNPKISDFGL AKLYDDTKTH ISTRVAGTIG YLAPEYAMRG HLTEKADVFG FGVVALEIVS 2040 GRPNSDTSLE EEKTYLLEWH TYRLWKLDLS ILAWQLHETN CELELVDSGL SEFSEEEATR 2100 MIGVALLCTQ TSPTLRPPMS HVVAMLSGDI EVSRVTTKPG YLTDWKFNDA SSFMSENSDL 2160 SSPSISMAVD TDCSALTVNK TESMRLLERA GEE* 2220 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| smart00221 | STYKc | 3.0e-46 | 775 | 983 | 217 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
| cd00180 | PKc | 5.0e-47 | 776 | 965 | 194 | + 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. | ||
| cd00180 | PKc | 1.0e-47 | 1851 | 2038 | 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. | ||
| pfam11721 | Malectin | 7.0e-58 | 1578 | 1762 | 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. | ||
| pfam11721 | Malectin | 2.0e-63 | 501 | 687 | 189 | + 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 |
| GenBank | AAG50909.1 | 0 | 90 | 2152 | 3 | 2016 | AC069159_10 receptor protein kinase, putative [Arabidopsis thaliana] |
| GenBank | AAG50909.1 | 0 | 1171 | 2174 | 1 | 987 | AC069159_10 receptor protein kinase, putative [Arabidopsis thaliana] |
| EMBL | CBI20016.1 | 0 | 1 | 2193 | 1 | 2193 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002267672.1 | 0 | 98 | 1087 | 32 | 1009 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002267672.1 | 0 | 1155 | 2187 | 6 | 1024 | 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 | 3tl8_H | 0 | 736 | 1043 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_H | 0 | 1811 | 2129 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 736 | 1043 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_G | 0 | 1811 | 2129 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
| PDB | 3tl8_D | 0 | 736 | 1043 | 1 | 317 | B Chain B, The Avrptob-Bak1 Complex Reveals Two Structurally Similar Kinaseinteracting Domains In A Single Type Iii Effector |
